{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T22:26:27Z","timestamp":1780093587149,"version":"3.54.0"},"reference-count":179,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2003,8,1]],"date-time":"2003-08-01T00:00:00Z","timestamp":1059696000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2003,8,1]],"date-time":"2003-08-01T00:00:00Z","timestamp":1059696000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":3638,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemistry &amp; Biology"],"published-print":{"date-parts":[[2003,8]]},"DOI":"10.1016\/s1074-5521(03)00174-1","type":"journal-article","created":{"date-parts":[[2003,9,11]],"date-time":"2003-09-11T22:36:28Z","timestamp":1063319788000},"page":"677-693","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":449,"title":["Metal and Redox Modulation of Cysteine Protein Function"],"prefix":"10.1016","volume":"10","author":[{"given":"Niroshini M","family":"Giles","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron B","family":"Watts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory I","family":"Giles","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fiona H","family":"Fry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer A","family":"Littlechild","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claus","family":"Jacob","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/S1074-5521(03)00174-1_BIB1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0006-291X(02)02770-5","article-title":"Multiple roles of cysteine in biocatalysis","volume":"300","author":"Giles","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB2","series-title":"Cellular Implications of Redox Signalling","article-title":"Protein S-thiolation, S-nitrosylation, and irreversible sulfhydryl oxidation","author":"Thomas","year":"2003"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB3","doi-asserted-by":"crossref","first-page":"5606","DOI":"10.1016\/S0021-9258(18)91057-4","article-title":"Free-radical metabolites of L-cysteine oxidation","volume":"259","author":"Harman","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB4","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1515\/BC.2002.042","article-title":"Reactive sulfur species","volume":"383","author":"Giles","year":"2002","journal-title":"Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB5","article-title":"Sulfur and selenium","volume":"in press","author":"Jacob","year":"2003","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB6","series-title":"Bioinorganic Chemistry","article-title":"The bioinorganic chemistry of the quintessentially toxic metals","author":"Kaim","year":"1991"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB7","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1093\/oxfordjournals.jbchem.a002976","article-title":"New inhibitors of iron-containing nitrile hydratases","volume":"130","author":"Bonnet","year":"2001","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB8","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1021\/bi0016467","article-title":"Crystal structure of the all-ferrous 4Fe-4S (0) form of the nitrogenase iron protein from Azotobacter vinelandii","volume":"40","author":"Strop","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB9","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1126\/science.1061500","article-title":"Crystal structure of a carbon monoxide dehydrogenase reveals a Ni-4Fe-5S cluster","volume":"293","author":"Dobbek","year":"2001","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB10","doi-asserted-by":"crossref","first-page":"11628","DOI":"10.1021\/ja012645k","article-title":"Structural studies of the carbon monoxide complex of NiFe hydrogenase from Desulfovibrio vulgaris Miyazaki F","volume":"124","author":"Ogata","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB11","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1126\/science.282.5395.1853","article-title":"X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution","volume":"282","author":"Peters","year":"1998","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB12","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1126\/science.3945804","article-title":"Crystal structure of Cd,Zn metallothionein","volume":"231","author":"Furey","year":"1986","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB13","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1146\/annurev.biochem.71.110601.135406","article-title":"Great metalloclusters in enzymology","volume":"71","author":"Rees","year":"2002","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB14","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S1534-5807(02)00132-6","article-title":"Oxidants painting the cysteine chapel","volume":"2","author":"Xu","year":"2002","journal-title":"Dev. Cell"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB15","doi-asserted-by":"crossref","first-page":"5854","DOI":"10.1073\/pnas.100114897","article-title":"Structure and mechanism of mammalian thioredoxin reductase","volume":"97","author":"Zhong","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB16","doi-asserted-by":"crossref","first-page":"6102","DOI":"10.1046\/j.1432-1327.2000.01701.x","article-title":"Physiological functions of thioredoxin and thioredoxin reductase","volume":"267","author":"Arn\u00e9r","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB17","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0969-2126(01)00153-8","article-title":"Thioredoxin structure and mechanism","volume":"3","author":"Holmgren","year":"1995","journal-title":"Structure"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB18","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1016\/S0021-9258(18)33050-3","article-title":"The catalytic mechanism of glutathione-reductase as derived from X-ray-diffraction analyses of reaction intermediates","volume":"258","author":"Pai","year":"1983","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB19","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/35041687","article-title":"Oxidants, oxidative stress and the biology of