{"id":69,"date":"2024-03-10T12:50:33","date_gmt":"2024-03-10T12:50:33","guid":{"rendered":"https:\/\/glocentrica.usquaresolutions.com\/?page_id=69"},"modified":"2025-12-31T10:49:40","modified_gmt":"2025-12-31T10:49:40","slug":"publications","status":"publish","type":"page","link":"https:\/\/pjthornalley.com\/index.php\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<h1 class=\"wp-block-heading\"><strong>Peer-reviewed articles in journals and chapters in books<\/strong><\/h1>\n\n\n\n<ol class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hill, H.A.O. and Thornalley, P.J. (1981) Phenyl radical production during the oxidation of phenylhydrazine and phenylhydrazine-induced haemolysis.&nbsp; FEBS Lett. <strong>125<\/strong>, 235-238.<\/li>\n<\/ol>\n\n\n\n<ol start=\"2\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hill, H.A.O. and Thornalley, P.J. (1982) Free radical production during phenylhydrazine-induced haemolysis. Can. J. Chem. <strong>66<\/strong>, 1528-1531.<\/li>\n<\/ol>\n\n\n\n<ol start=\"3\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V. and Bannister, W.H., Hill, H.A.O. and Thornalley, P.J. (1982). Enhanced production of hydroxyl radical by the xanthine\/xanthine oxidase reaction in the presence of lactoferrin. Biochim. Biophys. Acta <strong>715<\/strong>, 116-120.<\/li>\n<\/ol>\n\n\n\n<ol start=\"4\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Esnouf, M.P., Gainey, A.I., Hill, H.A.O. and Thornalley, P.J. (1982) The carboxylation of preprothrombin. Proc. Intern. Symp. on Metal Ions in Biological Processes, Little Rock, Arkansas, July 1981, Humana Press Inc., New York, pp. 209-220.<\/li>\n<\/ol>\n\n\n\n<ol start=\"5\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hill, H.A.O. and Thornalley, P.J. (1982) The oxidative ring-opening of the nitrone spin trap 5,5-dimethyl-1-pyrroline-N-oxide (DMPO): free radical involvement. Inorg. Chim. Acta <strong>67<\/strong>, L35-L36.<\/li>\n<\/ol>\n\n\n\n<ol start=\"6\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Sarchet, A.W., Hill, H.A.O. and Bannister, J.V. (1982) The inhibition of manganese superoxide dismutase by cacodylate buffer. Inorg. Chim. Acta <strong>67<\/strong>, 75-78.<\/li>\n<\/ol>\n\n\n\n<ol start=\"7\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Saez, G., Thornalley, P.J., Hill, H.A.O., Hems, R. and Bannister, J.V. (1982) The production of free radicals by the autoxidation of cysteine and their effect on isolated hepatocytes. Biochim. Biophys. Acta <strong>719<\/strong>, 24-31.<\/li>\n<\/ol>\n\n\n\n<ol start=\"8\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Bannister, W.H., Hill, H.A.O. and Thornalley, P.J. (1982) Some current aspects of oxygen-free radicals in biological systems. Life Chem. Reports <strong>1<\/strong>, 1-8.<\/li>\n<\/ol>\n\n\n\n<ol start=\"9\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Thornalley, P.J. and Bannister, W.H. (1982) Oxygen radicals in phagocytosis and cytotoxicity, Proc. 28th Nat. Symp. Italian Biochem. Soc., Firenze, September 1982, pp 116-119.<\/li>\n<\/ol>\n\n\n\n<ol start=\"10\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Bellavite, P., Serra, M.C., Thornalley, P.J. and Rossi, F. (1982) An EPR study of the production of superoxide radicals by the neutrophil NADPH oxidase. FEBS Lett. <strong>145<\/strong>, 323-326.<\/li>\n<\/ol>\n\n\n\n<ol start=\"11\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Bellavite, P., Davoli, A., Thornalley, P.J. and Rossi, F. (1982) Production of hydroxyl radicals from neutrophilic NADPH oxidase catalysed by transferrin. FEBS Lett. <strong>150<\/strong>, 300-302.<\/li>\n<\/ol>\n\n\n\n<ol start=\"12\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hill, H.A.O. and Thornalley, P.J. (1983) The effect of spin traps on phenylhydrazine-induced haemolysis. Biochim. Biophys. Acta <strong>762<\/strong>, 44-51.<\/li>\n<\/ol>\n\n\n\n<ol start=\"13\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Bannister, W.H., Searle, A.J.F. and Thornalley, P.J. (1983) The reaction of superoxide radicals with metal picolinate complexes. Inorg. Chim. Acta <strong>78<\/strong>, 139-142.<\/li>\n<\/ol>\n\n\n\n<ol start=\"14\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Bannister, J.V. (1983) The production of hydroxyl radicals from adriamycin-treated red blood cells. FEBS Lett. <strong>157<\/strong>, 170-172.<\/li>\n<\/ol>\n\n\n\n<ol start=\"15\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Stern, A. and Bannister, J.V. (1983) A mechanism for the oxidation of NADPH induced by primaquine in red blood cells. Biochem. Pharmacol. <strong>32<\/strong>, 3571-3575.<\/li>\n<\/ol>\n\n\n\n<ol start=\"16\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Davis, G. and Thornalley, P.J. (1983) Free radical involvement in the autoxidation of reduced pyridine nucleotides catalysed by phenazine derivatives. Biochim. Biophys. Acta <strong>724<\/strong>, 456-464.<\/li>\n<\/ol>\n\n\n\n<ol start=\"17\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hume, D.A., Gordon, S., Thornalley, P.J. and Bannister, J.V. (1983) The production of oxygen-centred free radicals by Bacillus-Calmette-Guerin- activated macrophages. An electron paramagnetic resonance study of the response to phorbol myristate acetate. Biochim. Biophys. Acta <strong>763<\/strong>, 245-250.<\/li>\n<\/ol>\n\n\n\n<ol start=\"18\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Trotta, R.J. and Stern, A. (1983) The involvement of free radicals in the oxidative phenomena induced by tert-butyl hydroperoxide in red cells. Biochim. Biophys. Acta <strong>759<\/strong>, 16-22.<\/li>\n<\/ol>\n\n\n\n<ol start=\"19\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Trotta, R.J. and Stern, A. (1984) Free radical production from the reaction of tert-butyl hydroperoxide with haemoglobin and iron complexes. In: Oxygen Radicals in Chemistry and Biology. (W. Bors, M. Saran and D. Taits, eds.) Walter de Gruyter &amp; Co., Berlin, pp 215-218.<\/li>\n<\/ol>\n\n\n\n<ol start=\"20\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Wolff, S., Crabbe, J. and Thornalley, P.J. (1984) The autoxidation of \u03b1-hydroxyketones. Experientia <strong>40<\/strong>, 244-246.<\/li>\n<\/ol>\n\n\n\n<ol start=\"21\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Wolff, S., Crabbe, J. and Stern, A. (1984) The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions, catalysed by buffer ions. Biochim. Biophys. Acta <strong>797<\/strong>, 276-287.<\/li>\n<\/ol>\n\n\n\n<ol start=\"22\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Wolff, S., Crabbe, J. and Stern, A. (1984) The oxidation of oxyhaemoglobin by glyceraldehyde and other simple monosaccharides under physiological conditions. Biochem. J. <strong>217<\/strong>, 615-622.<\/li>\n<\/ol>\n\n\n\n<ol start=\"23\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Vasak, M. (1985) Possible role of metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim. Biophys. Acta <strong>827<\/strong>, 36-44.<\/li>\n<\/ol>\n\n\n\n<ol start=\"24\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., D&#8217;Arcy Doherty, M., Smith, M.T., Bannister, J.V. and Cohen, G. (1984) Superoxide and hydroxyl radical formation by rat liver microsomal metabolism of 1-naphthol. Chem.-Biol. Interact. <strong>48<\/strong>, 195-206.<\/li>\n<\/ol>\n\n\n\n<ol start=\"25\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bannister, J.V., Bannister, W.H. and Thornalley, P.J. (1984) Effect of ferritin iron loading on the production of hydroxyl radicals. In: Oxidative Damage and Related Enzymes. (G. Rotilio and J.V. Bannister, eds.) Harwood Academic Publishers, New York, pp 64-72.<\/li>\n<\/ol>\n\n\n\n<ol start=\"26\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Bannister, J.V. (1985) The spin trapping of superoxide. Handbook of Methods for Oxygen Radical Research (R.A. Greenwald, ed.), CRC Press, Boca Raton, USA, pp 133-136.<\/li>\n<\/ol>\n\n\n\n<ol start=\"27\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Stern, A. (1984) The effect of glyceraldehyde on red cells. Haemoglobin status, oxidative metabolism and glycolysis. Biochim. Biophys. Acta <strong>804<\/strong>, 308-323.<\/li>\n<\/ol>\n\n\n\n<ol start=\"28\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Stern, A. (1984) Oxidative metabolism in hydroxypyruvaldehyde-treated red cells. Biochem. Pharmacol. <strong>34<\/strong>, 1157-1164.<\/li>\n<\/ol>\n\n\n\n<ol start=\"29\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Stern, A. (1984) Free radical production from the autoxidation of monosaccharides catalysed by buffer ions. Carbohydr. Res. <strong>143<\/strong>, 191-204.<\/li>\n<\/ol>\n\n\n\n<ol start=\"30\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1985) Monosaccharide Autoxidation. In: Health and Disease. Environmental Health Perspectives (R.P. Mason, ed.) <strong>64<\/strong>, 297-307.<\/li>\n<\/ol>\n\n\n\n<ol start=\"31\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1984) The haemolytic reactions of hydrazine and 1-acetyl-2-phenylhydrazine: a spin trapping study. Chem.-Biol. Interact. <strong>797<\/strong>, 276-287.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"32\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Stern, A. (1984) The mechanism of stimulation of oxidative metabolism in the red cell by 1,4-naphthoquinone-2-potassium sulphonate. Chem.-Biol. Interact. <strong>56<\/strong>, 55-71.<\/li>\n<\/ol>\n\n\n\n<ol start=\"33\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Dodd, N.J.F. (1984) Free radical production from normal and adriamycin-treated rat heart sarcosomes. Biochem. Pharmacol. <strong>34<\/strong>, 669-674.<\/li>\n<\/ol>\n\n\n\n<ol start=\"34\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1986) The theory and biological applications of the electron spin resonance technique of spin trapping. Invited review. Life Chem. Reports <strong>4<\/strong>, 57-112.<\/li>\n<\/ol>\n\n\n\n<ol start=\"35\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Stern, A. (1985) The effect of nitrone spin trapping agents on red blood cell metabolism. Free Radical Res. Commun. <strong>1<\/strong>, 111-117.<\/li>\n<\/ol>\n\n\n\n<ol start=\"36\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1986) Monosaccharide autoxidation: a prospective role in disease processes. In: Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine. (G. Rotilio, ed.) Elsevier, Amsterdam, pp 481-483.<\/li>\n<\/ol>\n\n\n\n<ol start=\"37\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Bannister, W.H. and Bannister, J.V. (1986) Reduction of oxygen by NADH\/NADH dehydrogenase in the presence of adriamycin. Free Radical Res. Commun. <strong>2<\/strong>, 163-171.<\/li>\n<\/ol>\n\n\n\n<ol start=\"38\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Jones, A.F., Winkles, J.W., Thornalley, P.J., Lunec, J., Jennings, P.E. and Barnett, A.H. (1987) The inhibitory effect of superoxide dismutase on the fructosamine assay. Clin. Chem. <strong>33<\/strong>, 147-149.<\/li>\n<\/ol>\n\n\n\n<ol start=\"39\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Della Bianca, V., Bellavite, P. and Rossi, F. (1987) S-D-lactoylglutathione in resting and activated human neutrophils. Biochem. Biophys. Res. Commun. <strong>145<\/strong>, 769-774.<\/li>\n<\/ol>\n\n\n\n<ol start=\"40\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Bellavite, P. (1987) Modification of the glyoxalase system in human neutrophils during functional activation. Biochim. Biophys. Acta <strong>931<\/strong>, 120-129.<\/li>\n<\/ol>\n\n\n\n<ol start=\"41\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hooper, N.I., Thornalley, P.J., Jones, A.F., Lunec, J., Florkowski, C. and Barnett, A.H. (1987) The glyoxalase system during hyperglycaemia <em>in vitro<\/em> and in diabetic patients <em>in vivo<\/em>. Clinical Science <strong>74<\/strong>, Suppl. 18, pp 73-74.<\/li>\n<\/ol>\n\n\n\n<ol start=\"42\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hooper, N.I., Tisdale, M.J. and Thornalley, P.J. (1987) Glyoxalase activity during differentiation of human leukaemic cells <em>in vitro<\/em>. Leukaemia Research <strong>11<\/strong>, 1141-1148.<\/li>\n<\/ol>\n\n\n\n<ol start=\"43\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hooper, N.I., Tisdale, M.J. and Thornalley, P.J. (1988) Modification of the glyoxalase system in human HL60 promyelocytic leukaemia cells during differentiation to neutrophils <em>in vitro<\/em>. Biochim. Biophys. Acta <strong>966<\/strong>, 362-369.<\/li>\n<\/ol>\n\n\n\n<ol start=\"44\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hooper, N.I., Tisdale, M.J. and Thornalley, P.J. (1988) Glyoxalase activity and cell proliferation in Burkitt&#8217;s lymphoma Raji (+) cells and transformed lymphoblastoid GM892 cells <em>in vitro<\/em>. Cell. Molec. Biol. <strong>34<\/strong>, 399-405.<\/li>\n<\/ol>\n\n\n\n<ol start=\"45\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1988) Modification of the red blood cell glyoxalase system by glucose <em>in vitro<\/em>. Biochem. J. <strong>254<\/strong>, 751-755.<\/li>\n<\/ol>\n\n\n\n<ol start=\"46\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Tisdale, M.J. (1988) Inhibition of growth of human promyelocytic leukaemia 60 cells by S-D-lactoylglutathione. Leukaemia Res. <strong>12<\/strong>, 897-904.<\/li>\n<\/ol>\n\n\n\n<ol start=\"47\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Atkins, T.W. and Thornalley, P.J. (1989) Glyoxalase activity in tissues of lean (HO) and genetically obese diabetic (ob\/ob) mice. Med. Sci. Res. <strong>17<\/strong>, 777-778.