{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T12:00:27Z","timestamp":1774785627291,"version":"3.50.1"},"reference-count":37,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[1998,2,1]],"date-time":"1998-02-01T00:00:00Z","timestamp":886291200000},"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":["Experimental Cell Research"],"published-print":{"date-parts":[[1998,2]]},"DOI":"10.1006\/excr.1997.3881","type":"journal-article","created":{"date-parts":[[2002,10,6]],"date-time":"2002-10-06T22:47:05Z","timestamp":1033944425000},"page":"23-30","source":"Crossref","is-referenced-by-count":3,"title":["Interaction of Heat Stress Glycoprotein GP50 with Classical Heat-Shock Proteins"],"prefix":"10.1006","volume":"239","author":[{"given":"Sunita M.","family":"Jethmalani","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kurt J.","family":"Henle","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/excr.1997.3881_EX973881RF1","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/355033a0","article-title":"Protein folding in the cell","volume":"355","author":"Gething","year":"1992","journal-title":"Nature"},{"key":"10.1006\/excr.1997.3881_EX973881RF2","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1146\/annurev.bi.62.070193.002025","article-title":"Molecular chaperone functions of heat-shock proteins","volume":"62","author":"Hendrick","year":"1993","journal-title":"Annu. Rev. Biochem."},{"key":"10.1006\/excr.1997.3881_EX973881RF3","series-title":"Thermotolerance","article-title":"Thermotolerance in cultured mammalian cells","author":"Henle","year":"1987"},{"key":"10.1006\/excr.1997.3881_EX973881RF4","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/j.1365-2184.1992.tb01484.x","article-title":"Relationship of heat shock proteins and induced thermal resistance","volume":"25","author":"Weber","year":"1992","journal-title":"Cell. Prolifer."},{"key":"10.1006\/excr.1997.3881_EX973881RF5","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1080\/09553008814551171","article-title":"Enhanced glycosylation of a 50 kD protein during thermotolerance development in CHO cells","volume":"53","author":"Henle","year":"1988","journal-title":"Int. J. Radiat. Biol."},{"key":"10.1006\/excr.1997.3881_EX973881RF6","first-page":"5717","article-title":"Effect of hyperthermia on the activity of three glycosyltransferases in CHO cells","volume":"48","author":"Henle","year":"1988","journal-title":"Cancer Res."},{"key":"10.1006\/excr.1997.3881_EX973881RF7","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/0014-4827(91)90249-T","article-title":"Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating","volume":"196","author":"Henle","year":"1991","journal-title":"Exp. Cell Res."},{"key":"10.1006\/excr.1997.3881_EX973881RF8","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1006\/excr.1993.1190","article-title":"Prompt protein glycosylation during acute heat stress","volume":"207","author":"Henle","year":"1993","journal-title":"Exp. Cell Res."},{"key":"10.1006\/excr.1997.3881_EX973881RF9","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1006\/excr.1994.1028","article-title":"Heat shock glycoprotein GP50: Product of the retinoic acid-inducible J6 gene","volume":"210","author":"Henle","year":"1994","journal-title":"Exp. Cell Res."},{"key":"10.1006\/excr.1997.3881_EX973881RF10","doi-asserted-by":"crossref","first-page":"191","DOI":"10.4052\/tigg.7.191","article-title":"Heat stress-induced protein glycosylation in mammalian cells","volume":"7","author":"Henle","year":"1995","journal-title":"Trends Glycosci. Glycotechnol."},{"key":"10.1006\/excr.1997.3881_EX973881RF11","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1006\/bbrc.1997.6215","article-title":"Protein glycosylation in a heat-resistant rat fibroblast cell model expressing human HSP70","volume":"232","author":"Henle","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1006\/excr.1997.3881_EX973881RF12","doi-asserted-by":"crossref","first-page":"15362","DOI":"10.1016\/S0021-9258(19)49542-2","article-title":"Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin","volume":"267","author":"Wang","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF13","doi-asserted-by":"crossref","first-page":"15818","DOI":"10.1016\/S0021-9258(18)55471-5","article-title":"A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue","volume":"265","author":"Wang","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF14","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1006\/excr.1997.3485","article-title":"Partial homology of stress glycoprotein GP62 with HSP70","volume":"232","author":"Jethmalani","year":"1997","journal-title":"Exp. Cell. Res."},{"key":"10.1006\/excr.1997.3881_EX973881RF15","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1002\/(SICI)1097-4644(19970701)66:1<98::AID-JCB11>3.0.CO;2-9","article-title":"Intracellular distribution of heat-induced stress glycoproteins","volume":"66","author":"Jethmalani","year":"1997","journal-title":"J. Cell. Biochem."},{"key":"10.1006\/excr.1997.3881_EX973881RF16","doi-asserted-by":"crossref","first-page":"17959","DOI":"10.1016\/S0021-9258(17)46798-6","article-title":"Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90)","volume":"268","author":"Margolese","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF17","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/370111a0","article-title":"Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones","volume":"370","author":"Frydman","year":"1994","journal-title":"Nature"},{"key":"10.1006\/excr.1997.3881_EX973881RF18","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/0014-5793(94)01417-Y","article-title":"Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant-type p53","volume":"358","author":"Sugito","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1006\/excr.1997.3881_EX973881RF19","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1038\/381571a0","article-title":"Molecular chaperones in cellular protein folding","volume":"381","author":"Hartl","year":"1996","journal-title":"Nature"},{"key":"10.1006\/excr.1997.3881_EX973881RF20","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0968-0004(94)90023-X","article-title":"Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones","volume":"19","author":"Jakob","year":"1994","journal-title":"Trends Biochem. Sci."