ageing","volume":"408","author":"Finkel","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB20","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/S0014-5793(00)01669-0","article-title":"Redox-dependent signal transduction","volume":"476","author":"Finkel","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB21","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1002\/anie.198610581","article-title":"Biochemistry of oxidative stress","volume":"25","author":"Sies","year":"1986","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB22","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1016\/S0891-5849(01)00710-9","article-title":"Hypothesis","volume":"31","author":"Giles","year":"2001","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB23","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1179\/135100001101536427","article-title":"Regulatory roles of thioredoxin in oxidative stress-induced cellular responses","volume":"6","author":"Nishinaka","year":"2001","journal-title":"Redox Rep."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1365-2958.2002.02851.x","article-title":"Oxidative protein folding in bacteria","volume":"44","author":"Collet","year":"2002","journal-title":"Mol. Microbiol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB25","doi-asserted-by":"crossref","first-page":"31016","DOI":"10.1074\/jbc.273.47.31016","article-title":"Cysteinyl and substrate radical formation in active site mutant E441Q of Escherichia coli class I ribonucleotide reductase","volume":"273","author":"Persson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3460001","article-title":"Thioredoxin reductase","volume":"346","author":"Mustacich","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB27","doi-asserted-by":"crossref","first-page":"4801","DOI":"10.1021\/ac010126u","article-title":"Determination of metallothionein at the femtomole level by constant current stripping chronopotentiometry","volume":"73","author":"Kizek","year":"2001","journal-title":"Anal. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB28","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0022-0728(98)00344-1","article-title":"Electrochemical study of metallothioneins using cyclic voltammetry","volume":"458","author":"Harlyk","year":"1998","journal-title":"J. Electroanalytic. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB29","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/0302-4598(88)85010-4","article-title":"Electrochemical characterization of metallothionein metal mercaptide complexes\u2014application of cyclic voltammetry to investigation of metalloproteins","volume":"19","author":"Olafson","year":"1988","journal-title":"Bioelectrochemistry Bioenergetics"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB30","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1523409","article-title":"Oxidized redox state of glutathione in the endoplasmic reticulum","volume":"257","author":"Hwang","year":"1992","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB31","doi-asserted-by":"crossref","first-page":"4248","DOI":"10.1016\/S0021-9258(18)34713-6","article-title":"The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver","volume":"257","author":"Akerboom","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB32","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1016\/0024-3205(93)90019-Y","article-title":"Metallothionein-I reduction of cytochrome-C","volume":"53","author":"Simpkins","year":"1993","journal-title":"Life Sci."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB33","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1146\/annurev.bi.62.070193.004053","article-title":"Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions","volume":"62","author":"Stadtman","year":"1993","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB34","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1128\/JB.181.5.1636-1642.1999","article-title":"Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli","volume":"181","author":"Park","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB35","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1139\/y00-085","article-title":"Sulfur-centered reactive intermediates derived from the oxidation of sulfur compounds of biological interest","volume":"79","author":"Abedinzadeh","year":"2001","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB36","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1146\/annurev.biochem.70.1.209","article-title":"Divergent evolution of enzymatic function","volume":"70","author":"Gerlt","year":"2001","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB37","doi-asserted-by":"crossref","first-page":"6827","DOI":"10.1074\/jbc.271.12.6827","article-title":"The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681","volume":"271","author":"Sun","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB38","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1146\/annurev.biochem.70.1.121","article-title":"Radical mechanisms of enzymatic catalysis","volume":"70","author":"Frey","year":"2001","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB39","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/S0065-3233(01)58006-7","article-title":"Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation","volume":"58","author":"Claiborne","year":"2001","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB40","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1515\/BC.2002.040","article-title":"Peroxiredoxins","volume":"383","author":"Hofmann","year":"2002","journal-title":"Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB41","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/S0092-8674(02)01165-0","article-title":"How to flip the (redox) switch","volume":"111","author":"Georgiou","year":"2002","journal-title":"Cell"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB42","doi-asserted-by":"crossref","first-page":"10319","DOI":"10.1021\/bi000781g","article-title":"Oxidant-induced S-gutathiolation inactivates protein kinase C-alpha (PKC-alpha)","volume":"39","author":"Ward","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB43","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1042\/bj3470821","article-title":"Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue","volume":"347","author":"Reddy","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB44","doi-asserted-by":"crossref","first-page":"6638","DOI":"10.1016\/S0021-9258(18)83475-5","article-title":"Direct evidence for intramolecular and intermolecular disulfide bond formation in the human glucocorticoid receptor\u2014inhibition of DNA-binding and identification of a new receptor-associated protein","volume":"264","author":"Silva","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB45","doi-asserted-by":"crossref","first-page":"15857","DOI":"10.1074\/jbc.274.22.15857","article-title":"Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation","volume":"274","author":"Klatt","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB46","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1006\/bbrc.2000.2617","article-title":"Enhancement of S-nitrosylation in glycosylated hemoglobin","volume":"271","author":"Padron","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB47","doi-asserted-by":"crossref","first-page":"9427","DOI":"10.1074\/jbc.274.14.9427","article-title":"Nitric oxide induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase","volume":"274","author":"Mohr","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB48","doi-asserted-by":"crossref","first-page":"16186","DOI":"10.1021\/bi962043r","article-title":"Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc","volume":"35","author":"Gergel","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB49","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1006\/bbrc.2000.2117","article-title":"Inhibition of protein tyrosine phosphatases by low-molecular-weight S-nitrosothiols and S-nitrosylated human serum albumin","volume":"268","author":"Xian","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB50","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0304-3940(97)00780-5","article-title":"Suppression of neuronal apoptosis by S-nitrosylation of caspases","volume":"236","author":"Tenneti","year":"1997","journal-title":"Neurosci. Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB51","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1006\/abbi.1998.1013","article-title":"S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione","volume":"362","author":"Ji","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB52","first-page":"63","volume":"12","author":"Kong","year":"1998","journal-title":"Restor. Neurol. Neurosci."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB53","series-title":"Healthy Aging for Functional Longevity, Volume 928","article-title":"Protein oxidation in aging and age-related diseases","author":"Stadtman","year":"2001"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB54","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1016\/S0531-5565(01)00137-1","article-title":"Aging and oxidation of reactive protein sulfhydryls","volume":"36","author":"Thomas","year":"2001","journal-title":"Exp. Gerontol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB55","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0022-2836(02)00780-5","article-title":"The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators","volume":"322","author":"Somoza","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB56","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/S0014-4827(02)00055-1","article-title":"Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro","volume":"283","author":"Premzl","year":"2003","journal-title":"Exp. Cell Res."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB57","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/S1050-1738(01)00112-8","article-title":"The structure of calcium-free human m-calpain\u2014implications for calcium activation and function","volume":"11","author":"Reverter","year":"2001","journal-title":"Trends Cardiovasc. Med."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB58","series-title":"Comprehensive Biological Catalysis, Volume 2","article-title":"Cysteine proteinases","author":"Brocklehurst","year":"1998"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB59","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0969-2126(99)80053-7","article-title":"The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease","volume":"7","author":"Odagaki","year":"1999","journal-title":"Struct. Fold. Des."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB60","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1006\/jmbi.1999.3003","article-title":"Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus","volume":"291","author":"Isupov","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB61","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0969-2126(99)80034-3","article-title":"X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis","volume":"7","author":"Singleton","year":"1999","journal-title":"Struct. Fold. Des."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB62","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/S0092-8674(01)00274-4","article-title":"Structural basis for the inhibition of caspase-3 by XIAP","volume":"104","author":"Riedl","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB63","series-title":"Nitric Oxide","article-title":"Regulation of caspases by nitric oxide","author":"Kim","year":"2002"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB64","doi-asserted-by":"crossref","first-page":"12894","DOI":"10.1074\/jbc.M213125200","article-title":"Presentation of nitric oxide regulates monocyte survival through effects on caspase-9 and caspase-3 activation","volume":"278","author":"Zeigler","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB65","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1083\/jcb.200104008","article-title":"S-nitrosylation of mitochondrial caspases","volume":"154","author":"Mannick","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB66","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0969-2126(00)00090-3","article-title":"The atomic-resolution structure of a novel bacterial esterase","volume":"8","author":"Bourne","year":"2000","journal-title":"Struct. Fold. Des."