<\/li>\n<\/ol>\n\n\n\n<ol start=\"48\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Hooper, N.I., Florkowski, C., Jones, A.P., Lunec, J. and Barnett, A.H. (1989) Modification of the human red blood cell glyoxalase system in diabetes mellitus. Diabetes Res. &amp; Clin. Pract. <strong>7<\/strong>, 115-120.<\/li>\n<\/ol>\n\n\n\n<ol start=\"49\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A. and Thornalley, P.J. (1989) Glyoxalase activities in age-fractioned human red blood cells. Mechanism of Ageing and Development <strong>48<\/strong>, 63-71.<\/li>\n<\/ol>\n\n\n\n<ol start=\"50\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Atkins, T.W. and Thornalley, P.J. (1989) Erythrocyte glyoxalase activity in genetically obese (ob\/ob) and streptozotocin-induced diabetic mice. Diabetes Res. <strong>11<\/strong>, 125-129.<\/li>\n<\/ol>\n\n\n\n<ol start=\"51\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1990) The glyoxalase system. New developments towards functional characterisation of a metabolic pathway fundamental to biological life. Biochem. J. <strong>269<\/strong>, 1-11.<\/li>\n<\/ol>\n\n\n\n<ol start=\"52\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1990) The glyoxalase system: towards functional characterisation and a role in disease processes. CRC Handbook on Glutathione Metabolism, (J. Vi\u00f1a, ed.), CRC Press, Boca Raton, USA, 135-144.<\/li>\n<\/ol>\n\n\n\n<ol start=\"53\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Clelland, J.D. and Thornalley, P.J. (1990) Synthesis of <sup>14<\/sup>C-labelled methylglyoxal and S-D-lactoylglutathione. J. Labelled Compounds and Radiopharmaceuticals <strong>28<\/strong>, 1454-1464.<\/li>\n<\/ol>\n\n\n\n<ol start=\"54\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Greskowiak, M. and Della Bianca, V. (1990) Potentiation of secretion from neutrophils by S-D-lactoylglutathione. Med. Sci. Res. <strong>18<\/strong>, 813-815.<\/li>\n<\/ol>\n\n\n\n<ol start=\"55\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1991) Esterification of reduced glutathione. Biochem. J. <strong>275<\/strong>, 535-539.<\/li>\n<\/ol>\n\n\n\n<ol start=\"56\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1991) Population genetics of human glyoxalases. Heredity <strong>67<\/strong>, 139-142.<\/li>\n<\/ol>\n\n\n\n<ol start=\"57\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Clelland, J.D. and Thornalley, P.J. (1991) S-2-Hydroxyacylglutathione derivatives. Enzymatic preparation, purification and characterisation. J. Chem. Soc. Perkin Trans. I, 3009-3015.<\/li>\n<\/ol>\n\n\n\n<ol start=\"58\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Smith, P. and Thornalley, P.J. (1992) Preparation and purification of N<sub>e<\/sub>-(1-deoxyfructosyl)hippuryllysine, Carbohydr. Res. <strong>223<\/strong>, 293-298.<\/li>\n<\/ol>\n\n\n\n<ol start=\"59\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C. and Thornalley, P.J. (1992) Optimisation of non-denaturing polyacrylamide gel electrophoresis analysis of glyoxalase I phenotypes in clinical blood samples. Clin. Chim. Acta <strong>204<\/strong>, 137-144.<\/li>\n<\/ol>\n\n\n\n<ol start=\"60\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Phillips, S.A. and Thornalley, P.J. (1992) Glyoxalase activity in the lens. Med. Sci. Res. <strong>20<\/strong>, 91-92.<\/li>\n\n\n\n<li class=\"has-medium-font-size\">Lo, T. and Thornalley, P.J. (1992) \u03b3-L-Glutamyl-O-acyl-L-serylglycine derivatives: synthesis, purification and evaluation as inhibitors of glyoxalases. J. Chem. Soc., Perkin Trans. I, 639-643.<\/li>\n<\/ol>\n\n\n\n<ol start=\"62\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C. and Thornalley, P.J. (1992) Sample storage conditions for the assay of glyoxalase activities in whole blood samples. Ann. Clin. Biochem. <strong>29<\/strong>, 222-223.<\/li>\n<\/ol>\n\n\n\n<ol start=\"63\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C. and Thornalley, P.J. (1992) Electrophoretic analysis of glyoxalase II in clinical blood samples. J. Clin. Chem. and Clin. Biochem. <strong>30<\/strong>, 7-10.<\/li>\n<\/ol>\n\n\n\n<ol start=\"64\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C. and Thornalley, P.J. (1992) Synthesis and chromatography of 1,2-diamino-4,5-dimethoxybenzene, 6,7-dimethoxy-2-methylquinoxaline and 6,7-dimethoxy-2,3-dimethylquinoxaline for use in a liquid chromatographic fluorimetric assay of methylglyoxal. Anal. Chim. Acta <strong>263<\/strong>, 137-142.<\/li>\n<\/ol>\n\n\n\n<ol start=\"65\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1992) Human Glyoxalase I. Human Protein Data (A. Haeberli, ed.), VCH Verlagsges. mbH, Weinheim.<\/li>\n<\/ol>\n\n\n\n<ol start=\"66\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1992) Human Glyoxalase II. Human Protein Data (A. Haeberli, ed.), VCH Verlagsges. mbH, Weinheim.<\/li>\n<\/ol>\n\n\n\n<ol start=\"67\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C., Phillips, S.A. and Thornalley, P.J. (1992) The assay of methylglyoxal in biological systems by derivatisation with 1,2-diamino-4,5-dimethoxybenzene. Anal. Biochem. <strong>206<\/strong>, 17-23.<\/li>\n<\/ol>\n\n\n\n<ol start=\"68\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Smith, P.R. and Thornalley, P.J. (1992) Influence of pH and phosphate ions on the kinetics of enolisation and degradation of fructosamines.&nbsp; Studies with the mode fructosamine, N<sub>\u03b5<\/sub>-(1-deoxy-D-fructos-1-yl)hippuryl-lysine. Biochem. Internat. <strong>28<\/strong>, 429-439.<\/li>\n<\/ol>\n\n\n\n<ol start=\"69\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C., Phillips, S.A. and Thornalley, P.J. (1992) Fluorimetric assay of D-lactate. Anal. Biochem. <strong>206<\/strong>, 12-16.<\/li>\n<\/ol>\n\n\n\n<ol start=\"70\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Clelland, J.D., Allen, R.E. and Thornalley, P.J. (1992) Inhibition growth of human leukaemia 60 cells in culture by S-2-hydroxyacyl-glutathiones and their monoethyl ester derivatives, Biochem. Pharmacol. <strong>44<\/strong>, 1953-1959.<\/li>\n<\/ol>\n\n\n\n<ol start=\"71\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Smith, P.R. and Thornalley, P.J. (1992) Mechanism of the degradation of fructosamines under physiological conditions. Studies with the model peptide fructosamine N-1-deoxy-D-fructos-1-yl-hippuryl-lysine, Eur. J. Biochem. <strong>210<\/strong>, 729-739.<\/li>\n<\/ol>\n\n\n\n<ol start=\"72\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Smith, P.R., Somani, H.H., Thornalley, P.J., Benn, J. and S\u00f6nksen, P.H. (1992) Evidence against the formation of N<sub>e<\/sub>-2-amino-6-(1-formyl-5-hydroxymethyl-pyrrol-1-yl)hexanoic acid, &#8220;Pyrraline&#8221;, an early-stage product or advanced glycation endproduct in non-enzymatic protein glycation. Clin. Sci. <strong>84<\/strong>, 87-93.<\/li>\n<\/ol>\n\n\n\n<ol start=\"73\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Lo, T.W.C. and Thornalley, P.J. (1992) Inhibition of growth of human leukaemia 60 cells in culture by diethyl esters of glyoxalase inhibitors, Biochem. Pharmacol. <strong>44<\/strong>, 2357-2363.<\/li>\n<\/ol>\n\n\n\n<ol start=\"74\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1993) Theory and application of the electron spin resonance technique of spin trapping. In &#8220;Autoxidation&#8221;, Vol. III (G. Scott, ed.), Elsevier, Amsterdam, pp. 33-69.<\/li>\n<\/ol>\n\n\n\n<ol start=\"75\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Allen, R.E., Lo, T.W.C. and Thornalley, P.J. (1993) A simplified method for the purification of human red blood cell glyoxalase I. Characteristics, immunoblotting and inhibitor studies. J. Protein Chem. <strong>12<\/strong>, 111-119.<br><\/li>\n\n\n\n<li class=\"has-medium-font-size\">Phillips, S.A. and Thornalley, P.J. (1993) The formation of methylglyoxal from triosephosphates. Investigation using a specific assay for methylglyoxal. Eur. J. Biochem. <strong>212<\/strong>, 101-105.<\/li>\n<\/ol>\n\n\n\n<ol start=\"77\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Edwards, L.G., Clelland, J.D. and Thornalley, P.J. (1993) Characteristics of the inhibition of human promyelocytic leukaemia HL60 cell growth by S-d-lactoylglutathione <em>in vitro<\/em>. Leuk. Res. <strong>17<\/strong>, 305-310.<\/li>\n<\/ol>\n\n\n\n<ol start=\"78\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ayoub, F.M., Zaman, M.A., Thornalley, P.J. and Masters, J.R.W. (1993) Glyoxalase activities in human tumour cell lines <em>in vitro<\/em>. Anticancer Res. <strong>13<\/strong>, 151-156.<\/li>\n<\/ol>\n\n\n\n<ol start=\"79\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ayoub, F.M., Allen, R.E. and Thornalley, P.J. (1993) Inhibition of proliferation of human leukaemia 60 cells by methylglyoxal <em>in vitro<\/em>. Leuk. Res. <strong>17<\/strong>, 397-401.<\/li>\n<\/ol>\n\n\n\n<ol start=\"80\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C., Phillips. S.A. and Thornalley, P.J. (1993) The assay of S-D-lactoylglutathione in biological systems. Anal. Biochem. <strong>211<\/strong>, 37-43.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"81\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Allen, R.E., Lo, T.W.C. and Thornalley, P.J. (1993) Purification and characterisation of glyoxalase II from human red blood cells. Eur. J. Biochem. <strong>213<\/strong>, 1261-1267.<\/li>\n<\/ol>\n\n\n\n<ol start=\"82\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Phillips, S.A., Mirrlees, D. and Thornalley, P.J. (1993) Modification of the glyoxalase system in streptozotocin-induced diabetic rats. Effect of the aldose reductase inhibitor Statil. Biochem. Pharmacol. <strong>46<\/strong>, 805-811.<\/li>\n<\/ol>\n\n\n\n<ol start=\"83\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1993) The glyoxalase system in health and disease. Mol. Aspects of Med. <strong>14<\/strong>, 287-371.<br><\/li>\n\n\n\n<li class=\"has-medium-font-size\">Lo, T.W.C. and Thornalley, P.J. (1994) Synthesis of <sup>14<\/sup>C-labelled aminoguanidine. J. Labelled Compounds &amp; Radiopharmaceuticals <strong>34<\/strong>, 179-184.<\/li>\n<\/ol>\n\n\n\n<ol start=\"85\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Strath, M.J. and Wilson, R.J.M. (1994) Anti-malarial activity of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester. Biochem. Pharmacol. <strong>47<\/strong>, 418-420.<\/li>\n<\/ol>\n\n\n\n<ol start=\"86\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1994) Methylglyoxal, glyoxalases and the development of diabetic complications. Amino Acids <strong>6<\/strong>, 15-23.<\/li>\n<\/ol>\n\n\n\n<ol start=\"87\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">M<sup>c<\/sup>Lellan, A.C., Thornalley, P.J., Benn, J. and S\u00f6nksen, P.H. (1994) The glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. <strong>87<\/strong>, 21-29.<\/li>\n<\/ol>\n\n\n\n<ol start=\"88\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Edwards, L.G. and Thornalley, P.J. (1994) Prevention of the S-D-lactoylglutathione-induced inhibition of human leukaemia 60 cell growth by uridine. Leuk. Res. <strong>18<\/strong>, 717-722.<\/li>\n<\/ol>\n\n\n\n<ol start=\"89\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Lo, T.W.C., Selwood, T. and Thornalley, P.J. (1994) The reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins. Biochem. Pharmacol. <strong>48<\/strong>, 1865-1870.<\/li>\n<\/ol>\n\n\n\n<ol start=\"90\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Haik, G., Jr., Lo, T.W.C. and Thornalley, P.J. (1994) Methylglyoxal concentration and glyoxalase activities in the human lens. Exp. Eye Res. <strong>59<\/strong>, 497-500.<\/li>\n<\/ol>\n\n\n\n<ol start=\"91\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Lo, T.W.C., Westwood, M.E., M<sup>c<\/sup>Lellan, A.C., Selwood, T. and Thornalley, P.J. (1994) Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N<sub>\u03b1<\/sub>-acetylarginine, N<sub>\u03b1<\/sub>-acetylcysteine and N<sub>\u03b1<\/sub>-acetyl-lysine, and bovine serum albumin. J. Biol. Chem. <strong>269<\/strong>, 32299-32305.<br><\/li>\n\n\n\n<li class=\"has-medium-font-size\">Westwood, M.E., M<sup>c<\/sup>Lellan, A.C. and Thornalley, P.J. (1994) Receptor-mediated endocytic uptake of methylglyoxal-modified protein. Competition with advanced glycation endproduct-modified protein at the advanced glycation endproduct receptor. J. Biol. Chem. <strong>269<\/strong>, 32293-32298.<\/li>\n<\/ol>\n\n\n\n<ol start=\"93\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Minhas, H.M. and Thornalley, P.J. (1995) Comparison of the delivery of reduced glutathione into reduced glutathione into P388D<sub>1<\/sub> cells by reduced glutathione and its mono- and di-ethyl ester derivatives. Biochem. Pharmacol. <strong>49<\/strong>, 1475-1482.<\/li>\n<\/ol>\n\n\n\n<ol start=\"94\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1995) Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-d-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor. Crit. Rev. Oncology &amp; Hematol. <strong>20<\/strong>, 99-128.<\/li>\n<\/ol>\n\n\n\n<ol start=\"95\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Westwood, M.E., Lo, T.W.C. and McLellan, A.C. (1995) Formation of methylglyoxal-modified proteins <em>in vitro<\/em> and <em>in vivo<\/em> and their involvement in AGE-related processes. Dialysis-related Amyloidosis (Maeda, K. and Shinzato, T. eds.), Contrib. Nephrol. <strong>112<\/strong>, 24-31.<\/li>\n<\/ol>\n\n\n\n<ol start=\"96\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Westwood, M.E. and Thornalley, P.J. (1995) Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. J. Protein Chem. <strong>14<\/strong>, 359-372.