{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,8,19]],"date-time":"2023-08-19T05:02:54Z","timestamp":1692421374400},"reference-count":32,"publisher":"Elsevier BV","issue":"2-3","license":[{"start":{"date-parts":[[2002,5,1]],"date-time":"2002-05-01T00:00:00Z","timestamp":1020211200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2002,5]]},"DOI":"10.1016\/s0301-4622(02)00017-0","type":"journal-article","created":{"date-parts":[[2002,10,14]],"date-time":"2002-10-14T13:45:48Z","timestamp":1034603148000},"page":"259-271","source":"Crossref","is-referenced-by-count":5,"title":["Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase"],"prefix":"10.1016","volume":"96","author":[{"given":"Margrit","family":"Killenberg-Jabs","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gunther","family":"Kern","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerhard","family":"H\u00fcbner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ralph","family":"Golbik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0301-4622(02)00017-0_BIB1","first-page":"188","article-title":"Untersuchungen \u00fcber die Cocarboxylase","volume":"294","author":"Lohmann","year":"1937","journal-title":"Biochemische Zeitschrift"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB2","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1111\/j.1749-6632.1982.tb31185.x","article-title":"The amino group and steric factors in thiamin catalysis","volume":"378","author":"Schellenberger","year":"1982","journal-title":"Ann. N.Y. Acad. Sci."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB3","doi-asserted-by":"crossref","first-page":"8726","DOI":"10.1021\/bi00152a007","article-title":"Synchrotron radiation solution X-ray scattering study of the pH dependence of the quaternary structure of yeast pyruvate decarboxylase","volume":"31","author":"K\u00f6nig","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB4","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1007\/BF00185779","article-title":"The influence of the effectors of yeast pyruvate decarboxylase (PDC) on the conformation of the dimers and tetramers and their pH-dependent equilibrium","volume":"22","author":"K\u00f6nig","year":"1993","journal-title":"Euro. Biophys. J."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB5","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/j.1432-1033.1980.tb04869.x","article-title":"Hydroxyl-ion-induced subunit dissociation of yeast cytoplasmatic pyruvate decarboxylase","volume":"110","author":"Hopmann","year":"1980","journal-title":"Euro. J. Bioc."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB6","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/S0926-6593(66)80017-6","article-title":"Molecular weight and coenzyme content of pyruvate decarboxylase from brewer's yeast","volume":"113","author":"Ullrich","year":"1966","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB7","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1006\/jmbi.1996.0111","article-title":"Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution","volume":"256","author":"Arjunan","year":"1996","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB8","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/0005-2795(75)90114-2","article-title":"Pyruvate decarboxylase III: specificity restriction for thiamine pyrophosphate in the protein association step; subunit structure","volume":"405","author":"Gounaris","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB9","doi-asserted-by":"crossref","first-page":"17413","DOI":"10.1016\/S0021-9258(18)38175-4","article-title":"Preliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers\u2019 yeast","volume":"265","author":"Dyda","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB10","doi-asserted-by":"crossref","first-page":"6165","DOI":"10.1021\/bi00075a008","article-title":"Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-\u00c5 resolution","volume":"32","author":"Dyda","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB11","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/0959-440X(93)90153-C","article-title":"Thiamin diphosphate dependent enzymes: transketolase, pyruvate oxidase and pyruvate decarboxylase","volume":"3","author":"Lindqvist","year":"1993","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB12","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1002\/j.1460-2075.1992.tb05301.x","article-title":"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 \u00c5 resolution","volume":"11","author":"Lindqvist","year":"1992","journal-title":"EMBO J."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB13","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/0969-2126(93)90025-C","article-title":"A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase","volume":"1","author":"Muller","year":"1993","journal-title":"Structure"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB14","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1002\/ange.19670792303","article-title":"Struktur und Wirkungsweise des aktiven Zentrums der Hefe-Pyruvatdecarboxylase","volume":"79","author":"Schellenberger","year":"1967","journal-title":"Angewandte Chemie"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB15","doi-asserted-by":"crossref","first-page":"3491","DOI":"10.1021\/ja00452a050","article-title":"Ring stacking interactions between thiamin and planar molecules as seen in the crystal structure of a picronolate dihydrate complex","volume":"99","author":"Shin","year":"1977","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB16","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1046\/j.1432-1327.2001.02044.x","article-title":"Active oligomeric states of pyruvate decarboxylase and their functional characterization","volume":"268","author":"Killenberg-Jabs","year":"2001","journal-title":"Euro. J. Biochem."