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB67","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1016\/S0021-9258(19)50556-7","article-title":"Protein disulfide isomerase\u2014a multifunctional protein resident in the lumen of the endoplasmic-reticulum","volume":"267","author":"Noiva","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB68","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1515\/BC.2000.017","article-title":"Responses to peroxynitrite in yeast","volume":"381","author":"Buchczyk","year":"2000","journal-title":"Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB69","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1042\/bj20011882","article-title":"Reactive sulphur species","volume":"364","author":"Giles","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB70","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1096\/fasebj.7.15.8262333","article-title":"Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation","volume":"7","author":"Claiborne","year":"1993","journal-title":"FASEB J."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB71","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1016\/S0960-894X(99)00563-6","article-title":"Peroxides as oxidative enzyme inhibitors","volume":"9","author":"Dussault","year":"1999","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB72","doi-asserted-by":"crossref","first-page":"13574","DOI":"10.1021\/bi991028u","article-title":"Inhibition of cathepsin K by nitric oxide donors","volume":"38","author":"Percival","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB73","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0014-5793(97)01044-2","article-title":"Rabbit muscle GAPDH","volume":"414","author":"Schmalhausen","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB74","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0006-2952(99)00060-X","article-title":"Critical role of sulfenic acid formation of thiols in the inactivation of glyceraldehyde-3-phosphate dehydrogenase by nitric oxide","volume":"58","author":"Ishii","year":"1999","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB75","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/S0969-2126(00)00147-7","article-title":"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 angstrom resolution","volume":"8","author":"Schr\u00f6der","year":"2000","journal-title":"Struct. Fold. Des."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB76","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1021\/ja962994s","article-title":"Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent","volume":"119","author":"Goto","year":"1997","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB77","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1002\/hc.10068","article-title":"Synthesis of highly reactive organosulfur compounds","volume":"13","author":"Okazaki","year":"2002","journal-title":"Heteroatom Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB78","doi-asserted-by":"crossref","first-page":"12836","DOI":"10.1021\/ja962995k","article-title":"Synthesis of a stable sulfenic acid by oxidation of a sterically hindered thiol (thiophenetriptycene-8-thiol) and its characterization","volume":"118","author":"Ishii","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB79","doi-asserted-by":"crossref","first-page":"4349","DOI":"10.1016\/S0021-9258(19)45387-8","article-title":"Binding of substrate in a ternary complex of horse liver alcohol-dehydrogenase","volume":"257","author":"Eklund","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB80","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/S0009-2797(00)00262-3","article-title":"Ternary complexes of liver alcohol dehydrogenase","volume":"130","author":"Pocker","year":"2001","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB81","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1006\/bbrc.1998.9026","article-title":"Ebselen, a selenium-containing redox drug, releases zinc from metallothionein","volume":"248","author":"Jacob","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB82","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/0741-8329(93)90024-I","article-title":"Effect of diet and disulfiram on acetaldehyde blood levels after ethanol in Ucha and Uchb rats","volume":"10","author":"Quintanilla","year":"1993","journal-title":"Alcohol"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB83","doi-asserted-by":"crossref","first-page":"849","DOI":"10.12968\/hosp.2000.61.12.1483","article-title":"Disulfiram revisited","volume":"61","author":"O'Shea","year":"2000","journal-title":"Hosp. Med."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB84","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1096\/fasebj.12.12.1075","article-title":"Matrix metalloproteinases","volume":"12","author":"Massova","year":"1998","journal-title":"FASEB J."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB85","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1126\/science.1073634","article-title":"S-nitrosylation of matrix metalloproteinases","volume":"297","author":"Gu","year":"2002","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB86","doi-asserted-by":"crossref","first-page":"41279","DOI":"10.1074\/jbc.M106958200","article-title":"Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase","volume":"276","author":"Fu","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB87","doi-asserted-by":"crossref","first-page":"29596","DOI":"10.1074\/jbc.M102417200","article-title":"Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation","volume":"276","author":"Okamoto","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB88","doi-asserted-by":"crossref","first-page":"10082","DOI":"10.1021\/bi000952h","article-title":"Crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 angstrom\u2014inhibitor-induced conformational changes","volume":"39","author":"van Aalten","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB89","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/37995","article-title":"Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1","volume":"389","author":"Gomis-Ruth","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB90","doi-asserted-by":"crossref","first-page":"18530","DOI":"10.1074\/jbc.272.30.18530","article-title":"Zinc