<\/li>\n<\/ol>\n\n\n\n<ol start=\"97\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Adesida, A., Edwards L.G. and Thornalley, P.J. (1995) Facile synthesis of (<em>R<\/em>)N-2-hydroxyacyl-l-cysteine derivatives: (<em>R<\/em>)N-2-hydroxyacyl transfer from enzymatically-synthesized (<em>R<\/em>)S-2-hydroxyacylglutathiones to l-cysteine. Amino Acids <strong>9<\/strong>, 185-189.<\/li>\n<\/ol>\n\n\n\n<ol start=\"98\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Edwards, L.G., Adesida, A. and Thornalley, P.J. (1996) Inhibition of human leukaemia 60 cell growth by <em>S<\/em>-d-lactoylglutathione <em>in vitro<\/em>. Mediation by metabolism to <em>N<\/em>-d-lactoylcysteine and induction of apoptosis. Leuk. Res. <strong>20<\/strong>, 17-26.<\/li>\n<\/ol>\n\n\n\n<ol start=\"99\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Minhas, H.S. and Thornalley, P.J. (1996) Reduced glutathione esters &#8211; antidotes to toxicity. Cytotoxicity induced by hydrogen peroxide, 1-chloro-2,4-dinitrobenzene and menadione in murine P388D<sub>1<\/sub> macrophages <em>in vitro<\/em>. J. Biochem. Toxicol. <strong>10<\/strong>, 245-250.<\/li>\n<\/ol>\n\n\n\n<ol start=\"100\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Adesida, A., Edwards, L.G. and Thornalley, P.J. (1996) Inhibition of human leukaemia 60 cell growth by <em>S<\/em>-(<em>N<\/em>-phenylethylthiocarbamoyl)cysteine. Food Chem. Toxicol. <strong>34<\/strong>, 385-392.<\/li>\n<\/ol>\n\n\n\n<ol start=\"101\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Kang, Y., Edwards, L.G. and Thornalley, P.J. (1996) Effect of methylglyoxal on human leukemia cell growth: modification of DNA, G<sub>1<\/sub> growth arrest and induction of apoptosis. Leuk. Res. <strong>20<\/strong>, 397-405.<\/li>\n<\/ol>\n\n\n\n<ol start=\"102\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Westwood, M.E. and Thornalley, P.J. (1996) Induction of synthesis and secretion of interleukin-1\u03b2 in the human monocytic leukaemia THP-1 cells by human serum albumins modified with methylglyoxal and advanced glycation endproducts. Immunol. Lett. <strong>50<\/strong>, 17-21.<\/li>\n<\/ol>\n\n\n\n<ol start=\"103\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1996) Pharmacology of Methylglyoxal: Formation, Modification of Proteins and Nucleic acids, and Enzymatic Detoxification. A role in pathogenesis and antiproliferative chemotherapy. General Pharmacol. <strong>27<\/strong>, 565-573.<\/li>\n<\/ol>\n\n\n\n<ol start=\"104\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Ladan, M.J., Ridgway, S.J.S and Kang, Y. (1996) Antitumour activity of S-p-bromobenzylglutathione diesters <em>in vitro<\/em>: a structure activity study. J. Med. Chem. <strong>39<\/strong>, 3409-3411.<br><\/li>\n\n\n\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1996) Advanced glycation and the development of diabetic complications. Unifying the involvement of glucose, methylglyoxal and oxidative stress. Endocrinol. &amp; Metab. <strong>3<\/strong>, 149-166.<\/li>\n<\/ol>\n\n\n\n<ol start=\"106\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Wyatt, C., Davies, N., Edwards, L.G., Kang, Y., Ladan, M.J. and Double, J. (1996) Antitumour activity of <em>S<\/em>-p-bromobenzylglutathione cyclopentyl diester <em>in vitro<\/em> and <em>in vivo<\/em>. Inhibition of glyoxalase I and induction of apoptosis. Biochem. Pharmacol. <strong>51<\/strong>, 1365-1372.<\/li>\n<\/ol>\n\n\n\n<ol start=\"107\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Abordo, E.A, Westwood, M.E. and Thornalley, P.J. (1996) Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts. Immunol. Lett. <strong>53<\/strong>, 7-13.<\/li>\n<\/ol>\n\n\n\n<ol start=\"108\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., M<sup>c<\/sup>Lellan, A.C., Lo, T.W.C., Benn, J. and S\u00f6nksen, P.H. (1996) Negative association of red blood cell reduced glutathione concentration with diabetic complications. Clin. Sci. <strong>91<\/strong>, 575-582.<\/li>\n<\/ol>\n\n\n\n<ol start=\"109\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Westwood, M.E. and Thornalley, P.J. (1997) Glycation and advanced glycation endproducts. In: \u201cThe Glycation hypothesis of atherosclerosis\u201d (C. Colaco ed.), R.G. Landes, Georgetown, USA, pp. 57-87.<\/li>\n<\/ol>\n\n\n\n<ol start=\"110\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Westwood, M.E., Argirov, O.K., Abordo, E.A and Thornalley, P.J. (1997) Methylglyoxal-modified arginine residues &#8211; a signal for receptor-mediated endocytosis and degradation of proteins by human monocytic THP-1 cells. Biochim. Biophys. Acta. <strong>1356<\/strong>, 84-94.<\/li>\n<\/ol>\n\n\n\n<ol start=\"111\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Abordo, E.A. and Thornalley, P.J. (1997) Synthesis and secretion of tumour necrosis factor-alpha by human monocytic THP-1 cells and chemotaxis induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts. Immunol. Lett. <strong>58<\/strong>, 139-147.<\/li>\n<\/ol>\n\n\n\n<ol start=\"112\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1997) Inhibition of glyoxalase I (EC 4.4.1.5). In: Emerging therapeutic targets (Anand, R., Smith, P. and Warne, P. eds.), Ashley Pubs Ltd, London <strong>1<\/strong>, 203-206<\/li>\n<\/ol>\n\n\n\n<ol start=\"113\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1998) Glyoxalase I. Human Protein Data, 2nd edn. (A. Haeberli, ed.), VCH Verlag GmbH, Weinheim.<\/li>\n<\/ol>\n\n\n\n<ol start=\"114\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1998) Human Glyoxalase II. Human Protein Data, 2nd edn (A. Haeberli, ed.), VCH Verlag GmbH, Weinheim.<\/li>\n<\/ol>\n\n\n\n<ol start=\"115\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Shinohara, M., Thornalley, P.J., Giardino, I., Beisswenger, P., Thorpe, S.R., Onorato, J. and Brownlee, M. (1998) Overexpression of glyoxalase I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycaemia-induced increases in macromolecular endocytosis. J. Clin. Invest. <strong>101<\/strong>, 1142-1147.<\/li>\n<\/ol>\n\n\n\n<ol start=\"116\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1998) GSH-dependent detoxification of \u03b1-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors. Chemico-biol. Interact. <strong>111-112<\/strong>, 137-151.<\/li>\n<\/ol>\n\n\n\n<ol start=\"117\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Cook, L.J., Davies, J., Yates, A.P., Sheader, E.A., Elliott, A.C., Lovell, J., Joule, J.A., Thornalley, P.J. and Best, L. (1998) Effects of methylglyoxal on pancreatic \u03b2-cells. Biochem. Pharmacol. <strong>55<\/strong>, 1361-1367.<\/li>\n<\/ol>\n\n\n\n<ol start=\"118\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Abordo, E.A. and Thornalley, P.J. (1998) Pro-inflammatory cytokine synthesis by human monocytes induced by proteins minimally-modified by methylglyoxal. In: The Maillard Reaction in Foods and Medicine, Royal Soc. Chem. Spec. Pub. No 223 (Nursten, H.E., Crabbe, M.J.C. and Ames, J.M. eds.), pp. 357-362.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"119\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1998) Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. Cell. Molec. Biol. <strong>44<\/strong>, 1013-1023.<\/li>\n<\/ol>\n\n\n\n<ol start=\"120\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Eriksson, U.J., Wentzel, P., Minhas, H.S. and Thornalley, P.J. (1998) 3-Deoxyglucosone is a teratogenic agent in diabetic embryopathy. Diabetes <strong>47<\/strong>, 1960-1966.<\/li>\n<\/ol>\n\n\n\n<ol start=\"121\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Minhas, H.S. (1999) Rapid hydrolysis and slow \u03b1,\u03b2-dicarbonyl cleavage of an agent proposed to cleave glucose-derived protein crosslinks. Biochem. Pharmacol. <strong>57<\/strong>, 303-307.<\/li>\n<\/ol>\n\n\n\n<ol start=\"122\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Best, L. and Thornalley, P.J. (1999) Trioses and related substances: tools for the study of pancreatic beta-cell function. Biochem. Pharmacol. <strong>57<\/strong>, 583-588.<\/li>\n<\/ol>\n\n\n\n<ol start=\"123\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1999) The clinical significance of glycation. Clin. Lab. <strong>5-6,<\/strong> 263-273.<\/li>\n<\/ol>\n\n\n\n<ol start=\"124\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (1999) More good things in vegetables than you ever imagined. How dietary isothiocyanates activate mitogen-activated proteins kinase to induce apoptosis of pre-clinical tumours and protect against cancer. The Biochemist <strong>21,<\/strong> no 3, 19-23.<\/li>\n<\/ol>\n\n\n\n<ol start=\"125\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Abordo, E.A., Minhas, H.S. and Thornalley, P.J. (1999) Accumulation of \u03b1-oxoaldehydes during oxidative stress. A role in cytotoxicity. Biochem. Pharmacol. <strong>58,<\/strong> 641-648.<\/li>\n<\/ol>\n\n\n\n<ol start=\"126\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xu, K. and Thornalley, P.J. (1999) Synthesis of <sup>14<\/sup>C-labelled phenethyl isothiocyanate and the cysteine conjugate S-(N-phenethylthiocarbamoyl)cysteine and use in cell interactions with these agents. J. Labelled Compds Radiopharm. <strong>42<\/strong>, 1069-1074.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"127\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Langborg, A. and Minhas, H.S. (1999) Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem. J. <strong>344,<\/strong> 109-116.<\/li>\n<\/ol>\n\n\n\n<ol start=\"128\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xu, K. and Thornalley, P.J. (2000) Antitumour activity of sphingoid adducts of phenethyl isothiocyanate. Bio-org. Medicinal. Chem. Lett. <strong>10,<\/strong> 1-2.<\/li>\n<\/ol>\n\n\n\n<ol start=\"129\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Yurek-George, A. and Argirov, O.K. (2000) Kinetics and mechanism of the reaction of aminoguanidine with the \u03b1-oxoaldehydes, glyoxal, methylglyoxal and 3-deoxyglucosone, under physiological conditions. Biochem. Pharmacol. <strong>60<\/strong>, 55-65.<\/li>\n<\/ol>\n\n\n\n<ol start=\"130\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xu, K. and Thornalley, P.J. (2000) Studies on the mechanism of the inhibition of human leukaemia cell growth by dietary isothiocyanates and their cysteine adducts <em>In vitro<\/em> Biochem. Pharmacol. <strong>60<\/strong>, 221-231.<\/li>\n<\/ol>\n\n\n\n<ol start=\"131\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Argirova, M., Argirov, O.K., Ahmed, N., Mann, V.M. and Dawnay, A. (2000) Mass spectrometric monitoring of albumin in uraemia. Kidney Internat. <strong>58<\/strong>, 2228-2234.<\/li>\n<\/ol>\n\n\n\n<ol start=\"132\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xu, K. and Thornalley, P.J. (2001) Involvement of GSH metabolism in the cytotoxicity of the phenethyl isothiocyanate and its cysteine conjugate to human leukaemia cells <em>in vitro<\/em>. Biochem. Pharmacol. <strong>61<\/strong>, 165-177.<\/li>\n<\/ol>\n\n\n\n<ol start=\"133\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xu, K. and Thornalley, P.J. (2001) Signal transduction activated by the cancer chemopreventive isothiocyanates: cleavage of BID protein, tyrosine phosphorylation and activation of JNK. Brit. J. Cancer&nbsp; <strong>84<\/strong>, 670-673.<\/li>\n<\/ol>\n\n\n\n<ol start=\"134\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Jahan, I. and Ng, R. (2001) Suppression of the accumulation of triosephosphates and increased formation of methylglyoxal in human red blood cells during hyperglycaemia by thiamine <em>in vitro<\/em>. Japanese J. Biochem. <strong>129<\/strong>, pp. 543\u2013549.<\/li>\n<\/ol>\n\n\n\n<ol start=\"135\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Argirov, O.K., Minhas, H.S., Cordeiro, C. and Thornalley, P.J. (2002) Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatisation by aminoquinolyl-N-hydroxysuccimidyl-carbamate and application to N<sub>\u03b5<\/sub>-carboxymethyl-lysine- and N<sub>\u03b5<\/sub>-(1-carboxyethyl)lysine-modified albumin. Biochem. J. <strong>364<\/strong>, 1 \u2013 14.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"136\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N. and Thornalley, P.J. (2002) Chromatographic assay of glycation adducts in human serum albumin glycated <em>in vitro<\/em> by derivatisation with aminoquinolyl-N-hydroxysuccimidyl-carbamate and intrinsic fluorescence. Biochem. J. <strong>364<\/strong>, 15 \u2013 24.<\/li>\n<\/ol>\n\n\n\n<ol start=\"137\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2002) Isothiocyanates: mechanism of cancer chemopreventive action. Anticancer drugs 13, 331-338.<\/li>\n<\/ol>\n\n\n\n<ol start=\"138\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2002) Methods for studying the binding of advanced glycated proteins to receptors for advanced glycation end products (AGE receptors). In: Ultrastructural and Molecular Biology Protocols, vol. 196 (D. Armstrong ed.), Humana Press, Totowa, USA, pp. 49-62.<\/li>\n<\/ol>\n\n\n\n<ol start=\"139\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2002) Glycation in diabetic neuropathy. Characteristics, consequences, causes and therapeutic options. Neurobiology of Diabetic neuropathy (D. Tomlinson Ed.), Intern. Review of Neurobiology, vol 50, pp. 37 \u2013 57, Academic Press, New York.