},{"key":"10.1006\/excr.1997.3881_EX973881RF21","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/S0021-9258(18)53939-9","article-title":"ATP induces a conformational change of the 90-kDa heat shock protein (hsp90)","volume":"268","author":"Csermely","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF22","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev.ge.22.120188.003215","article-title":"The heat-shock proteins","volume":"22","author":"Lindquist","year":"1988","journal-title":"Annu. Rev. Genet."},{"key":"10.1006\/excr.1997.3881_EX973881RF23","doi-asserted-by":"crossref","first-page":"21303","DOI":"10.1016\/S0021-9258(19)36608-6","article-title":"The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains","volume":"267","author":"Melnick","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF24","doi-asserted-by":"crossref","first-page":"11155","DOI":"10.1016\/S0021-9258(19)78104-6","article-title":"Characterization of the protein\u2013protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex","volume":"269","author":"Czar","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF25","doi-asserted-by":"crossref","first-page":"6695","DOI":"10.1016\/S0021-9258(17)37431-8","article-title":"The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex","volume":"269","author":"Wartmann","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF26","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1021\/bi00454a028","article-title":"Direct stoichiometric evidence that the untransformed Mr","volume":"29","author":"Bresnick","year":"1990","journal-title":"Biochemistry"},{"key":"10.1006\/excr.1997.3881_EX973881RF27","doi-asserted-by":"crossref","first-page":"11803","DOI":"10.1016\/S0021-9258(18)60884-1","article-title":"The molybdate-stabilized nonactivated glucocorticoid receptor contains a dimer of Mr","volume":"262","author":"Denis","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF28","doi-asserted-by":"crossref","first-page":"6695","DOI":"10.1016\/S0021-9258(18)68698-3","article-title":"Isoform composition and stoichiometry of the approximately 90-kDa heat shock protein associated with glucocorticoid receptors","volume":"263","author":"Mendel","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF29","doi-asserted-by":"crossref","first-page":"17230","DOI":"10.1016\/S0021-9258(19)47363-8","article-title":"A collagen-binding protein in the endoplasmic reticulum of myoblasts exhibits relationship with serine protease inhibitors","volume":"266","author":"Clarke","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1006\/excr.1997.3881_EX973881RF30","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/0167-4781(92)90498-O","article-title":"Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins","volume":"1129","author":"Clarke","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1006\/excr.1997.3881_EX973881RF31","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1038\/332462a0","article-title":"The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins","volume":"332","author":"Kozutsumi","year":"1988","journal-title":"Nature"},{"key":"10.1006\/excr.1997.3881_EX973881RF32","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/333330a0","article-title":"Homologous plant and bacterial proteins chaperone oligomeric protein assembly","volume":"333","author":"Hemmingsen","year":"1988","journal-title":"Nature"},{"key":"10.1006\/excr.1997.3881_EX973881RF33","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1083\/jcb.117.3.505","article-title":"Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum","volume":"117","author":"Marquardt","year":"1992","journal-title":"J. Cell. Biol."},{"key":"10.1006\/excr.1997.3881_EX973881RF34","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1126\/science.274.5293.1715","article-title":"Chaperone function of Hsp90-associated proteins","volume":"274","author":"Bose","year":"1996","journal-title":"Science"},{"key":"10.1006\/excr.1997.3881_EX973881RF35","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1126\/science.274.5293.1718","article-title":"Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23","volume":"274","author":"Freeman","year":"1996","journal-title":"Science"},{"key":"10.1006\/excr.1997.3881_EX973881RF36","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1126\/science.274.5293.1713","article-title":"A cyclophilin function in Hsp90-dependent signal transduction","volume":"274","author":"Duina","year":"1996","journal-title":"Science"},{"key":"10.1006\/excr.1997.3881_EX973881RF37","doi-asserted-by":"crossref","first-page":"19509","DOI":"10.1074\/jbc.271.32.19509","article-title":"Efficient folding of firefly luciferase after transport into mammalian microsomes in the absence of luminal chaperones and folding catalysts","volume":"271","author":"Tyedmers","year":"1996","journal-title":"J. Biol. Chem."}],"container-title":["Experimental Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014482797938817?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014482797938817?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,3]],"date-time":"2021-05-03T06:18:17Z","timestamp":1620022697000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0014482797938817"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,2]]},"references-count":37,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1998,2]]}},"alternative-id":["S0014482797938817"],"URL":"https:\/\/doi.org\/10.1006\/excr.1997.3881","relation":{},"ISSN":["0014-4827"],"issn-type":[{"value":"0014-4827","type":"print"}],"subject":[],"published":{"date-parts":[[1998,2]]}}}