is a potent inhibitor of the apoptotic protease, caspase-3\u2014a novel target for zinc in the inhibition of apoptosis","volume":"272","author":"Perry","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB91","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1006\/taap.2001.9239","article-title":"Zinc inhibition of caspase-3 activation does not protect HeLa cells from apoptotic cell death","volume":"175","author":"Lambert","year":"2001","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB92","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1073\/pnas.96.5.1936","article-title":"Inhibitory sites in enzymes","volume":"96","author":"Maret","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB93","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/BF00436922","article-title":"Effects of zinc on macromolecular-synthesis and nuclear division during the yeast to mycelium transition in Sporothrix schenckii","volume":"106","author":"Rodriguez-del Valle","year":"1989","journal-title":"Mycopathologia"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB94","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S1096-4959(03)00051-4","article-title":"In vitro effect of metal ions on the activity of two amphibian glyceraldehyde-3-phosphate dehydrogenases","volume":"135","author":"Mounaji","year":"2003","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB95","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1074\/jbc.M007663200","article-title":"The molecular mechanism of lead inhibition of human porphobilinogen synthase","volume":"276","author":"Jaffe","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB96","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/S0014-5793(96)01412-3","article-title":"Inhibition of carboxypeptidase A by excess zinc","volume":"400","author":"Gomez-Ortiz","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB97","doi-asserted-by":"crossref","first-page":"9620","DOI":"10.1021\/bi00451a012","article-title":"Carboxypeptidase-A","volume":"28","author":"Larsen","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB98","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1021\/bi00224a007","article-title":"Characterization of an inhibitory metal-binding site in carboxypeptidase-A","volume":"30","author":"Larsen","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB99","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1073\/pnas.91.1.237","article-title":"Oxidative metal release from metallothionein via zinc thiol-disulfide interchange","volume":"91","author":"Maret","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB100","doi-asserted-by":"crossref","first-page":"12325","DOI":"10.1073\/pnas.231481398","article-title":"Crosstalk of the group IIa and IIb metals calcium and zinc in cellular signaling","volume":"98","author":"Maret","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB101","doi-asserted-by":"crossref","first-page":"8509","DOI":"10.1021\/bi00423a001","article-title":"Biochemistry of metallothionein","volume":"27","author":"K\u00e4gi","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB102","doi-asserted-by":"crossref","first-page":"4813","DOI":"10.1021\/ja01574a064","article-title":"A cadmium protein from equine kidney complex","volume":"79","author":"Margoshes","year":"1957","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB103","doi-asserted-by":"crossref","first-page":"8428","DOI":"10.1073\/pnas.95.15.8428","article-title":"The elusive function of metallothioneins","volume":"95","author":"Palmiter","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB104","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1007\/s00018-002-8454-2","article-title":"Metallothionein","volume":"59","author":"Coyle","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB105","doi-asserted-by":"crossref","first-page":"26389","DOI":"10.1074\/jbc.M200462200","article-title":"Functional characterization of a novel mammalian zinc transporter, ZnT6","volume":"277","author":"Huang","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB106","doi-asserted-by":"crossref","first-page":"4096","DOI":"10.1074\/jbc.M207644200","article-title":"ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus","volume":"278","author":"Kirschke","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB107","doi-asserted-by":"crossref","first-page":"323","DOI":"10.2174\/1389450033491082","article-title":"Zinc homeostasis-regulating proteins","volume":"4","author":"Chimienti","year":"2003","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB108","doi-asserted-by":"crossref","first-page":"19049","DOI":"10.1074\/jbc.M200910200","article-title":"Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells","volume":"277","author":"Kambe","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB109","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1093\/jn\/128.4.667","article-title":"Mammalian zinc transporters","volume":"128","author":"McMahon","year":"1998","journal-title":"J. Nutr."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB110","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/S0005-2736(00)00138-3","article-title":"The ZIP family of metal transporters","volume":"1465","author":"Guerinot","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB111","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1023\/A:1012988914300","article-title":"Eukaryotic zinc transporters and their regulation","volume":"14","author":"Gaither","year":"2001","journal-title":"Biometals"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB112","doi-asserted-by":"crossref","first-page":"2277","DOI":"10.1093\/nar\/23.12.2277","article-title":"Functional domains of the heavy metal-responsive transcription regulator Mtf-1","volume":"23","author":"Radtke","year":"1995","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB113","doi-asserted-by":"crossref","first-page":"11152","DOI":"10.1021\/bi980843r","article-title":"Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1","volume":"37","author":"Chen","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB114","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1128\/MCB.17.5.2781","article-title":"Reversible