<\/li>\n<\/ol>\n\n\n\n<ol start=\"140\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Prinsen, B. H.C.M.T., Kaysen, G.A., Klomp, L.W.J., de Boer, J., Barrett, P.H.R., Thornalley, P.J., Battah, S., Berger, R., Rabelink, T.J., and de Sain-van der Velden<sup>, <\/sup>M.G.M. (2002) Idiopathic hypoalbuminemia explained by reduced synthesis rate and an increased catabolic rate. Clin. Biochem. 35, 545-553.<\/li>\n<\/ol>\n\n\n\n<ol start=\"141\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Kilhovd, B.K., Giardino,I., Torjesen, P.A., Birkeland,K.I., Berg, T.J., Thornalley, P.J., Brownlee, M. and Hansen, K.F. (2003) Increased serum levels of the specific age-compound methylglyoxal derived hydroimidazolone on patients with type 2 diabetes. Metabolism. 52, 163-167.<\/li>\n<\/ol>\n\n\n\n<ol start=\"142\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Babaei-Jadidi, R., Karachalias, N., Battah, S., Ahmed, N.M. and Thornalley, P.J. (2003) Prevention of incipient diabetic nephropathy by high dose thiamine and Benfotiamine. Diabetes 52, 2110-2120.<\/li>\n<\/ol>\n\n\n\n<ol start=\"143\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2003) Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts (AGEs). Arch. Biochem. Biophys. 419, 31-40<\/li>\n<\/ol>\n\n\n\n<ol start=\"144\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Battah, S., Ahmed, N., Karachalias, N., Agalou, S., Babaei-Jadidi, R. and Dawnay, A. (2003) Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by <strong>tandem mass spectrometry Biochem. J. 375, 581-592<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"145\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Battah, S., Karachalias, N., Babaei-Jadidi, R., Hor\u00e1nyi, M., Bar\u00f3ti, M., Hollan, S., and Thornalley, P.J. (2003) Increased formation of methylglyoxal and protein glycation, oxidation and nitrosation in triosephosphate isomerase deficiency. Biochim. Biophys. Acta Mechanisms of disease <strong>1639<\/strong>, 121-132<\/li>\n<\/ol>\n\n\n\n<ol start=\"146\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Thornalley, P.J., Dawczynski, J., Franke, S., Strobel, J. and Stein, G. (2003) Methylglyoxal-derived hydroimidazolone advanced glycation endproducts of human lens proteins. Invest. Ophthamol. Vis. Sci. <strong>44<\/strong>, 5287-5202<\/li>\n<\/ol>\n\n\n\n<ol start=\"147\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2004) Glycation, receptor-mediated cell activation and vascular complications of diabetes. Diabetes and Vascular Disease <strong>1<\/strong>, 21-22.<\/li>\n<\/ol>\n\n\n\n<ol start=\"148\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2004) Glycation- and\/or Polyol Pathway-inducing Complications. Encyclopedia of Endocrinology and related diseases, Academic Press, New York, <strong>2<\/strong>, 275-278.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"149\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">McWalter, G.K., Higgins, L.G., McLellan, L.I., Henderson, C.J., Song, L., Thornalley, P.J., Itoh, K., Yamamoto, M. and Hayes, J.D. (2004) Transcription factor Nrf2 is essential for induction of NAD(P)H: quinone oxidoreductase-1, glutathione S-transferase and glutamate cysteine ligase by broccoli seeds and isothiocyanates. J. Nutr. <strong>134<\/strong>, 3499S-3506S<\/li>\n<\/ol>\n\n\n\n<ol start=\"150\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Thornalley, P.J., L\u00fcthen, R., H\u00e4ussinger, D., Sebekova, K., Schinzel, R., Voelker, W. and Heidland, A. (2004) Processing of protein glycation, oxidation and nitrosation adducts in the liver and the effect of cirrhosis. J. Hepatology <strong>41<\/strong>, 913-919.<\/li>\n<\/ol>\n\n\n\n<ol start=\"151\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Jono, T., Nagai, R., Lin, X., Ahmed, N., Thornalley, P.J., Takeya, M., Horiuchi, S. (2004) N<sub>\u03b5<\/sub>-(Carboxymethyl)lysine and 3-DG-imidazolone are major AGE structures in protein modification by 3-deoxyglucosone. J. Biochem. <strong>136<\/strong>, 351-358.<\/li>\n<\/ol>\n\n\n\n<ol start=\"152\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., and IARC Working Group (2004) Cruciferous Vegetables, Isothiocyanates and Indoles, IARC Handbook on Cancer Prevention, IARC Press, Lyon, pp. 1 \u2013 262.<\/li>\n<\/ol>\n\n\n\n<ol start=\"153\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Babaei-Jadidi, R., Karachalias, N., Kupich, C., Ahmed, N. and Paul J. Thornalley. (2004) High dose thiamine therapy counters dyslipidaemia in diabetes. Diabetologia <strong>47<\/strong>, 2235 \u2013 2246<\/li>\n<\/ol>\n\n\n\n<ol start=\"154\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Ahmed, U., Hager, K., Fleischer, G., M\u00fcnch, G. and Thornalley, P.J. (2005) Protein glycation, oxidation and nitration marker residues and free adducts of cerebrospinal fluid in Alzheimer\u2019s disease and link to cognitive impairment. J. Neurochem. <strong>92<\/strong>, 255\u2013263.<\/li>\n<\/ol>\n\n\n\n<ol start=\"155\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N.<sub>,<\/sub> Dobler, D., Dean, M.<sub> <\/sub>and Thornalley, P.J. (2005) Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J. Biol. Chem. <strong>280<\/strong>, 5724-5732<\/li>\n<\/ol>\n\n\n\n<ol start=\"156\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Agalou, A., Ahmed, N., Babaei-Jadidi, R., Dawnay, A. and Thornalley, P.J. (2005) Profound mishandling of protein glycation degradation products in uremia and dialysis. J. Am. Soc. Nephrol. 16, 1471 \u2013 1485<\/li>\n<\/ol>\n\n\n\n<ol start=\"157\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Berlanga, J., Cibrian, D., Guill\u00e9n,&nbsp;I., Freyre, F., Alba, J.S., Merino, N., Aldama, A., Quintela, A.M., Triana, M.E., Ajameich, H., Lopez, P., Ahmed, N. and Thornalley, P.J. (2005) Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of skin wounds. Clin. Sci. 109, 83-95.<\/li>\n<\/ol>\n\n\n\n<ol start=\"158\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Mirshekar-Syahkal, B., Kennish, L., Karachalias, N., Babaei-Jadidi, R. and Thornalley, P.J. (2005) Assay of advanced glycation endproducts in selected beverages and food by liquid chromatography with tandem mass spectrometric detection. Molec. Nutrit. Food Res. 47, 691-699.<\/li>\n<\/ol>\n\n\n\n<ol start=\"159\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Babaei-Jadidi, R., Karachalias, N., Kupich, C., Ahmed, N. and Thornalley, P.J. (2005) High dose thiamine therapy counters dyslipidemia and advanced glycation of plasma protein in streptozotocin-induced diabetic rats. Ann. N.Y. Acad. Sci. 1043, 777 \u2013 783.<\/li>\n<\/ol>\n\n\n\n<ol start=\"160\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N. and Thornalley, P.J. (2005) Peptide mapping of human serum albumin modified minimally by methylglyoxal <em>in vitro<\/em> and <em>in vivo<\/em>. Ann. N.Y. Acad. Sci. 1043, 260 &#8211; 266.<\/li>\n<\/ol>\n\n\n\n<ol start=\"161\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2005) Dicarbonyl intermediates in the Maillard reaction. Ann. N.Y. Acad. Sci. 1043, 111 \u2013 117.<\/li>\n<\/ol>\n\n\n\n<ol start=\"162\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Agalou, S, Ahmed, N, Thornalley, P.J. and Dawnay, A. (2005) Removal of free advanced glycation endproducts by haemodialysis. Ann. N.Y. Acad. Sci. 1043, 734 &#8211; 739.<\/li>\n<\/ol>\n\n\n\n<ol start=\"163\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Thornalley, P.J., L\u00fcthen, R., H\u00e4ussinger, D.,<sup> <\/sup>Sebekova, K., Schinzel, R., Voelker, W. and Heidland, A. (2005) increased protein glycation in cirrhosis. Ann. N.Y. Acad. Sci. 1043, 718 \u2013 724.<\/li>\n<\/ol>\n\n\n\n<ol start=\"164\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed<sub>,<\/sub> N.,<sub> <\/sub>Babaei-Jadidi,<sup> <\/sup>Howell, S.K., Beisswenger, P.J.<sub> <\/sub>and Thornalley, P.J. (2005) Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes. Diabetologia 48, 1590 \u2013 1603.<\/li>\n<\/ol>\n\n\n\n<ol start=\"165\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2005) <strong>The potential role of thiamine (vitamin B<\/strong><strong><sub>1<\/sub><\/strong><strong>) in diabetic complications. Current Diabetes Reviews 1, 287 \u2013 298.<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"166\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2005) Glycation free adduct accumulation in renal disease: The new AGE. Pediatric Nephrol. 20, 1515-1522.<\/li>\n<\/ol>\n\n\n\n<ol start=\"167\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N., Babaei-Jadidi, R., Howell, S.K., Thornalley, P.J. and Beisswenger, P.J. (2005) Glycated and oxidised protein degradation products are indicators of fasting and postprandial hyperglycemia in diabetes. Diabetes Care 28, 2465\u20132471.<\/li>\n<\/ol>\n\n\n\n<ol start=\"168\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Song, L., Morrison, J.J., Botting, N.P. and Thornalley, P.J. (2005) Analysis of glucosinolates, isothiocyanates and amine degradation products in vegetable extracts and blood plasma by LC-MS\/MS. Anal. Biochem. 347, 234\u2013243.<\/li>\n<\/ol>\n\n\n\n<ol start=\"169\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2005) Technological advances in peritoneal dialysis research: Measurement of protein glycation, glycated peptides and glycation free adducts. Peritoneal. Dialysis Internat. 25, 522\u2013533.<\/li>\n<\/ol>\n\n\n\n<ol start=\"170\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2006) Quantitative screening of protein glycation, oxidation and nitration adducts by LC-MS\/MS: protein damage in diabetes, uremia, cirrhosis and Alzheimer\u2019s disease. Redox Proteomics, Protein Oxidative Modifications, and Human Disease (Dalle-Donne, I., Scaloni, A. and Butterfield, A. eds.), Wiley-Interscience, 681 \u2013 727<\/li>\n<\/ol>\n\n\n\n<ol start=\"171\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Song, L., Iori, R. and Thornalley, P.J. (2006) Purification of major glucosinolates from <em>Brassicaceae<\/em> seeds and preparation of isothiocyanate and amine metabolites. J. Sci. Food and Agric. 86, <strong>1271-1280.<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"172\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2006) Unease on the role of glyoxalase 1 in high-anxiety-related behaviour. Trends in Molec. Med. 12, 195-199.<\/li>\n<\/ol>\n\n\n\n<ol start=\"173\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Dobler, D., Ahmed, N., Song, L., Eboigbodin, K.E. and Thornalley, P.J. (2006) Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification. Diabetes 55, 1961-1969.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"174\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2006) Advanced glycation endproducts in renal failure. J. Renal Nutrit. 16, 178-184.<\/li>\n<\/ol>\n\n\n\n<ol start=\"175\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\"><strong>Thornalley, P.J. (2006) <\/strong>Protein oxidation marker residues and oxidised amino acids in disease &#8211; the damage and the debris of protein oxidation. In: Protein Oxidation and Disease (Pandalai, S.G. and Pietzsch, J. eds), Research Signpost, Kerala, India, 143-178.<\/li>\n<\/ol>\n\n\n\n<ol start=\"176\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Nicolay, J.P., Schneider, J., Niemoeller, O.M., Artunc, F., Portero-Otin, M., Haik Jr., G., Thornalley, P.J., Schleicher, E., Wieder, T., Lang, F. (2006) Stimulation of suicidal erythrocyte death by methylglyoxal. Cell. Physiol. &amp; Biochem. 18, 223-232<\/li>\n<\/ol>\n\n\n\n<ol start=\"177\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Song, L. and Thornalley, P.J. (2007) Effect of storage, processing and cooking on glucosinolates in <em>Brassica<\/em> vegetables. Food Chem. Toxicol. 45,&nbsp; 216\u2013224<\/li>\n<\/ol>\n\n\n\n<ol start=\"178\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, N. and Thornalley, P.J. (2007) Advanced glycation endproducts: what is their relevance to diabetic complications? Diabetes, Obesity and Metabolism 9, 2007, 233\u2013245<\/li>\n<\/ol>\n\n\n\n<ol start=\"179\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2007) Endogenous \u03b1-oxoaldehydes and formation of protein and nucleotide advanced glycation endproducts in tissue damage. Novartis Foundation Symposium Series No 285 Acetaldehyde-related pathology: bridging the trans-disciplinary divide, Wiley, Chichester, pp 229 \u2013 246.<\/li>\n<\/ol>\n\n\n\n<ol start=\"180\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Babaei-Jadidi, R., Al Ali, H., Rabbani, N., Antonysunil, A.K., Larkin, J., Ahmed, A., Rayman, G., Bodmer, C.W. (2007) High prevalence of low plasma thiamine concentration in diabetes linked to a marker of vascular disease. Diabetologia 50, 2164 \u2013 2170.<\/li>\n<\/ol>\n\n\n\n<ol start=\"181\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Sebekova, K., Sebekova, K. Jr, Heidland, A. and Thornalley, P.J. (2007) Protein glycation, oxidation and nitration free adduct accumulation after bilateral nephrectomy and ureteral ligation. Kidney Internat. 72, 1113\u20131121<br><\/li>\n\n\n\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2007) Dietary AGEs and ALEs and risk to human health by their interaction with the receptor for advanced glycation endproducts (RAGE) &#8211; an introduction. Molec. Nutrit. and Food Res. 51, <strong>1107 \u2013 1110.<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"183\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Yao, D., Taguchi, T., Matsumura, T., Pestell, R., Edelstein, D., Giardino, I., Suske, G., Rabbani, N., Thornalley, P.J., Sarthy, V.P., Hammes, H.-P., and Michael Brownlee. High Glucose Increases Angiopoietin-2 Transcription in Microvascular Endothelial Cells through Methylglyoxal Modification of mSin3A J. Biol. Chem. 282: 31038 \u2013 31045, 2007.