{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T10:32:31Z","timestamp":1782901951420,"version":"3.54.5"},"reference-count":40,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[1992,6,1]],"date-time":"1992-06-01T00:00:00Z","timestamp":707356800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[1992,6,1]],"date-time":"1992-06-01T00:00:00Z","timestamp":707356800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2005,8,23]],"date-time":"2005-08-23T00:00:00Z","timestamp":1124755200000},"content-version":"vor","delay-in-days":4831,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[1992,6]]},"DOI":"10.1016\/0092-8674(92)90622-j","type":"journal-article","created":{"date-parts":[[2004,8,27]],"date-time":"2004-08-27T14:36:45Z","timestamp":1093617405000},"page":"1043-1050","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":412,"title":["A cytoplasmic chaperonin that catalyzes \u03b2-actin folding"],"prefix":"10.1016","volume":"69","author":[{"given":"Yijie","family":"Gao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John O.","family":"Thomas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert L.","family":"Chow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gwo-Hwa","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas J.","family":"Cowan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/0092-8674(92)90622-J_BIB1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0167-4781(90)90214-M","article-title":"Cloning of a Chinese hamster protein homologous to the mouse t-complex protein TCP-1: structural similarity to the ubiquitous \u2018chaperonin\u2019 family of heat shock proteins","volume":"1087","author":"Ahmed","year":"1990","journal-title":"Biochim. Biophys. Acts."},{"key":"10.1016\/0092-8674(92)90622-J_BIB2","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1139\/m89-031","article-title":"Gene organization and structure of two transcriptional units from Methanococcus coding for ribosomal proteins and elongation factors","volume":"35","author":"Auer","year":"1989","journal-title":"Canadian J. Microbiol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB3","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1038\/336254a0","article-title":"Transient association of newly synthesized unfolded proteins with the heat shock GroEL protein","volume":"336","author":"Bochkareva","year":"1988","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB4","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1749-6632.1987.tb40596.x","article-title":"The origin of eukaryotic and archaebacterial cells","volume":"503","author":"Cavalier-Smith","year":"1987","journal-title":"Ann. NY Aced. Sci."},{"key":"10.1016\/0092-8674(92)90622-J_BIB5","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1038\/337620a0","article-title":"Mitochondrial heat shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria","volume":"337","author":"Cheng","year":"1989","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB6","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/348455a0","article-title":"The mitochondrial chaperonin hsp60 is required for its own assembly","volume":"346","author":"Cheng","year":"1990","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB7","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/0092-8674(80)90238-X","article-title":"Numberand evolutionary conservation of \u03b1- and \u03b2-tubulin and cytoplasmic \u03b2- and \u03b3-actin genes using specific cloned cDNA probes","volume":"20","author":"Cleveland","year":"1980","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB8","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1038\/328378a0","article-title":"Proteins as molecular chaperones","volume":"328","author":"Ellis","year":"1987","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB9","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1126\/science.250.4983.954","article-title":"Molecular chaperones: the plant connection","volume":"250","author":"Ellis","year":"1990","journal-title":"Science"},{"key":"10.1016\/0092-8674(92)90622-J_BIB10","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1016\/0955-0674(91)90030-3","article-title":"Molecular chaperones: individualists or groupies?","volume":"3","author":"Gething","year":"1991","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB11","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":"10.1016\/0092-8674(92)90622-J_BIB12","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/0092-8674(86)90076-0","article-title":"Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport","volume":"46","author":"Gething","year":"1986","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB13","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1038\/337044a0","article-title":"GroE heat shock proteins promote assembly of foreign procaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli","volume":"337","author":"Goloubinoff","year":"1989","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB14","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/342884a0","article-title":"Reconstitution of active ribulose biphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP","volume":"342","author":"Goloubinoff","year":"1989","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB15","first-page":"833","article-title":"Sequence and structural homology between a mouse t-complex protein TCP-1 and the chaperonin family of bacterial (GroEL 65kDa heat-shock antigen) and eukaryotic proteins","volume":"20","author":"Gupta","year":"1990","journal-title":"Biochem. International"},{"key":"10.1016\/0092-8674(92)90622-J_BIB16","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":"10.1016\/0092-8674(92)90622-J_BIB17","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/0022-2836(79)90502-3","article-title":"Purification and properties of GroE, a host protein involved in bacteriophage assembly","volume":"129","author":"Hendrix","year":"1979","journal-title":"J. Mol. Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB18","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0022-2836(79)90501-1","article-title":"Isolation and characterization of the host protein GroE involved in bacteriophage lambda assembly","volume":"129","author":"John","year":"1979","journal-title":"J. Moll. Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB19","first-page":"1484","article-title":"Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora cressa mitochondria","volume":"8","author":"Hutchison","year":"1989","journal-title":"EMBO J."