activation of mouse metal response element-binding transcription factor 1 DNA binding involves zinc interaction with the zinc finger domain","volume":"17","author":"Dalton","year":"1997","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB115","doi-asserted-by":"crossref","first-page":"9377","DOI":"10.1074\/jbc.275.13.9377","article-title":"Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1","volume":"275","author":"Smirnova","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB116","doi-asserted-by":"crossref","first-page":"30394","DOI":"10.1074\/jbc.M303598200","article-title":"Putative zinc-sensing zinc-fingers of metal response element-binding transcription factor-1 stabilize a metal-dependent chromatin complex on the endogenous metallothionein-I promoter","volume":"278","author":"Jiang","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB117","doi-asserted-by":"crossref","first-page":"42322","DOI":"10.1074\/jbc.M106517200","article-title":"Conformational heterogeneity in the C-terminal zinc finers of human MTF-1","volume":"276","author":"Giedroc","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB118","first-page":"213","article-title":"Spectroscopic properties of metallothionein","volume":"15","author":"Va\u0161\u00e1k","year":"1983","journal-title":"Met. Ions Biol. Syst."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB119","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1073\/pnas.95.7.3489","article-title":"Control of zinc transfer between thionein, metallothionein, and zinc proteins","volume":"95","author":"Jacob","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB120","doi-asserted-by":"crossref","first-page":"1460S","DOI":"10.1093\/jn\/133.5.1460S","article-title":"Cellular zinc and redox states converge in the metallothionein\/thionein pair","volume":"133","author":"Maret","year":"2003","journal-title":"J. Nutr."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB121","doi-asserted-by":"crossref","first-page":"5556","DOI":"10.1073\/pnas.101123298","article-title":"Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein","volume":"98","author":"Yang","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB122","doi-asserted-by":"crossref","first-page":"3478","DOI":"10.1073\/pnas.95.7.3478","article-title":"Thiolate ligands in metallothionein confer redox activity on zinc clusters","volume":"95","author":"Maret","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB123","first-page":"1269","article-title":"Refined crystal-structure of Cd, Zn metallothionein at 2.0 \u00c5 resolution","volume":"221","author":"Robbins","year":"1991","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB124","doi-asserted-by":"crossref","first-page":"6744","DOI":"10.1021\/bi00345a003","article-title":"Products of metal exchange-reactions of metallothionein","volume":"24","author":"Nettesheim","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB125","doi-asserted-by":"crossref","first-page":"3483","DOI":"10.1073\/pnas.95.7.3483","article-title":"The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase","volume":"95","author":"Jiang","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB126","doi-asserted-by":"crossref","first-page":"2233","DOI":"10.1073\/pnas.94.6.2233","article-title":"Coordination dynamics of biological zinc \u201cclusters\u201d in metallothioneins and in the DNA-binding domain of the transcription factor Gal4","volume":"94","author":"Maret","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB127","doi-asserted-by":"crossref","first-page":"9146","DOI":"10.1073\/pnas.95.16.9146","article-title":"The ATP-metallothionein complex","volume":"95","author":"Jiang","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB128","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1073\/pnas.96.5.1910","article-title":"Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes","volume":"96","author":"Jacob","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB129","first-page":"65","article-title":"Oxidation of biological thiols by highly reactive disulfide-S-oxides","volume":"21","author":"Giles","year":"2002","journal-title":"Gen. Physiol. Biophys."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB130","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/0891-5849(93)90029-T","article-title":"Oxygen free-radicals and metallothionein","volume":"14","author":"Sato","year":"1993","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB131","doi-asserted-by":"crossref","first-page":"3346","DOI":"10.1046\/j.1432-1327.2001.02250.x","article-title":"Catalytic selenols couple the redox cycles of metallothionein and glutathione","volume":"268","author":"Chen","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB132","series-title":"Redox Cell Biology and Genetics, Pt B, Volume 353","article-title":"Redox sensor function of metallothioneins","author":"Fabisiak","year":"2002"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB133","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1007\/s004380051088","article-title":"Heavy metal-mediated activation of the rat Cn\/Zn superoxide dismutase gene via a metal-responsive element","volume":"262","author":"Yoo","year":"1999","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB134","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0006-2952(99)00301-9","article-title":"Regulation of metallothionein gene expression by oxidative stress and metal ions","volume":"59","author":"Andrews","year":"2000","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB135","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1089\/15230860152542907","article-title":"Redox control of zinc finger proteins","volume":"3","author":"Lee","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB136","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1089\/15230860152542961","article-title":"Zinc binding and redox control of p53 structure and function","volume":"3","author":"Hainaut","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB137","doi-asserted-by":"crossref","first-page":"31963","DOI":"10.1074\/jbc.M004960200","article-title":"Structural