<\/li>\n<\/ol>\n\n\n\n<ol start=\"184\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Cohen, G., Glorieux, G., Thornalley, P.J., Schepers, E., Meert, N., Jankowski, J., Jankowski, V., Argiles, A., Anderstam, B., Brunet, P., Cerini, C., Dou, L., Deppisch, R., Marescau, B., Massy, Z., Perna, A., Raupachova, J., Rodriguez, M., Stegmayr, B., Vanholder, R., H\u00f6rl, W.H., for the European Uremic Toxin Work Group (EUTox) (2007) Review on uraemic toxins III: recommendations for handling uraemic retention solutes in vitro\u2014towards a standardized approach for research on uraemia. Nephrol. Dialysis Trans 22: 3381\u20133390<\/li>\n<\/ol>\n\n\n\n<ol start=\"185\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Fleming, T., Rabbani, R. and Thornalley, P.J. (2008) Preparation of nucleotide advanced glycation endproducts \u2013 imidazopurinone adducts formed by glycation of deoxyguanosine with glyoxal and methylglyoxal. Ann. N. Y. Acad. Sci. 1126,&nbsp; 280-2.<\/li>\n<\/ol>\n\n\n\n<ol start=\"186\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2008) The dicarbonyl proteome \u2013 proteins susceptible to dicarbonyl glycation at functional sites in health, ageing and disease. Ann. N. Y. Acad. Sci. <strong>1126,<\/strong> 124-127.<\/li>\n<\/ol>\n\n\n\n<ol start=\"187\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U., Dobler, D., Carpenter, S.J., Rabbani, N. and Thornalley, P.J. (2008) Reversal of hyperglycaemia-induced angiogenesis deficit of human endothelial cells by overexpression of glyoxalase 1 <em>in vitro<\/em>. Ann. N. Y. Acad. Sci. 1126, 262 &#8211; 264.<\/li>\n<\/ol>\n\n\n\n<ol start=\"188\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. (2008) Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems &#8211; role in ageing and disease. Drug Metabolism and Drug Interactions 23, 125 \u2013 150.<\/li>\n<\/ol>\n\n\n\n<ol start=\"189\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Morcos, M., Du, X., Sayed, A.A.R., Hutter, H., Pfisterer, F., Thornalley, P.J., Baynes, J., Thorpe, S., Abd El Baki, R., Ahmed, N., Miftari, N., Stern, D., Schlotterer, A., M\u00f6hrlen, F., Hamann, A., Becker, C., Humpert, P., Hammes, H.P., B\u00fcchler, M., Bierhaus, A., Brownlee, M., Nawroth, P.P. (2008) Glyoxalase-1 prevents mitochondrial protein modification and enhances life-span in <em>C. elegans. <\/em>Aging Cell 7, 260-269.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"190\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2008) Assay of 3-Nitrotyrosine in Tissues and Body Fluids by Liquid Chromatography with Tandem Mass Spectrometric Detection. Methods in Enzymol. 440, 337-359.<\/li>\n<\/ol>\n\n\n\n<ol start=\"191\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2008) Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress. Biochem. Soc. Trans. 36, 1045-1050<\/li>\n<\/ol>\n\n\n\n<ol start=\"192\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M. Qian, Q., Antonysunil, A., Rabbani, N., Babaei-Jadidi, R. and Thornalley, P.J. (2008) Activation of NF-E2-related factor-2 reverses biochemical dysfunction of endothelial cells induced by hyperglycemia linked to vascular disease. Diabetes 57, 2809 -2817.<\/li>\n<\/ol>\n\n\n\n<ol start=\"193\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Foyer,CH, Faragher,R, Thornalley,P: Redox metabolism and longevity relationships in animals and plants. Preface. <em>SEB Exp Biol Ser<\/em> 62:xix-xxx, 2009<\/li>\n<\/ol>\n\n\n\n<ol start=\"194\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M.Z., AntonySunil, A., Rabbani, N. and Thornalley, P.J. (2009) Chapter 15. Protein damage by glycation, oxidation and nitration in the ageing process. Advances in quantitation of protein damage and the emerging importance of decline in enzymatic defences as the ageing phenotype develops. In: Redox Metabolism and Longevity Relationships in Animals and Plants (Foyer, C., Faraghar, R. and Thornalley, P.J. eds), Garland Science, London, pp. 227 \u2013 265.<\/li>\n<\/ol>\n\n\n\n<ol start=\"195\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Wendler, A., Irsch, T., Rabbani, N., Thornalley, P.J. Luise Krauth-Siegel, R. (2009) Glyoxalase II does not support methylglyoxal detoxification but serves as a general trypanothione thioesterase in African trypanosomes. Molecular &amp; Biochemical Parasitology <strong>163<\/strong>, 19 \u2013 27.<\/li>\n<\/ol>\n\n\n\n<ol start=\"196\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Shahzad Alam, S., Riaz, S., Larkin, J.R.,&nbsp; Akhtar, M.W., Shafi, T. and Thornalley, P.J. (2009)&nbsp; High dose thiamine therapy for patients with type 2 diabetes and microalbuminuria: a pilot randomised, double-blind, placebo-controlled study. Diabetologia <strong>52<\/strong>, 208-212<\/li>\n<\/ol>\n\n\n\n<ol start=\"197\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Alam, S.S., Riaz, S., Larkin, J.R., Akhtar, M.W., Shafi, T. and Thornalley, P.J. (2009) Thiamine in diabetic nephropathy: a novel treatment modality? Reply to Alkhalaf A, Kleefstra N, Groenier KH et al. [letter] Diabetologia (2009) <strong>52<\/strong>,1214\u20131216<\/li>\n<\/ol>\n\n\n\n<ol start=\"198\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Vanhorebeek, I., Ellger, B., De Vos, R., Debaveye, Y., Vander Perre, S., Rabbani, N., Thornalley, P.J. and Van den Berghe, G. (2009) Tissue-specific glucose toxicity induces mitochondrial damage in a burn injury model of critical illness. Critical Care Medicine <strong>37<\/strong>, 1355 -1364&nbsp;&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"199\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2009) Quantitation of markers of protein damage by glycation, oxidation and nitration in peritoneal dialysis. Peritoneal Dialysis Internat. <strong>29<\/strong>, Suppl. 2, S51-S56<\/li>\n<\/ol>\n\n\n\n<ol start=\"200\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Kempler, P. (eds). (2009) Thiamine and benfotiamine therapy for the prevention of diabetic nephropathy. In: Complications of diabetes mellitus: pathophysiology and pathogenically-based treatment options (Thornalley, P.J. and Kempler, P. eds), Thieme, Stuttgart, Germany.<\/li>\n<\/ol>\n\n\n\n<ol start=\"201\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2009) Thiamine and benfotiamine therapy for the prevention of diabetic nephropathy. In: Complications of diabetes mellitus: pathophysiology and pathogenically-based treatment options (Thornalley, P.J. and Kempler, P. eds), Thieme, Stuttgart, Germany, pp. 9 \u2013 17.<\/li>\n<\/ol>\n\n\n\n<ol start=\"202\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2009) Thiamine deficiency and renal function in diabetes. In: Complications of diabetes mellitus: pathophysiology and pathogenically-based treatment options (Thornalley, P.J. and Kempler, P. eds), Thieme, Stuttgart, Germany, pp. 18 \u2013 25.<\/li>\n<\/ol>\n\n\n\n<ol start=\"203\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">VanHolder, R., Abou-Deif, O., Argiles, A., Baurmeister, U., Beige, J., Brouckaert, P., Brouckaert, P., Brunet, P., Cohen, G , De Deyn, P.P., Drueke, T.B., Fliser, D., Glorieux, G., Herget-Rosenthal, S., Horl,W.H., Jankowski, J., Jorres, A., Massy, Z.A., Mischak, H., Perna, A.F., Rodriguez-Portillo, J.M., Spasovski, G., Stegmayr, B.G., Stenvinkel, P., Thornalley, P.J., Wanner, C., Wiecek, A. (2009) The Role of EUTox in Uremic Toxin Research. <em>Semin Dial<\/em> <strong>22<\/strong>, 323 \u2013 328<\/li>\n<\/ol>\n\n\n\n<ol start=\"204\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2009) Highlights and hotspots of protein glycation in end stage renal disease. Seminars in Dialysis 22, 400 &#8211; 404.<\/li>\n<\/ol>\n\n\n\n<ol start=\"205\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Vanhorebeek, I., Ellger, B., De Vos, R., Debaveye, Y., Vander Perre, S., Rabbani, N., Thornalley, P.J. and Van den Berghe, G. (2009). Hyperglycemic damage to renal tissue in an animal model of prolonged critical illness. Kidney Internat. <strong>76<\/strong>, 512 \u2013 520.<\/li>\n<\/ol>\n\n\n\n<ol start=\"206\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bechtold, U., Rabbani, N., Mullineux, P. and Thornalley, P.J. (2009) Quantitative measurement of specific biomarkers for protein oxidation, nitration and glycation in Arabidopsis leaves. Plant Journal <strong>59<\/strong>, 661 \u2013 671.<\/li>\n<\/ol>\n\n\n\n<ol start=\"207\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Klooster, A., Larkin, J.R., Adaikalakoteswari, A., Gans, R.O.B., van Goor, H., Thornalley, P.J., Rabbani, N., Navis, G., Leuvenink, H.G.D.<sup> <\/sup>and Bakker, S.J.L. (2009) Severe thiamine deficiency complicated by weight loss protects against renal ischemia-reperfusion injury in rats. Nephrol. Dial. Transplant. Plus <strong>2<\/strong>, 182-183<\/li>\n<\/ol>\n\n\n\n<ol start=\"208\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Duran-Jimenez, B., Dobler, D., Moffatt, S., Rabbani, N., Streuli, C.H. Thornalley, P.J., Tomlinson, D.R. and Gardiner, N.J. (2009) Advanced Glycation Endproducts in extracellular matrix proteins contribute to the failure of sensory nerve regeneration in diabetes. Diabetes <strong>58<\/strong>, <strong>2893-2903.<\/strong><strong>&nbsp;&nbsp;<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"209\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Schlotterer, A.,&nbsp; Kukudov, G.,&nbsp; Bozorgmehr, F.,&nbsp; Hutter, H., Du, X., Oikonomou, D., Ibrahim, Y., Pfisterer, F., Aydin, D., Rabbani, N., Thornalley, P.J., Sayed, A.A.R.,&nbsp; Fleming, T., Humpert, P., Schwenger, V., Zeier, M., Hamann, A., Stern, D., Brownlee, M., Bierhaus, A., Nawroth, P. and Morcos, M. (2009) C. elegans as model for the study of high glucose mediated lifespan reduction. Diabetes <strong>58<\/strong>, <strong>2450-2456<\/strong><strong> &nbsp;<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"210\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Karachalias, N., Babaei-Jadidi, R., Rabbani, N. and Thornalley, P.J. (2010) Protein glycation, oxidation and nitration in renal glomeruli, retina, nerve, plasma and urine of streptozotocin-induced diabetic rats and effect of thiamine and Benfotiamine therapy. Diabetologia <strong>53<\/strong>, 1506\u20131516<\/li>\n<\/ol>\n\n\n\n<ol start=\"211\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Varma Chittari, M., Bodmer, C.W., Zehnder, D., Ceriello, A. and Thornalley, P.J. (2010) Increased glycation and oxidative damage to apolipoprotein B100 of LDL in patients with type 2 diabetes and effect of metformin. Diabetes <strong>59<\/strong>, 1038 \u2013 1045<\/li>\n<\/ol>\n\n\n\n<ol start=\"212\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Santarius, T., Bignell, G., Greenman, C.D., Widaa, S., Chen, L., Mahoney, C.L. Butler, A., Edkins, S., Waris, S., Thornalley, P.J., Futreal, A. and Stratton, M.R. (2010) <em>GLO1-<\/em> a novel amplified gene in human cancer. Chromosome, Genes and Cancer <strong>49, 711-725<\/strong>&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"213\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J., Waris, S., Fleming, T., Santarius, T., Larkin, S.J., Winklhofer-Roob, B.M., Stratton, M.R. and Rabbani, N. (2010) Imidazopurinones are markers of physiological genomic damage linked to DNA instability and glyoxalase 1-associated tumour multidrug resistance. Nucleic Acids Res <strong>38<\/strong>, 5432-5442.<\/li>\n<\/ol>\n\n\n\n<ol start=\"214\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J and Rabbani, N. (2010) Oxidation modification of proteins: an overview. In: Biomarkers For Antioxidant Defense And Oxidative Damage Principles And Practical Applications (Aldini, G., Yeum, K.-J., Niki, E., and Russell, R.M. eds.), Wiley-Blackwell, New York, 137 \u2013 156.<\/li>\n<\/ol>\n\n\n\n<ol start=\"215\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J and Rabbani, N. (2010) Vitamin B6, B9 and B12 in diabetic nephropathy \u2013 beware. Nature Reviews in Endocrinology <strong>6<\/strong>, 477-478.<\/li>\n<\/ol>\n\n\n\n<ol start=\"216\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2010) Dicarbonyls in cola drinks sweetened with sucrose or high fructose corn syrup. Maillard Reaction: Interface Between Aging, Nutrition and Metabolism (Thomas, M. and Forbes, J. eds.), 158 \u2013 163.<\/li>\n<\/ol>\n\n\n\n<ol start=\"217\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) Protein damage in diabetes and uremia \u2013 identifying hotspots of proteome damage where minimal modification is amplified to marked pathophysiological effect. Free Radical Research <strong>45<\/strong>,&nbsp;89 \u2013 100.<\/li>\n<\/ol>\n\n\n\n<ol start=\"218\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J<strong>. <\/strong>and Rabbani, N. (2011) Thiamine in diabetic renal disease \u2013 dietary insufficiency, renal washout, anti-stress gene response, therapeutic supplements, risk predictor and link to genetic susceptibility. In: &#8216;Oxidative Stress in Applied Basic Research and Clinical Practice: Renal Disorders (Miyata, T., Eckardt, K.-U. and Nangaku, M. eds), Human Press, 93 \u2013 104.<\/li>\n<\/ol>\n\n\n\n<ol start=\"219\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Kurz, A., Rabbani, N., Walter, M., Bonin, M., Thornalley, P.J., Auburger, G. and Gispert, S. (2011) Alpha-synuclein deficiency leads to increased glyoxalase I expression and glycation stress. Cell and Molecular Life Sci. 68, 721 \u2013 733.