},{"key":"10.1016\/0092-8674(92)90622-J_BIB20","first-page":"9355","article-title":"Evolutionary relationship of archaebacteria, eubacteria, and eucaryotes inferred from phylogenetic trees of duplicated genes","volume":"86","author":"Iwabe","year":"1989"},{"key":"10.1016\/0092-8674(92)90622-J_BIB21","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/348137a0","article-title":"Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins","volume":"345","author":"Kang","year":"1990","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB22","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1152\/physrev.1982.62.2.672","article-title":"Actin polymerization","volume":"62","author":"Korn","year":"1982","journal-title":"Physiol. Rev."},{"key":"10.1016\/0092-8674(92)90622-J_BIB23","first-page":"4742","article-title":"Actin is the naturally occurring inhibitor of deoxyribonuclease I","volume":"71","author":"Lazarides","year":"1974"},{"key":"10.1016\/0092-8674(92)90622-J_BIB24","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/0300-9084(84)90147-0","article-title":"Actin purification from a gel of rat brain extracts","volume":"66","author":"Levilliers","year":"1984","journal-title":"Biochemie"},{"key":"10.1016\/0092-8674(92)90622-J_BIB25","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/352036a0","article-title":"Chaperonin mediated folding at the surface of GroEL through a \u2018molten globule\u2019-like intermediate","volume":"352","author":"Martin","year":"1991","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB26","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/0022-2836(90)90190-W","article-title":"Identification and characterization of a testis-specific isoform of a chaperonin in a moth, Heliothis virescens","volume":"214","author":"Miller","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB27","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/341125a0","article-title":"Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis","volume":"341","author":"Ostermann","year":"1989","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB28","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/0092-8674(86)90693-8","article-title":"Speculations on the functions of the major heat shock and glucose-regulated proteins","volume":"46","author":"Pelham","year":"1986","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB29","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1002\/j.1460-2075.1991.tb07695.x","article-title":"A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria","volume":"10","author":"Phipps","year":"1991","journal-title":"EMBO J."},{"key":"10.1016\/0092-8674(92)90622-J_BIB30","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/0092-8674(89)90005-6","article-title":"Polypeptide chain binding proteins: catalysis of protein folding and related processes in cells","volume":"59","author":"Rothman","year":"1989","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB31","article-title":"The transport of proteins into the nucleus requires the 70kDa heat shock protein or its cytoplasmic cognate","author":"Shi","year":"1992","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB32","first-page":"6077","article-title":"A major testicular cell protein specified by a mouse tT complex","volume":"77","author":"Silver","year":"1979"},{"key":"10.1016\/0092-8674(92)90622-J_BIB33","doi-asserted-by":"crossref","first-page":"4865","DOI":"10.1016\/S0021-9258(18)62016-2","article-title":"The regulation of rabbit skeletal muscle contraction","volume":"246","author":"Spudich","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0092-8674(92)90622-J_BIB34","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/0076-6879(90)85008-C","article-title":"Use of T7 RNA polymerase to direct expression of cloned genes","volume":"185","author":"Studier","year":"1990","journal-title":"Meth. Enzymol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB35","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1038\/354490a0","article-title":"A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1","volume":"354","author":"Trent","year":"1992","journal-title":"Nature"},{"key":"10.1016\/0092-8674(92)90622-J_BIB36","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/S0021-9258(18)48338-X","article-title":"Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring","volume":"267","author":"Viitanen","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0092-8674(92)90622-J_BIB37","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1083\/jcb.110.6.1885","article-title":"Loss of BiP\/GRP78 functions blocks translocation of secretory proteins in yeast","volume":"110","author":"Vogel","year":"1990","journal-title":"J. Cell Biol."},{"key":"10.1016\/0092-8674(92)90622-J_BIB38","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/0092-8674(86)90839-1","article-title":"Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1","volume":"44","author":"Willison","year":"1986","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB39","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/0092-8674(89)90131-1","article-title":"The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes.","volume":"57","author":"Willison","year":"1989","journal-title":"Cell"},{"key":"10.1016\/0092-8674(92)90622-J_BIB40","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1111\/j.1749-6632.1987.tb40599.x","article-title":"Eukaryotic traits in archaebacteria: could the eukaryotic cytoplasm have arisen from archaebacterial origin?","volume":"503","author":"Zillig","year":"1987","journal-title":"Ann. NY Aced. Sci."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:009286749290622J?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:009286749290622J?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,9]],"date-time":"2025-09-09T18:54:43Z","timestamp":1757444083000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/009286749290622J"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,6]]},"references-count":40,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1992,6]]}},"alternative-id":["009286749290622J"],"URL":"https:\/\/doi.org\/10.1016\/0092-8674(92)90622-j","relation":{},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[1992,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A cytoplasmic chaperonin that catalyzes \u03b2-actin folding","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/0092-8674(92)90622-J","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 1992","name":"copyright","label":"Copyright"}]}}