characterization of the cysteine-rich domain of TFIIH p44 subunit","volume":"275","author":"Fribourg","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB138","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1089\/15230860152542989","article-title":"SAG\/ROC\/Rbx\/Hrt, a zinc RING finger gene family","volume":"3","author":"Sun","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB139","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1089\/15230860152542916","article-title":"Oxidation of zinc finger transcription factors","volume":"3","author":"Webster","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB140","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1128\/MCB.16.3.1035","article-title":"Physical and functional sensitivity of zinc finger transcription factors to redox change","volume":"16","author":"Wu","year":"1996","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB141","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1021\/jm970147+","article-title":"Zinc ejection as a new rationale for the use of cystamine and related disulfide-containing antiviral agents in the treatment of AIDS","volume":"40","author":"McDonnell","year":"1997","journal-title":"J. Med. Chem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB142","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.1110\/ps.52601","article-title":"Experimental determination and calculations of redox potential descriptors of compounds directed against retroviral zinc fingers","volume":"10","author":"Topol","year":"2001","journal-title":"Protein Sci."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB143","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1006\/bbrc.2001.5897","article-title":"Crystal structure of cobalt-containing nitrile hydratase","volume":"288","author":"Miyanaga","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB144","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/S1367-5931(99)80035-0","article-title":"Redox metals and neurodegenerative disease","volume":"3","author":"Sayre","year":"1999","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB145","series-title":"Environmental Stressors in Health and Disease","author":"Fuchs","year":"2001"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB146","series-title":"Oxidative Stress in Cancer, AIDS and Neurodegenerative Diseases","author":"Montagnier","year":"1998"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB147","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1023\/A:1015967305659","article-title":"In vivo measurement of tumor redox environment using EPR spectroscopy","volume":"234","author":"Ilangovan","year":"2002","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB148","first-page":"29","article-title":"Use of hypoxia-directed drugs in the therapy of solid tumors","volume":"19","author":"Rockwell","year":"1992","journal-title":"Semin. Oncol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB149","first-page":"461","article-title":"Enzyme-directed bioreductive drug development revisited","volume":"6","author":"Workman","year":"1994","journal-title":"Oncol. Res."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB150","first-page":"405","article-title":"Enzymology of mitomycin C metabolic activation in tumour tissue","volume":"56","author":"Cummings","year":"1998","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB151","first-page":"525","article-title":"Antioxidant enzyme levels in cancer","volume":"12","author":"Oberley","year":"1997","journal-title":"Histol. Histopathol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB152","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1002\/bies.10131","article-title":"Going malignant","volume":"24","author":"Hochachka","year":"2002","journal-title":"Bioessays"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB153","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0014-5793(02)03890-5","article-title":"Redox catalysts as sensitisers towards oxidative stress","volume":"535","author":"Giles","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB154","doi-asserted-by":"crossref","first-page":"2490","DOI":"10.1039\/b107972g","article-title":"Electrochemistry of chalcogen compounds","volume":"23","author":"Giles","year":"2001","journal-title":"Chem. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB155","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S0006-2952(97)00542-X","article-title":"Protection by organotellurium compounds against peroxynitrite-mediated oxidation and nitration reactions","volume":"55","author":"Briviba","year":"1998","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB156","doi-asserted-by":"crossref","first-page":"2030","DOI":"10.1039\/b302877a","article-title":"Electrochemical, in vitro and cell culture analysis of integrated redox catalysts","volume":"16","author":"Giles","year":"2003","journal-title":"Chem. Commun."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB157","doi-asserted-by":"crossref","first-page":"3116","DOI":"10.1001\/jama.287.23.3116","article-title":"Vitamins for chronic disease prevention in adults","volume":"287","author":"Fairfield","year":"2002","journal-title":"JAMA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB158","first-page":"10","article-title":"A review of vitamins A, C, and E and their relationship to cardiovascular disease","volume":"2","author":"Brown","year":"1998","journal-title":"Clin. Excell. Nurse Pract."