<\/li>\n<\/ol>\n\n\n\n<ol start=\"220\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) The glyoxalase system \u2013 from microbial metabolism, through ageing to human disease and multidrug resistance.<strong> <\/strong>Seminars in Cell and Developmental Biology <strong>22<\/strong>,&nbsp; 261<\/li>\n<\/ol>\n\n\n\n<ol start=\"221\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Rabbani, N. and Thornalley, P.J. (2011) Glyoxalase in ageing.<em> <\/em>Seminars in Cell and Developmental Biology <strong>22<\/strong>, 293 &#8211; 301.<\/li>\n<\/ol>\n\n\n\n<ol start=\"222\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) Glyoxalase in tumourigenesis and multidrug resistance. Seminars in Cell and Developmental Biology <strong>22<\/strong>, 318 &#8211; 325.<\/li>\n<\/ol>\n\n\n\n<ol start=\"223\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) Glyoxalase in diabetes, obesity and related disorders. Seminars in Cell and Developmental Biology <strong>22<\/strong>, 309 &#8211; 317.<\/li>\n<\/ol>\n\n\n\n<ol start=\"224\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Murphy, M.P., Holmgren, Nils-G\u00f6ran Larsson, A., Halliwell, B., Chang, C.J., Kalyanaraman, B., Rhee, S.G., Thornalley, P.J., Partridge, L., Gems, D., Nystr\u00f6m, T., Belousov, V., Schumacker, P.T. and Winterbourn, C.C. (2011) Unravelling the Biological Roles of Reactive Oxygen Species. Cell Metabolism <strong>13<\/strong>, 361-366.<\/li>\n<\/ol>\n\n\n\n<ol start=\"225\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Kihm, L.P., M\u00fcller-Krebs, S., Klein, J., Ehrlich, G., Mertes, L., Gross, M.-L., Adaikalakoteswari, A. Thornalley, P.J. Hammes, H.-P., Nawroth, P., Zeier, M. and Schwenger, V. (2011) Benfotiamine Prevents Peritoneal Damage and Protects the Remnant Kidney in a PD Model in Uremic Rats. J Amer Soc Nephrol. <strong>22<\/strong>, 914 &#8211; 926.<\/li>\n<\/ol>\n\n\n\n<ol start=\"226\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) Emerging role of thiamine therapy for prevention and treatment of early stage diabetic nephropathy. Diabetes, Obesity and Metabolism <strong>13<\/strong>, 577 \u2013 583<\/li>\n<\/ol>\n\n\n\n<ol start=\"227\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Godfrey, L., Xue, M., Shaheen, F., Geoffrion, M., Milne, R. and Thornalley, P.J. (2011) Glycation of LDL by Methylglyoxal Increases Arterial Atherogenicity. A Possible Contributor to Increased Risk of Cardiovascular Disease in Diabetes. Diabetes <strong>60<\/strong>, 1973-1980 &nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"228\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J<strong>,<\/strong><strong> <\/strong>Xue, M.<strong> <\/strong>and Rabbani, N. (2011) Methodologies for <em>in-vitro<\/em> and <em>in-vivo<\/em> activity of bioactive compounds.<strong> <\/strong>In: Health-Promoting Properties of Fruits and Vegetables (Terry, L. ed.), CABI, Oxford, UK, 180 &#8211; 204.<\/li>\n<\/ol>\n\n\n\n<ol start=\"229\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2011) Methylglyoxal modification of LDL \u2013 pro-atherogenicity without oxidation opens new paths to prevention of cardiovascular disease. Clinical Lipidology <strong>6<\/strong>, 631-634.<\/li>\n<\/ol>\n\n\n\n<ol start=\"230\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2012) Dietary and synthetic activators of the antistress gene response in treatment of renal disease.&nbsp; J. Renal Nutrit. <strong>22<\/strong>, 195-202.<\/li>\n<\/ol>\n\n\n\n<ol start=\"231\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Rabbani, N., Momiji, H., Imbasi, P., Anwar, M.M., Kitteringham, N., Parks, B.K., Souma, T., Moriguchi, T., Yamamoto, M. and Thornalley, P.J. (2012) Transcriptional control of glyoxalase 1 by Nrf2 provides a stress responsive defence against dicarbonyl glycation. Biochem. J. <strong>443<\/strong>, 213 \u2013 222.<\/li>\n<\/ol>\n\n\n\n<ol start=\"232\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Adaikalakoteswari, A., Rabbani, N., Waspadji, S., Tjokroprawiro, A., Kariadi, H.K.S., Adam, J.M.F. and Thornalley, P.J. (2012) Disturbance of B-vitamin status in patients with type 2 diabetes in Indonesia \u2013 link to renal status, glycemic control and vascular inflammation. Diabetes Research &amp; Clinical Practice <strong>95<\/strong>, 415 \u2013 424.<\/li>\n<\/ol>\n\n\n\n<ol start=\"233\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2012) Amino Acids Glycation Section.<strong> <\/strong>Amino Acids <strong>42<\/strong>, 1085\u20131086<\/li>\n<\/ol>\n\n\n\n<ol start=\"234\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2012) Glycation research in Amino Acids \u2013 a place to call home.<strong> <\/strong>Amino Acids <strong>42<\/strong>, 1087\u20131096.<\/li>\n<\/ol>\n\n\n\n<ol start=\"235\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2012) Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino acids<strong> 42<\/strong>,<strong> <\/strong>1133-1142.<\/li>\n<\/ol>\n\n\n\n<ol start=\"236\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Adaikalakoteswari, A., Rossing, K., Rossing, P., Tarnow, L., Parving, H.-H. and Thornalley, P.J. (2012) Effect of Irbesartan treatment on plasma and urinary protein glycation, oxidation and nitration markers in patients with type 2 diabetes and microalbuminuria. Amino Acids <strong>42<\/strong>, 1627-1639<\/li>\n<\/ol>\n\n\n\n<ol start=\"237\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Bierhaus, A., Stoyanov, S., Fleming, T., Sauer, S.K., Leffler, A., Babes, A., Kichko, T.I., Neacsu, C., Konrade, I., Pirags, V., Lukic, I.K., Morcos, M., Dehmer, T., Rabbani, N., Thornalley, P.J., Edelstein, D., Nau, C., Forbes, J., Stern, D.M., Cooper, M.E, Humpert, P.M., Brownlee, M., Reeh, P. and Nawroth, P.P. (2012) Metabolic hyperalgesia \u2013 a novel concept based on the reactive metabolite methylglyoxal and the sensory neuronal Na<sup>+<\/sup> channel Na<sub>v<\/sub>1.8. Nature Medicine <strong>18, <\/strong>926\u2013933<\/li>\n<\/ol>\n\n\n\n<ol start=\"238\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Perkins, B.A., Rabbani, N., Weston, A., Ficociello, L.H., Antonysunil, A., Niewczas, M., Warram, J., Krolewski, A. and Thornalley, P.J. (2012) Plasma levels of advanced glycation endproducts and other markers of protein damage in type 1 diabetes patients with new onset microalbuminuria. PLOS One 7(4): e35655<\/li>\n<\/ol>\n\n\n\n<ol start=\"239\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2012) Dicarbonyls (Glyoxal, methylglyoxal, and 3-deoxyglucosone).<strong> <\/strong>In:&nbsp; Uremic Toxins (Niwa, T., Ed.) Wiley-Blackwell, 177 \u2013 192.<\/li>\n<\/ol>\n\n\n\n<ol start=\"240\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2012) Advanced glycation end-product (AGE)-modified proteins and peptides.<strong> <\/strong>In:&nbsp; Uremic Toxins (Niwa, T., Ed.) Wiley-Blackwell, 293 \u2013 304.<\/li>\n<\/ol>\n\n\n\n<ol start=\"241\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Abou Deif, O., Argiles, A., Drueke, T., Baurmeister, U., Beige, J., Brunet, P., Cohen, G., Fliser, D., Glorieux, G., Herget-Rosenthal, S., Jankowski, V., Jankowski, J., Massy, Z., Mischak, H., Ortiz, A., Perna, A., Rodriguez Portillo, J.M., Spasovski, G., Stegmayr, B., Stenvinkel, P., Thornalley, P., Vanholder, R., Wanner, C., Wiecek, A. (2012). Normal and pathologic concentrations of uremic toxins. J Amer Soc Nephrol 23, 1258-1270<\/li>\n<\/ol>\n\n\n\n<ol start=\"242\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Larkin, J.R., Zhang, F., Godfrey, L. Rabbani, N., Zehnder, D. and Thornalley, P.J. (2013) Down regulation of thiamine transporter expression in human kidney proximal tubular epithelial cells in hyperglycemia. PLOS One 7 (12), e53175<\/li>\n<\/ol>\n\n\n\n<ol start=\"243\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Lopez-Clavijo, A.F., Barrow, M.P., Rabbani, N., Thornalley, P.J. and&nbsp; O\u2019Connor, P.B. (2013) Determination of Types and Binding Sites of Advanced Glycation End Products for Substance P. Anal. Chem. 84, 10568 \u2013 10575<\/li>\n<\/ol>\n\n\n\n<ol start=\"244\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Klooster, A., Larkin, J.R., Wiersema-Buist, J., Gans, R.O.B., Thornalley, P.J., Navis, G., van Goor, H., Leuvenink, H.G.D. and Bakker, S.J.L. (2013)<strong> <\/strong>Are brain and heart tissue prone to the development of thiamine deficiency? Alcohol 47, 215 \u2013 221.<\/li>\n<\/ol>\n\n\n\n<ol start=\"245\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ajjan, R.A., Gamlen, T., Standeven, K.F., Mughal, S., Hess, K., Smith, K.A., Dunn, E.J., Phoenix, F., Anwar, M.M., Rabbani, N., Thornalley, P.J., Philippou, H. and Grant, P.J. (2013) Fructosamine modified plasminogen alters plasminogen-fibrin interactions and the specific activity of plasmin to inhibit fibrinolysis. Blood 122, 134 \u2013 142.<\/li>\n<\/ol>\n\n\n\n<ol start=\"246\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Fleming, T.H., Theilen, T.-M.,&nbsp;Masania, J., Wunderle, M., Karimi, J., Vittas, S., Bernauer, R., Bierhaus, A., Rabbani, N., Thornalley, P.J., Kroll, J., Tyedmers, J., Nawrotzki, R., Herzig, S., Brownlee, M. and Nawroth, P.P. (2013) Aging-dependent reduction in Glyoxalase-I delays wound healing.&nbsp; Gerontology 59, 427 \u2013 437<\/li>\n<\/ol>\n\n\n\n<ol start=\"247\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2014) Special edition of <em>Amino Acids<\/em> of selected papers from the eleventh international symposium on the Maillard reaction, September 16\u201320, 2012. Amino Acids 46, 259 \u2013 259.<\/li>\n<\/ol>\n\n\n\n<ol start=\"248\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Lopez-Clavijo, A.F., Duque-Daza, C.A., Romero Canelon, I., Barrow, M.P., Kilgour, D., Rabbani, N., Thornalley, P.J. and O\u2019Connor, P.B. (2014) Study of an Unusual Advanced Glycation End-Product (AGE) Derived from Glyoxal Using Mass Spectrometry. J. Amer. Soc. Mass Spectrometry 25, 673 \u2013 683.&nbsp;&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"249\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2014) Detection of oxidized and glycated proteins in clinical samples using mass spectrometry &#8211; a user&#8217;s perspective<strong>. <\/strong>Biochim. Biophys.<strong> <\/strong>Acta 1840, 818 \u2013 829.<\/li>\n<\/ol>\n\n\n\n<ol start=\"250\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2014) The critical role of methylglyoxal and glyoxalase 1 in diabetic nephropathy. Diabetes 63, 50 \u2013 52.<\/li>\n<\/ol>\n\n\n\n<ol start=\"251\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2014) Glyoxalase Centennial conference: introduction, history of research on the glyoxalase system and future prospects. Biochem. Soc. Trans. 42, 413 \u2013 418.<\/li>\n<\/ol>\n\n\n\n<ol start=\"252\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2014) Activity, regulation, copy number and function in the glyoxalase system. Biochem. Soc. Trans. 42, 419 \u2013 424.<\/li>\n<\/ol>\n\n\n\n<ol start=\"253\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Arai, M., Nihonmatsu-Kikuchi, N., Itokawa, M., Rabbani, N. and Thornalley, P.J. (2014) Measurement of glyoxalase activities. Biochem. Soc. Trans. 42, 491 \u2013 494.<\/li>\n<\/ol>\n\n\n\n<ol start=\"254\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Thornalley, P.J. and Rabbani, N. (2014) Assay of methylglyoxal and glyoxal and control of peroxidase interference. Biochem. Soc. Trans. 42, 504 \u2013 510.<\/li>\n<\/ol>\n\n\n\n<ol start=\"255\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Shaheen, F., Shmygol, A., Rabbani, N. and Thornalley, P.J. (2014) A fluorogenic assay for methylglyoxal. Biochem. Soc. Trans. 42, 548 \u2013 555.<\/li>\n<\/ol>\n\n\n\n<ol start=\"256\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Shaheen, F., Anwar, A., Masania, J. and Thornalley, P.J. (2014) Assay of methylglyoxal-derived protein and nucleotide advanced glycation endproducts. Biochem. Soc. Trans. 42, 511 \u2013 517<\/li>\n<\/ol>\n\n\n\n<ol start=\"257\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Shafie, A., Xue, M., Thornalley, P.J. and Rabbani, N. (2014) Copy number variation of Glyoxalase 1. Biochem. Soc. Trans. 42, 500 \u2013 503.<\/li>\n<\/ol>\n\n\n\n<ol start=\"258\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Rabbani, N. and Thornalley, P.J. (2014) Measurement of glyoxalase gene expression. Biochem. Soc. Trans. 42, 495 \u2013 499.<\/li>\n<\/ol>\n\n\n\n<ol start=\"259\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2014) Dicarbonyl proteome and genome damage in metabolic and vascular disease.<strong> <\/strong>Biochem. Soc. Trans. 42, 425 \u2013 432<strong><em>.<\/em><\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"260\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U.,<strong> <\/strong>Rabbani, N. and Thornalley, P.J. (2014) Possible role of methylglyoxal and glyoxalase in arthritis. Biochem. Soc. Trans. 42, 538 \u2013 542<strong>.<\/strong><\/li>\n<\/ol>\n\n\n\n<ol start=\"261\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Geoffrion, M., Du, X., Irshad, Z., Vanderhyden, B.C., Courville, K., Sui, G., D\u2019Agati, V.D., Ott-Braschi, S., Rabbani, N., Thornalley, P.J., Brownlee, M. and Milne, R.W. (2014) Differential effects of glyoxalase 1 over expression on diabetic atherosclerosis and renal dysfunction in streptozotocin-treated apolipoprotein E-deficient mice. Physiological Reports 2, e12043.<\/li>\n<\/ol>\n\n\n\n<ol start=\"262\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2014) Measurement of methylglyoxal by stable isotopic dilution analysis LC-MS\/MS with corroborative prediction in physiological samples. Nature Protocols <strong>9<\/strong>, 1969 \u2013 1979.