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB17","series-title":"Folding and Unfolding of Homotetrameric Pyruvate Decarboxylase from S. cerevisiae","first-page":"195","article-title":"Biochemistry and physiology of thiamin diphosphate enzymes","author":"Killenberg-Jabs","year":"1996"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB18","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0079-6107(87)90011-3","article-title":"Folding and association of proteins","volume":"49","author":"Jaenicke","year":"1987","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB19","first-page":"206","article-title":"Protein stability and protein folding","volume":"161","author":"Jaenicke","year":"1991","journal-title":"Ciba Found. Symp."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB20","series-title":"Folding of Large Proteins: Multidomain and Multisubunit Proteins","first-page":"405","article-title":"Protein folding","author":"Garel","year":"1992"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB21","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1021\/bi961341l","article-title":"Role of Glu51 for cofactor binding and catalytic activity in pyruvate decarboxylase from yeast studied by site-directed mutagenesis","volume":"36","author":"Killenberg-Jabs","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB22","series-title":"Ph.D. thesis, Martin-Luther-Universit\u00e4t Halle-Wittenberg","author":"Killenberg-Jabs","year":"1997"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB23","first-page":"331","article-title":"Isolierung der Hefecarboxylase und Untersuchung \u00fcber die Aktivit\u00e4t des Enzyms in lebenden Zellen","volume":"327","author":"Holzer","year":"1956","journal-title":"Biochemische Zeitschrift"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB24","doi-asserted-by":"crossref","first-page":"8069","DOI":"10.1021\/bi00421a015","article-title":"Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of \u0394G(N\u2212U) values in a thermodynamic cycle","volume":"27","author":"Bolen","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB25","doi-asserted-by":"crossref","first-page":"8063","DOI":"10.1021\/bi00421a014","article-title":"Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants","volume":"27","author":"Santoro","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB26","doi-asserted-by":"crossref","first-page":"4322","DOI":"10.1021\/bi00067a022","article-title":"Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation","volume":"32","author":"Clarke","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB27","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1110\/ps.8.7.1505","article-title":"Folding of barstar C40A\/C82A\/P27A and catalysis of the peptidyl\u2013prolyl cis\/trans isomerization by human cytosolic cyclophilin (Cyp18)","volume":"8","author":"Golbik","year":"1999","journal-title":"Prot. Sci."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB28","doi-asserted-by":"crossref","first-page":"10428","DOI":"10.1021\/bi00107a010","article-title":"Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition","volume":"30","author":"Jackson","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB29","series-title":"Ultraviolet Spectroscopy of Proteins","author":"Demchenko","year":"1986"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB30","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/S0006-3495(94)80799-4","article-title":"The use of fluorescence methods to monitor unfolding transitions in proteins","volume":"66","author":"Eftink","year":"1994","journal-title":"Biophys. J."},{"key":"10.1016\/S0301-4622(02)00017-0_BIB31","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1515\/bchm3.1993.374.7-12.1129","article-title":"Effects of metal ions, thiamine diphosphate analogues and subunit interactions on the reconstitution behaviour of pyruvate decarboxylase from brewer's yeast","volume":"374","author":"Eppendorfer","year":"1993","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"10.1016\/S0301-4622(02)00017-0_BIB32","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1096\/fasebj.10.1.8566550","article-title":"Thermodynamics of denaturation of staphylococcal nuclease mutants: an intermediate state in protein folding","volume":"10","author":"Carra","year":"1996","journal-title":"FASEB J."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462202000170?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462202000170?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,4]],"date-time":"2021-05-04T01:39:53Z","timestamp":1620092393000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462202000170"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,5]]},"references-count":32,"journal-issue":{"issue":"2-3","published-print":{"date-parts":[[2002,5]]}},"alternative-id":["S0301462202000170"],"URL":"https:\/\/doi.org\/10.1016\/s0301-4622(02)00017-0","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2002,5]]}}}