{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T14:05:22Z","timestamp":1790431522135,"version":"4.1.0"},"reference-count":63,"publisher":"Elsevier BV","issue":"32","license":[{"start":{"date-parts":[[2019,8,1]],"date-time":"2019-08-01T00:00:00Z","timestamp":1564617600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,31]],"date-time":"2020-08-31T00:00:00Z","timestamp":1598832000000},"content-version":"vor","delay-in-days":396,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID)","doi-asserted-by":"publisher","award":["R01AI099493"],"award-info":[{"award-number":["R01AI099493"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2019,8]]},"DOI":"10.1074\/jbc.ra119.008568","type":"journal-article","created":{"date-parts":[[2019,6,20]],"date-time":"2019-06-20T22:45:13Z","timestamp":1561070713000},"page":"12122-12131","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"title":["HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol"],"prefix":"10.1016","volume":"294","author":[{"given":"Helen","family":"Burress","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alisha","family":"Kellner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica","family":"Guyette","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suren A.","family":"Tatulian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4176-9361","authenticated-orcid":false,"given":"Ken","family":"Teter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA119.008568_bib1","series-title":"The Comprehensive Sourcebook of Bacterial Protein Toxins","first-page":"195","article-title":"Vibrio cholerae and Escherichia coli heat-labile enterotoxins and beyond","author":"Heggelund","year":"2015"},{"key":"10.1074\/jbc.RA119.008568_bib2","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1083\/jcb.201108103","article-title":"Identification of host cell factors required for intoxication through use of modified cholera toxin","volume":"195","author":"Guimaraes","year":"2011","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA119.008568_bib3","doi-asserted-by":"crossref","first-page":"2941","DOI":"10.1172\/JCI116917","article-title":"Entry of cholera toxin into polarized human intestinal epithelial cells: identification of an early brefeldin A-sensitive event required for A1-peptide generation","volume":"92","author":"Lencer","year":"1993","journal-title":"J. Clin. Invest"},{"key":"10.1074\/jbc.RA119.008568_bib4","doi-asserted-by":"crossref","first-page":"12010","DOI":"10.1016\/S0021-9258(19)50301-5","article-title":"Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action","volume":"268","author":"Orlandi","year":"1993","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib5","doi-asserted-by":"crossref","first-page":"e1003925","DOI":"10.1371\/journal.ppat.1003925","article-title":"Substrate-induced unfolding of protein-disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin","volume":"10","author":"Taylor","year":"2014","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.RA119.008568_bib6","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1016\/S0092-8674(01)00289-6","article-title":"Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin","volume":"104","author":"Tsai","year":"2001","journal-title":"Cell"},{"key":"10.1074\/jbc.RA119.008568_bib7","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1016\/j.jmb.2007.10.025","article-title":"Conformational instability of the cholera toxin A1 polypeptide","volume":"374","author":"Pande","year":"2007","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.008568_bib8","doi-asserted-by":"crossref","first-page":"6172","DOI":"10.1128\/IAI.70.11.6172-6179.2002","article-title":"Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin","volume":"70","author":"Teter","year":"2002","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib9","series-title":"Moonlighting Cell Stress Proteins in Microbial Infections","first-page":"323","article-title":"Cholera toxin interactions with host cell stress proteins","author":"Teter","year":"2013"},{"key":"10.1074\/jbc.RA119.008568_bib10","doi-asserted-by":"crossref","first-page":"11051","DOI":"10.1021\/bi971383p","article-title":"Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells","volume":"36","author":"Hazes","year":"1997","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA119.008568_bib11","doi-asserted-by":"crossref","first-page":"1222","DOI":"10.1093\/embo-reports\/kvf239","article-title":"Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation","volume":"3","author":"Rodighiero","year":"2002","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.RA119.008568_bib12","doi-asserted-by":"crossref","first-page":"781","DOI":"10.4155\/fmc.13.42","article-title":"Cholera: pathophysiology and emerging therapeutic targets","volume":"5","author":"Muanprasat","year":"2013","journal-title":"Future Med. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib13","doi-asserted-by":"crossref","first-page":"997","DOI":"10.3390\/biom3040997","article-title":"Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol","volume":"3","author":"Teter","year":"2013","journal-title":"Biomolecules"},{"key":"10.1074\/jbc.RA119.008568_bib14","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.bbamcr.2011.09.002","article-title":"The Cdc48 machine in endoplasmic reticulum associated protein degradation","volume":"1823","author":"Wolf","year":"2012","journal-title":"Biochim. Biophys Acta"},{"key":"10.1074\/jbc.RA119.008568_bib15","doi-asserted-by":"crossref","first-page":"28127","DOI":"10.1074\/jbc.M503138200","article-title":"Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate","volume":"280","author":"Kothe","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib16","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/j.bbrc.2007.02.077","article-title":"Ufd1-Npl4 is a negative regulator of cholera toxin retrotranslocation","volume":"355","author":"McConnell","year":"2007","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA119.008568_bib17","doi-asserted-by":"crossref","first-page":"31261","DOI":"10.1074\/jbc.M110.148981","article-title":"Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol","volume":"285","author":"Taylor","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib18","doi-asserted-by":"crossref","first-page":"33644","DOI":"10.1074\/jbc.M114.609800","article-title":"Co- and post-translocation roles for Hsp90 in cholera intoxication","volume":"289","author":"Burress","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib19","doi-asserted-by":"crossref","first-page":"4557","DOI":"10.1038\/sj.emboj.7601307","article-title":"p97 functions as an auxiliary factor to facilitate TM domain extraction during CFTR ER-associated degradation","volume":"25","author":"Carlson","year":"2006","journal-title":"EMBO