<\/li>\n<\/ol>\n\n\n\n<ol start=\"263\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Godfrey, L., Yamada-Fowler, N., Thornalley, P.J. and Rabbani, N. (2014) Arginine-directed glycation and decreased HDL plasma concentration and functionality. Nutrition and Diabetes 4, e134.<\/li>\n<\/ol>\n\n\n\n<ol start=\"264\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani N. and Thornalley P.J. (2014) Glycation- and\/or Polyol Pathway-inducing Complications. Reference Module in Biomedical Sciences. Elsevier, 1 \u2013 7.<\/li>\n<\/ol>\n\n\n\n<ol start=\"265\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2015) The hidden complexities in measurement of fructosyl-lysine and advanced glycation endproducts for risk prediction of vascular complications of diabetes. Diabetes 64, 9 -11.&nbsp;<\/li>\n<\/ol>\n\n\n\n<ol start=\"266\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2015) Dicarbonyl stress in cell and tissue dysfunction contributing to ageing and disease. Biochem. Biophys. Res. Commun. 458, 221-226, 2015.<\/li>\n<\/ol>\n\n\n\n<ol start=\"267\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U., Savage, R.S., Anwar, M.M., Costa, M.L., Filer, A., Raza, K., Watts, R.A., Winyard, P.G., Tarr, J., Haigh, R.C., Thornalley, P.J. and Rabbani, N. (2015) Biomarker combination detects early-stage and discriminates osteoarthritis, rheumatoid arthritis and other inflammatory joint disease. Scientific Reports 5: 9259.<\/li>\n<\/ol>\n\n\n\n<ol start=\"268\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Waris, S., Winklhofer-Roob, B.M., Roob, J.M., Fuchs, S., Sourij, H., Rabbani, N. and Thornalley, P.J. (2015) Increased dicarbonyl glycation and oxidation adducts of deoxyguanosine in plasma and urine of patients with type 2 diabetes and link to diabetic nephropathy. J. Diabetes Res, 915486, 1 \u2013 10.<\/li>\n<\/ol>\n\n\n\n<ol start=\"269\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Duivenvoorde, L.P.M., van Schothorst, E. M., Derous, D., van der Stelt, I., Masania, J., Rabbani, N., Thornalley, P.J. and Keijer, J.&nbsp; (2015) Oxygen restriction as challenge test reveals early high-fat-diet-induced changes in glucose and lipid metabolism. Pflugers Arch &#8211; Eur J Physiol 467, 1179\u20131193.<\/li>\n<\/ol>\n\n\n\n<ol start=\"270\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Momiji, H., Rabbani, N., Bretschneider, T., Rand, D.A.<sup> <\/sup>and Thornalley, P.J. (2015) Frequency modulated translocational oscillations of Nrf2 &#8211; a transcription factor functioning like a wireless sensor. Biochem. Soc. Trans.43, 669\u2013673.<\/li>\n<\/ol>\n\n\n\n<ol start=\"271\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Momiji, H., Rabbani, N., Barker, G., Shmygol, A., Bretschneider, T., Rand, D.A.<sup> <\/sup>and Thornalley, P.J. (2015) Frequency modulated translocational oscillations of Nrf2 mediate the ARE cytoprotective transcriptional response. Antioxidants &amp; Redox Signalling 23, 613 &#8211; 629.<\/li>\n<\/ol>\n\n\n\n<ol start=\"272\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U., Thornalley, P.J. and Rabbani, N. (2015) Developing a plasma\/serum-based biochemical assay for diagnosing early-stage arthritis. Biomarkers in Medicine 9, 943 \u2013 945.<\/li>\n<\/ol>\n\n\n\n<ol start=\"273\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U., Thornalley, P.J. and Rabbani, N. (2015) Factors influencing the development and effectiveness of biomarkers in rheumatoid arthritis and osteoarthritis. Internat. J. Clin. Rheumatol. 10, 313\u2013316.<\/li>\n<\/ol>\n\n\n\n<ol start=\"274\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Zhang, F., Masania, J., Anwar, A., Xue, M., Zehnder, D., Kanji, H., Rabbani, N. and Thornalley, P.J. (2016) The uremic toxin oxythiamine causes functional thiamine de\ufb01ciency in end-stage renal disease by inhibiting transketolase activity. Kidney Internat. 90, 396 \u2013 403.<\/li>\n<\/ol>\n\n\n\n<ol start=\"275\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Weickert, M.O., Qureshi, S., Kandala, N.-B., Anwar, A., Waldron, M., Shafie, A., Messenger, D., Fowler, M., Jenkins, G., Rabbani, N.<sup> <\/sup>and Thornalley, P.J. (2016)<strong> <\/strong>Improved glycemic control and vascular function in overweight and obese subjects by glyoxalase 1 inducer formulation. Diabetes 65, 2282 \u2013 2294.<\/li>\n<\/ol>\n\n\n\n<ol start=\"276\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Masania, J., Malczewska-Malec, M., Razny, U., Goralska, J., Zdzienicka, A., Kiec-Wilk, B., Gruca, A., Stancel-Mozwillo, J., Dembinska-Kiec, A., Rabbani, N., Thornalley, P.J. (2016) Dicarbonyl stress in clinical obesity. Glycoconjugate J. 33, 581-589.<\/li>\n<\/ol>\n\n\n\n<ol start=\"277\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2016) Dicarbonyl and glyoxalase in disease mechanisms and clinical therapeutics. Glycoconjugate J. 33, 513 \u2013 525.<\/li>\n<\/ol>\n\n\n\n<ol start=\"278\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Ashour, A. and Thornalley, P.J. (2016) Mass spectrometric determination of advanced glycation in biology. Glycoconjugate J. 33, 553-568.<\/li>\n<\/ol>\n\n\n\n<ol start=\"279\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2016) Methylglyoxal-induced dicarbonyl stress in ageing and disease \u2013 first steps towards glyoxalase 1-based treatments. Clin. Sci. 130, 1677\u20131696.<\/li>\n<\/ol>\n\n\n\n<ol start=\"280\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2016) Glycation of proteins. In: Analysis of Post-Translational Modifications Using Mass Spectrometry (Griffiths, J.R. and Unwin, R.D., eds.), Wiley, Holboken, USA, 307-332.<\/li>\n<\/ol>\n\n\n\n<ol start=\"281\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ahmed, U., Anwar, A., Savage, R.S., Thornalley, P.J. and Rabbani, N. (2016) Application of protein glycation, oxidation and nitration for early-stage diagnosis and severity of osteoarthritis and other arthritic disease. Arthritis Research &amp; Therapy 18:250.<\/li>\n<\/ol>\n\n\n\n<ol start=\"282\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Shafie, A., Xue, M., Barker, G., Zehnder, D., Thornalley, P.J. and Rabbani, N. (2016) <strong>Re-appraisal of&nbsp;putative glyoxalase 1 deficient mouse and&nbsp;dicarbonyl stress on embryonic stem cells <\/strong><strong><em>in vitro<\/em><\/strong>. Biochem. J. 473, 4255\u20134270.<\/li>\n<\/ol>\n\n\n\n<ol start=\"283\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Anwar, A., Marini, M., Abruzzo, P.M., Bolotta, A., Ghezzo, A., Visconti, P., Thornalley, P.J.<sup> <\/sup>and Rabbani, N. (2016)<sup> <\/sup>Quantitation of plasma thiamine, related metabolites and plasma protein oxidative damage markers in children with autism spectrum disorder and healthy controls. Free Radical Res 50, S85\u2013S90.<\/li>\n<\/ol>\n\n\n\n<ol start=\"284\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Stratmann, B., Engelbrecht, B., Espelage, B.C., Klusmeier, N., Tiemann, J., Gawlowski, T.,&nbsp; Mattern, Y., Eisenacher, M., Meyer, H.E., Rabbani, N., Thornalley, P.J., Tschoepe, D., Poschmann, G. and St\u00fchler, K. (2016) Glyoxalase 1-knockdown in human aortic endothelial cells \u2013 effect on the proteome and endothelial function estimates. Scientific Reports 6, 37737.<\/li>\n<\/ol>\n\n\n\n<ol start=\"285\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Stratmann, B., Goldstein, B., Thornalley, P.J., Rabbani, N. and Tschoepe, D. (2017) Intracellular accumulation of methylglyoxal by glyoxalase 1 knock down alters collagen homoeostasis in L6 myoblasts. Internat. J. Molec. Sci. 18, 480 (1 \u2013 10).<\/li>\n<\/ol>\n\n\n\n<ol start=\"286\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rowan, S., Jiang, S., Korem, T., Szymanski, J., Chang, M.-L., Szelog, J., Cassalman, C., Dasuri, K., McGuire, C., Nagai, R., Du, X.-L., Brownlee, M., Rabbani, N., Thornalley, P.J., Baleja, J., Clish, C., Smith, D., Segal, E. and Taylor, A. (2017) Involvement of a gut-retina axis in protection against dietary glycemia induced age-related macular degeneration. Proc. Natl. Acad. Sci. USA 114, E4472\u2013E4481.<\/li>\n<\/ol>\n\n\n\n<ol start=\"287\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Shafie, A., Qaiser, T., Rajpoot, N.M., Kaltsas, G., James, S., Gopalakrishnan, K., Fisk, A., Dimitriadis, G.K., Grammatopoulos, D.K., Rabbani. N, Thornalley, P.J. and Weickert, M.O. (2017)<sup> <\/sup>Glyoxalase 1 copy number variation in patients with well differentiated gastro-entero-pancreatic neuroendocrine tumours (GEP-NET). Oncotarget 8, 76961\u201376973.<\/li>\n<\/ol>\n\n\n\n<ol start=\"288\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Razny, U., Goralska, J., Zdzienicka, A, Fedak, D., Masania, J., Rabbani, N., Thornalley, P.J., Pawlica-Gosiewska, D., Gawlik, K., Dembinska-Kiec, A., Solnica, B. and Malczewska-Malec, M. (2017) Relation of protein glycation, oxidation and nitration with osteocalcin level in obese subjects. Acta Biochim. Polon. 64, 415-422.<\/li>\n<\/ol>\n\n\n\n<ol start=\"289\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2018) Protein advanced glycation endproducts in the pathogenesis of chronic kidney disease. Kidney Internat. 93, 803\u2013813.<\/li>\n<\/ol>\n\n\n\n<ol start=\"290\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M., Weickert, M.O. and Thornalley, P.J. (2018) Multiple roles of glyoxalase 1-mediated suppression of methylglyoxal glycation in cancer biology&nbsp;\u2013 involvement in tumour suppression, tumour growth, multidrug resistance and target for chemotherapy. Seminars in Cancer Biology 49, 83 \u2013 93.<\/li>\n<\/ol>\n\n\n\n<ol start=\"291\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Anwar, A., Abruzzo, P.M., Pasha, S., Rajpoot, K., Bolotta, A., Ghezzo, A., Marini, M., Posar, A., Visconti, P., Thornalley, P.J.<sup> <\/sup>and Rabbani, N. (2018) Advanced glycation endproducts, dityrosine and arginine transporter dysfunction in autism &#8211; a source of biomarkers for clinical diagnosis. Molecular Autism 9: 3.<\/li>\n<\/ol>\n\n\n\n<ol start=\"292\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Spanos, C., Maldonado, E.M., Fisher, C.P., Leenutaphong, P., Oviedo-Orta, E., Windridge, D., Salguero, F.J., Berm\u00fadez-Fajardo, A., Weeks, M.E., Evans, C., Corfe, B.M., Rabbani, N., Thornalley, P.J., Miller, M.H., Wang, H., Dillon, J.F., Quaglia, A.,&nbsp; Dhawan, A., Fitzpatrick, E. and Moore, J.B. (2018) Proteomic identification and characterization of hepatic glyoxalase 1 dysregulation in non-alcoholic fatty liver disease. Proteome Science 16:4.<\/li>\n<\/ol>\n\n\n\n<ol start=\"293\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Chiu, C.-J., Rowan, S., Chang, M.-L., Sawyer, S., Hu, F., Willett, W., Rabbani, N., Thornalley, P.J., Bar, L., Kang, J.H. and Taylor, A. (2018) Studies of advanced glycation end products and oxidation biomarkers for type 2 diabetes. Biofactors 44, 281 \u2013 288.<\/li>\n<\/ol>\n\n\n\n<ol start=\"294\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Legrand, C., Ahmed, U., Anwar, A., Rajpoot, K., Pasha, S., Lambert, C., Davidson, R.K., Clark, I.M., Thornalley, P.J., Henrotin, Y. and Rabbani, N. (2018) Glycation marker glucosepane increases with the progression of osteoarthritis and correlates with morphological and functional changes of cartilage <em>in vivo<\/em>. Arthritis Res. Therap. 20: 131.<\/li>\n<\/ol>\n\n\n\n<ol start=\"295\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Hariton, F., Xue, M., Rabbani, N., Fowler, M. and Paul J Thornalley. (2018) Sulforaphane delays fibroblast senescence by curbing cellular glucose uptake, increased glycolysis and oxidative damage. Oxidative Medicine &amp; Longevity 2018, Article ID 5642148<\/li>\n<\/ol>\n\n\n\n<ol start=\"296\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2019) Glyoxalase 1 modulation in obesity and diabetes. Antioxidants and Redox Signalling 30, 354\u2013374.<\/li>\n<\/ol>\n\n\n\n<ol start=\"297\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2019) Autism Spectrum Disorders \u2013 in Search of Mechanistic Biomarkers. Autism and Developmental Disorders 17, 15 \u2013 23.<\/li>\n<\/ol>\n\n\n\n<ol start=\"298\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Irshad, Z.,<sup> <\/sup>Xue, M., Ashour, A., Larkin, J.R., Thornalley, P.J. and Rabbani, N. (2019) Activation of the unfolded protein response of endothelial cells in high glucose by methylglyoxal. Scientific Reports <strong>9<\/strong>, 7889.<\/li>\n<\/ol>\n\n\n\n<ol start=\"299\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2019) Hexokinase-2 glycolytic overload in diabetes and ischemia-reperfusion injury. Trends in Endocrinology &amp; Metabolism 30, 419 \u2013 431.<\/li>\n<\/ol>\n\n\n\n<ol start=\"300\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2019) Dicarbonyl stress and the glyoxalase system. In: Oxidative Stress: Eustress And Distress (Siess, H., ed.), Elsevier, San Diego, USA, pp. 759 \u2013 777.<\/li>\n<\/ol>\n\n\n\n<ol start=\"301\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Masania, J., Faustmann, G. , Anwar, A., Hafner-Giessauf, H., Rajpoot, N., Grabher, J., Rajpoot, K., Tiran, B., Obermayer-Pietsch, B., Winklhofer-Roob, B.M., Roob, J.M., and Rabbani, N.<sup> <\/sup>and Thornalley, P.J. (2019) Urinary metabolomic markers of protein glycation, oxidation and nitration in early-stage decline in metabolic, vascular and renal health. Oxidative Medicine &amp; Longevity 2019, Article ID 4851323.