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB159","first-page":"392","article-title":"Effects of fruits and vegetables on levels of vitamins E and C in the brain and their association with cognitive performance","volume":"6","author":"Martin","year":"2002","journal-title":"J. Nutr. Health Aging"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB160","first-page":"164","article-title":"The voltammetric behaviour of superoxide\/catalase mimics","volume":"2","author":"O'Hare","year":"2003","journal-title":"Electroanalysis"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB161","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/S1367-5931(99)00073-3","article-title":"Metals and neuroscience","volume":"4","author":"Bush","year":"2000","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB162","series-title":"Trace Element Medicine and Chelation Therapy","author":"Taylor","year":"1995"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB163","first-page":"219","article-title":"Conceptual and practical advances in the measurement and clinical management of lead toxicity","volume":"14","author":"Graziano","year":"1993","journal-title":"Neurotoxicology"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB164","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1046\/j.1442-200x.1999.01093.x","article-title":"Treatment and management of Wilson's disease","volume":"41","author":"Shimizu","year":"1999","journal-title":"Pediatr. Int."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB165","first-page":"456","article-title":"Mercury toxicity and antioxidants","volume":"7","author":"Patrick","year":"2002","journal-title":"Altern. Med. Rev."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB166","doi-asserted-by":"crossref","first-page":"553","DOI":"10.2165\/00002018-200326080-00003","article-title":"Benefits and risks of deferiprone in iron overload in thalassaemia and other conditions","volume":"26","author":"Kontoghiourghes","year":"2003","journal-title":"Drug Saf."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB167","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0006-8993(02)03893-3","article-title":"A novel trivalent cation chelator Feralex dissociates binding of aluminum and iron associated with hyperphosphorylated tau of Alzheimer's disease","volume":"961","author":"Shin","year":"2003","journal-title":"Brain Res."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB168","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/S0891-5849(02)00884-5","article-title":"A novel iron chelator that does not induce HIF-1 activity","volume":"33","author":"Creighton-Gutteridge","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB169","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0300-483X(98)00104-8","article-title":"Effects of N-acetylcysteine and 2,3-dimercaptosuccinic acid on lead induced oxidative stress in rat lenses","volume":"130","author":"Neal","year":"1998","journal-title":"Toxicology"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB170","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1097\/00001756-200008030-00029","article-title":"N-acetyl-L-cysteine improves survival and preserves motor performance in an animal model of familial amyotrophic lateral sclerosis","volume":"11","author":"Andreassen","year":"2000","journal-title":"Neuroreport"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB171","first-page":"931","article-title":"Essential viral and cellular zinc and iron containing metalloproteins as targets for novel antiviral and anticancer agents","volume":"21","author":"Fernandez-Pol","year":"2001","journal-title":"Anticancer Res."},{"key":"10.1016\/S1074-5521(03)00174-1_BIB172","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1126\/science.1063143","article-title":"Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion","volume":"294","author":"Ritz","year":"2001","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB173","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1126\/science.1080273","article-title":"Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation","volume":"300","author":"Woo","year":"2003","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB174","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1126\/science.1080405","article-title":"Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling","volume":"300","author":"Wood","year":"2003","journal-title":"Science"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB175","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0092-8674(01)00300-2","article-title":"Structural basis of the redox switch in the OxyR transcription factor","volume":"105","author":"Choi","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB176","series-title":"Generating and Displaying Molecules","author":"QUANTA2000","year":"1997"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB177","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1021\/bi00677a008","article-title":"Non-identical alkylation sites in rabbit muscle glyceraldehyde-3-phosphate dehyrodrogenase","volume":"14","author":"Bode","year":"1975","journal-title":"Biochemistry"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB178","doi-asserted-by":"crossref","first-page":"7414","DOI":"10.1073\/pnas.102185399","article-title":"Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2","volume":"99","author":"Morgunova","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1074-5521(03)00174-1_BIB179","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1093\/emboj\/17.17.5238","article-title":"Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor","volume":"17","author":"Fernandez-Catalan","year":"1998","journal-title":"EMBO J."}],"container-title":["Chemistry &amp; Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074552103001741?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074552103001741?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T06:58:17Z","timestamp":1761029897000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1074552103001741"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,8]]},"references-count":179,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2003,8]]}},"alternative-id":["S1074552103001741"],"URL":"https:\/\/doi.org\/10.1016\/s1074-5521(03)00174-1","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1006731.197159","asserted-by":"object"}]},"ISSN":["1074-5521"],"issn-type":[{"value":"1074-5521","type":"print"}],"subject":[],"published":{"date-parts":[[2003,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Metal and Redox Modulation of Cysteine Protein Function","name":"articletitle","label":"Article Title"},{"value":"Chemistry & Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/S1074-5521(03)00174-1","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2003 Cell Press. Published by Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}