<\/li>\n<\/ol>\n\n\n\n<ol start=\"302\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., and Thornalley, P.J. (2020) Reading the patterns of proteome damage by glycation, oxidation and nitration &#8211; quantitation by stable isotopic dilution analysis LC-MS\/MS. Essays in Biochem 64, 169 \u2013 183<\/li>\n<\/ol>\n\n\n\n<ol start=\"303\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rowan, S., Jiang, S., Chang, M.-L., Volkin, J., Smith, K.M., Moreira-Neto, C., Rabbani, N., Thornalley, P.J., Smith, D.E., Waheed, N.K. and Taylor, A. (2020) A low glycemic diet protects disease-prone Nrf2-deficient mice against age-related macular degeneration. Free Radicals in Biology &amp; Medicine 150, 75\u201386.<\/li>\n<\/ol>\n\n\n\n<ol start=\"304\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Al-Motawa, M.S. and Thornalley, P. J. (2020) Protein glycation in plants \u2013 an under-researched field with much still to discover. Internat. J. Molec. Sci. 21, 3942.<\/li>\n<\/ol>\n\n\n\n<ol start=\"305\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Perkins, B.A., Rabbani, N., Weston, A., Antonysunil, A., Lee, JA, Lovblom, LE., Cardinez, N., Thornalley, P.J. (2020) Higher fractional excretion of glycation adducts is associated with subsequent early GFR decline in type 1 diabetes. Scientific Reports <strong>10,<\/strong> 12709<\/li>\n<\/ol>\n\n\n\n<ol start=\"306\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Feskens, E., Brennan, L., Dussort, P., Flourakis, M., Lindner, L.M.E., Mela, D., Rabbani, N., Rathmann, W., Respondek, F., Stehouwer, C., Theis, S., Thornalley, P.J., Vinoy, V. (2020) Potential markers of dietary glycemic exposures for sustained dietary interventions in populations without diabetes. Adv Nutr <strong>11<\/strong>, 1221\u20131236.<\/li>\n<\/ol>\n\n\n\n<ol start=\"307\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Al-Motawa, M.S., Abbas, H., Wijten, P., de la Fuente, A., Xue, M., Rabbani, N. and Thornalley, P.J. (2020) Vulnerabilities of the SARS-CoV-2 virus to proteotoxicity \u2013 opportunity for repurposed chemotherapy of COVID-19 infection. Frontiers in Pharmacology 11, Article 585408<\/li>\n<\/ol>\n\n\n\n<ol start=\"308\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ashour, A., Xue, M., Al-Motawa, M.S., Thornalley, P. J. and Rabbani, N. (2020) Glycolytic overload-driven dysfunction of periodontal ligament fibroblasts in high glucose concentration, corrected by glyoxalase 1 inducer. BMJ Open Diabetes Research &amp; Care. 8, e001458.<\/li>\n<\/ol>\n\n\n\n<ol start=\"309\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2021) Protein glycation \u2013 biomarkers of metabolic dysfunction and early-stage decline in health in the era of precision medicine. Redox Biology <strong>42<\/strong>, 101920.<\/li>\n<\/ol>\n\n\n\n<ol start=\"310\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2021) Dicarbonyl stress, protein glycation and the unfolded protein response. Glycoconjugate J. <strong>38<\/strong>, 331 \u2013 334.<\/li>\n<\/ol>\n\n\n\n<ol start=\"311\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M., Weickert, M.O. and Thornalley, P.J. (2021) Reversal of insulin resistance in overweight and obese subjects by <em>trans-<\/em>resveratrol and hesperetin combination \u2013 link to dysglycemia, blood pressure, dyslipidemia and low-grade inflammation.&nbsp; Nutrients <strong>13<\/strong>, 237.<\/li>\n<\/ol>\n\n\n\n<ol start=\"312\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Alhujaily,<sup> <\/sup>M., Abbas,<sup> <\/sup>H., Xue,<sup> <\/sup>M., de la Fuente, A., Rabbani,<sup> <\/sup>N. and Thornalley, P.J.&nbsp; (2021) Studies of glyoxalase 1-linked multidrug resistance reveal glycolysis-derived reactive metabolite, methylglyoxal, is a common contributor in cancer chemotherapy targeting the spliceosome. Frontiers in Oncol <strong>11<\/strong>, 748698<\/li>\n<\/ol>\n\n\n\n<ol start=\"313\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Xue, M. and Thornalley, P.J. (2022) Hexokinase-2-linked glycolytic overload and unscheduled glycolysis \u2013 driver of insulin resistance and development of vascular complications of diabetes. Internat J. Molec. Sci. 23, 2165.<\/li>\n<\/ol>\n\n\n\n<ol start=\"314\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2022) Emerging glycation-based therapeutics \u2013 glyoxalase 1 inducers and glyoxalase 1 inhibitors. Internat J. Molec. Sci. <em>23<\/em>, 2453<\/li>\n<\/ol>\n\n\n\n<ol start=\"315\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Aldous, E.K., Toor, S.M., Parray, A., Al-Sarraj, Y., Diboun, I., Abdelalim, E.,&nbsp; Arredouani, A., El-Agnaf, O., Thornalley, P.J., Akhtar, N., Pananchikkal, S.V., Shuaib, A., Alajez, N.M., Albagha, O.M.E. (2022) Identification of Novel Circulating miRNAs in Patients with Acute Ischemic Stroke. Internat J. Molec. Sci. 23 (6), 3387<\/li>\n<\/ol>\n\n\n\n<ol start=\"316\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Murphy, M.P., Bayir, H., Belousov, V., Chang, C.J., Davies, K.J.A., Davies, M.J., Dick, T.P., Finkel, T., Forman, H.J., Janssen-Heininger, Y., Gems, D., Kagan, V.E., Kalyanaraman, B., Larsson, N.-G., Milne, G.L., Nystr\u00f6m, T., Poulsen, H.E., Radi, R., Van Remmen, H., Schumacker, P.T., Thornalley, P.J., Toyokuni, S., Winterbourn, C.C., Yin, H. and Halliwell, B. (2022) CONSENSUS STATEMENT<strong> <\/strong>Guidelines for measuring reactive oxygen species and oxidative damage in cells and <em>in vivo<\/em>. Nature Metabolism&nbsp;<strong>4<\/strong>,&nbsp;651 \u2013 662<\/li>\n<\/ol>\n\n\n\n<ol start=\"317\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Toor, S.M., Aldous, E.K., Parray, A., Al-Sarraj, Y., Abdelalim, E.M., Arredouani, A., El-Agnaf, O., Thornalley, P.J., Akhtar, N., <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/?sort=date&amp;size=20&amp;term=Pananchikkal+SV&amp;cauthor_id=32353433\">Pananchikkal<\/a>, S.V., Shuaib, A., Alajez, N.M. and Albagha, O.M.E. (2022) Identification of distinct circulating microRNAs in acute ischemic stroke patients with type 2 diabetes mellitus. Front Cardiovasc Med 9: 1024790<\/li>\n<\/ol>\n\n\n\n<ol start=\"318\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N. and Thornalley, P.J. (2022) An Introduction to Special Issue &#8220;Protein Glycation in Food, Nutrition, Health and Disease&#8221;. Int J. Molec. Sci. 23, 13053.<\/li>\n<\/ol>\n\n\n\n<ol start=\"319\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Rabbani, N., Adaikalakoteswari, A., Larkin, J.R., Panagiotopoulos, S., MacIsaac, R.J., Yue, D.K., Fulcher, G.R., Roberts, M., Thomas, M., Ekinci, E. and Thornalley, P.J. (2023) Analysis of serum advanced glycation endproducts reveals methylglyoxal-derived advanced glycation MG-H1 free adduct is a risk marker in non-diabetic and diabetic chronic kidney disease. Internat. J. Molec. Sci. 24, 152.<\/li>\n<\/ol>\n\n\n\n<ol start=\"320\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Masania, J., Witjen, P., Keipert, S., Ost, M., Klaus, S., Rabbani, N. and Thornalley, P.J. (2023) Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle. Redox Biology 59, 102574<\/li>\n<\/ol>\n\n\n\n<ol start=\"321\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Toor, S.M., Aldous, E.K., Parray, A., Akhtar, N., Al-Sarraj, Y., Abdelalim, E.M., Arredouani, A., El-Agnaf, O., Thornalley, P.J., Pananchikkal, S.V., Pir, G.J., Kuni, R.A.T., Shuaib, A., Alajez, N.M. and Albagha, O.M.E. (2023) Circulating MicroRNA Profiling Identifies Distinct MicroRNA Signatures in Acute Ischemic Stroke and Transient Ischemic Attack Patients. Internat. J. Molec. Sci. 24, 108.<\/li>\n<\/ol>\n\n\n\n<ol start=\"322\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Ehtewish, H., Mesleh, A., Ponirakis, G., De la Fuente, A., Parray, A., Bensmail, I., Abdesselem, H., Ramadan, M., Khan, S., Chandran, M., Ayadathil, R., Elsotouhy, A., Own, A., Al Hamad, H., Abdelalim, E.M., Decock, J., Alajez, N.M., Albagha, O., Thornalley, P.J., Arredouani, A., Malik, R.A. and El-Agnaf, O.M.A. (2023) Blood-Based Proteomic Profiling Identifies Potential Biomarker Candidates and Pathogenic Pathways in Dementia. Internat. J. Molec. Sci. 24, 8117.<\/li>\n<\/ol>\n\n\n\n<ol start=\"323\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Islam, Z., Diane, A., Khattab, N., Dehbi, M., Thornalley, P.J. and Kolatkar, P.R. (2023) DNAJB3 attenuates ER stress through direct interaction with AKT. PLoS ONE 18(8): e0290340.<\/li>\n<\/ol>\n\n\n\n<ol start=\"324\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Nejat, S., Menikdiwela, K.R., Efotte, A., Scoggin, S., Vandanmagsar, B., Debi, M., Thornalley, P.J. and Moustaid-Moussa, N. (2023) &nbsp; Genetic deletion of DNAJB3 using CRISPR-Cas 9 produced discordant phenotypes. Genes 14, 1857.<\/li>\n<\/ol>\n\n\n\n<ol start=\"325\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Xue, M., Rabbani, N. and Thornalley, P.J. (2024) Increased cellular protein modification by methylglyoxal activates three sensors of the unfolded protein response. Redox Biol. 65, 103025.<\/li>\n<\/ol>\n\n\n\n<ol start=\"326\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Wada, O.Z., Rashid, N., Wijten, P., Thornalley, P.J., Mckay, G. and Mackey, H.R. Evaluation of cell disruption methods for protein and coenzyme Q10 quantification in purple non-sulfur bacteria. Front. Microbiol. 15: 1324099.<\/li>\n<\/ol>\n\n\n\n<ol start=\"327\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\">Al-Saei, A.N.J.M., Eldine, W.N., Rajpoot, K., Arshad, N., Al-Shammari, A.R., Kamal, M., Al-Shabeeb Akil, A., Fakhro, K.A., Thornalley, P.J. and Rabbani, N. (2023) Validation of plasma protein glycation and oxidation biomarkers for the diagnosis of autism<strong>. <\/strong>Molecular Psychiatry 29, 653 &#8211; 659.<\/li>\n<\/ol>\n\n\n\n<ol start=\"328\" class=\"wp-block-list\">\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/www.frontiersin.org\/journals\/endocrinology\/articles\/10.3389\/fendo.2023.1268308\/full\">Rabbani, N. and Thornalley, P.J. (2024) Hexokinase-linked glycolytic overload and unscheduled glycolysis in hyperglycemia-induced pathogenesis in insulin resistance, beta-cell glucotoxicity and diabetic vascular complications. Frontiers in Endocrinology 14, 1268303<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0168822724008155\" data-type=\"link\" data-id=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0168822724008155\">Rabbani, N. and Thornalley, P.J. (2024) Unraveling the impaired incretin effect in obesity and type 2 diabetes: key role of hyperglycemia-induced unscheduled glycolysis and glycolytic overload. Diabetes Res. Clin. Pract., 217, 111905<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/www.mdpi.com\/2076-3921\/14\/8\/956\" data-type=\"link\" data-id=\"https:\/\/www.mdpi.com\/2076-3921\/14\/8\/956\">Xue, M., Rabbani, N. and Thornalley, P.J. (2025) Glyoxalase 1 inducer, <em>trans<\/em>-resveratrol and hesperetin \u2013 dietary supplement with multi-modal health benefits. Antioxidants 14, 956.<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/www.mdpi.com\/2076-3921\/14\/8\/1022\" data-type=\"link\" data-id=\"https:\/\/www.mdpi.com\/2076-3921\/14\/8\/1022\">Wentzel, P., Xue, M., Rabbani, N., Eriksson, U.J. and Thornalley, P.J. (2025) Overload of glucose metabolism as initiating factor in diabetic embryopathy and prevention by dietary supplement. Antioxidants 14, 1022<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/www.mdpi.com\/2076-3921\/14\/10\/1146\" data-type=\"link\" data-id=\"https:\/\/www.mdpi.com\/2076-3921\/14\/10\/1146\">Al-Saei, A.N.J.M., Ahmed, U., Dickinson, E., Rajpoot, K., Xue, M., Abdelalim, E.M., Arredouani, A., Albagha, O.M.E., Griffin, D., Thornalley, P.J. and Rabbani, N. (2025) Plasma glycated and oxidized amino acid-based screening test for clinical early-stage osteoarthritis. Antioxidants 14, 1146.<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/oby.70063\">Nejat, S., Menikdiwela, K.R., Iskander, O., Scoggin, S., Zu, Y., Dufour, J., Chakroborty, A., Vandanmagsar, B., Thornalley, P.J., Dehbi, M., Kalupahana, N.S., and Moustaid-Moussa, N. (2025) DNAJB3 Deficiency in Mice, Sex-Dependently, Exacerbates High-fat Diet Induced Metabolic Dysfunctions. Obesity, <\/a><a href=\"https:\/\/doi.org\/10.1002\/oby.70063\">doi.org\/10.1002\/oby.70063<\/a><a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/oby.70063\">.<\/a><\/li>\n\n\n\n<li class=\"has-medium-font-size\"><a href=\"https:\/\/portlandpress.com\/clinsci\/article\/139\/21\/1405\/236741\/Molecular-mechanisms-of-metabolic-dysfunction\">Rabbani, N. and Thornalley, P.J. (2025) Molecular mechanisms of metabolic dysfunction-associated steatotic liver disease (MASLD): functional analysis of glucose and fructose metabolism pathways. Clinical Science 139, 1406 &#8211; 1429.<\/a><\/li>\n<\/ol>\n\n\n\n<p><\/p>\n\n\n\n<p><\/p>\n\n\n\n<p><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Peer-reviewed articles in journals and chapters in books<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"templates\/template-full.php","meta":{"footnotes":""},"class_list":["post-69","page","type-page","status-publish","hentry","post"],"_links":{"self":[{"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/pages\/69","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/comments?post=69"}],"version-history":[{"count":31,"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/pages\/69\/revisions"}],"predecessor-version":[{"id":2981,"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/pages\/69\/revisions\/2981"}],"wp:attachment":[{"href":"https:\/\/pjthornalley.com\/index.php\/wp-json\/wp\/v2\/media?parent=69"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}