J"},{"key":"10.1074\/jbc.RA119.008568_bib20","doi-asserted-by":"crossref","first-page":"4606","DOI":"10.1091\/mbc.e06-05-0432","article-title":"Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells","volume":"17","author":"W\u00f3jcik","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA119.008568_bib21","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1083\/jcb.200210028","article-title":"The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex","volume":"160","author":"Ratts","year":"2003","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA119.008568_bib22","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41598-017-00780-x","article-title":"The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells","volume":"7","author":"Schuster","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA119.008568_bib23","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1128\/IAI.72.5.3066-3068.2004","article-title":"The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary \u03b9-like toxins","volume":"72","author":"Haug","year":"2004","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib24","doi-asserted-by":"crossref","first-page":"32266","DOI":"10.1074\/jbc.M303980200","article-title":"The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol","volume":"278","author":"Haug","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib25","doi-asserted-by":"crossref","first-page":"3913","DOI":"10.1128\/IAI.05372-11","article-title":"Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90","volume":"79","author":"Kaiser","year":"2011","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib26","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1111\/cmi.12228","article-title":"The chaperone Hsp90 and PPIases of the cyclophilin and FKBP families facilitate membrane translocation of Photorhabdus luminescens ADP-ribosyltransferases","volume":"16","author":"Lang","year":"2014","journal-title":"Cell Microbiol"},{"key":"10.1074\/jbc.RA119.008568_bib27","doi-asserted-by":"crossref","first-page":"106","DOI":"10.4103\/2319-4170.113230","article-title":"Structure, function, and regulation of the Hsp90 machinery","volume":"36","author":"Li","year":"2013","journal-title":"Biomed. J"},{"key":"10.1074\/jbc.RA119.008568_bib28","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.mce.2013.01.023","article-title":"Foldosome regulation of androgen receptor action in prostate cancer","volume":"369","author":"Cano","year":"2013","journal-title":"Mol. Cell Endocrinol"},{"key":"10.1074\/jbc.RA119.008568_bib29","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1002\/bip.21292","article-title":"Hsp90 and co-chaperones twist the functions of diverse client proteins","volume":"93","author":"Zuehlke","year":"2010","journal-title":"Biopolymers"},{"key":"10.1074\/jbc.RA119.008568_bib30","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1046\/j.1365-2443.1999.00299.x","article-title":"Hsc70\/Hsp40 chaperone system mediates the Hsp90-dependent refolding of firefly luciferase","volume":"4","author":"Minami","year":"1999","journal-title":"Genes Cells"},{"key":"10.1074\/jbc.RA119.008568_bib31","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1379\/1466-1268(2003)008<0309:MFROHF>2.0.CO;2","article-title":"Mechanisms for regulation of Hsp70 function by Hsp40","volume":"8","author":"Fan","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"10.1074\/jbc.RA119.008568_bib32","doi-asserted-by":"crossref","first-page":"38294","DOI":"10.1074\/jbc.M206566200","article-title":"The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex","volume":"277","author":"Hern\u00e1ndez","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib33","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1083\/jcb.200104079","article-title":"Hsp90: a specialized but essential protein-folding tool","volume":"154","author":"Young","year":"2001","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA119.008568_bib34","doi-asserted-by":"crossref","first-page":"11873","DOI":"10.1074\/jbc.M111445200","article-title":"HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor","volume":"277","author":"Hern\u00e1ndez","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib35","doi-asserted-by":"crossref","first-page":"35194","DOI":"10.1074\/jbc.273.52.35194","article-title":"Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery","volume":"273","author":"Chen","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib36","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1074\/jbc.273.6.3679","article-title":"Hop modulates Hsp70\/Hsp90 interactions in protein folding","volume":"273","author":"Johnson","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib37","doi-asserted-by":"crossref","first-page":"3702","DOI":"10.1016\/j.febslet.2007.05.039","article-title":"The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions","volume":"581","author":"Daugaard","year":"2007","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA119.008568_bib38","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1158\/1541-7786.MCR-11-0019","article-title":"HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells","volume":"9","author":"Leu","year":"2011","journal-title":"Mol. Cancer Res"},{"key":"10.1074\/jbc.RA119.008568_bib39","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.pharmthera.2012.08.014","article-title":"Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential","volume":"136","author":"Liu","year":"2012","journal-title":"Pharmacol. Ther"},{"key":"10.1074\/jbc.RA119.008568_bib40","first-page":"67","article-title":"Modulation of cholera toxin structure\/function by Hsp90","author":"Taylor","year":"2015"},{"key":"10.1074\/jbc.RA119.008568_bib41","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.molcel.2009.09.023","article-title":"A small molecule inhibitor of inducible heat shock protein 70","volume":"36","author":"Leu","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA119.008568_bib42","doi-asserted-by":"crossref","first-page":"6166","DOI":"10.1128\/IAI.70.11.6166-6171.2002","article-title":"Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway","volume":"70","author":"Teter","year":"2002","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib43","doi-asserted-by":"crossref","first-page":"2259","DOI":"10.1128\/IAI.74.4.2259-2267.2006","article-title":"The cholera toxin A13 subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol","volume":"74","author":"Teter","year":"2006","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib44","first-page":"163","article-title":"Host cell chaperones Hsp70\/Hsp90 and peptidyl-prolyl cis\/trans isomerases are required for the membrane translocation of bacterial ADP-ribosylating toxins","volume":"406","author":"Ernst","year":"2017","journal-title":"Curr. Top. Microbiol. Immunol"},{"key":"10.1074\/jbc.RA119.008568_bib45","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1080\/10409230490892513","article-title":"Functional specificity of co-chaperone interactions with Hsp90 client proteins","volume":"39","author":"Riggs","year":"2004","journal-title":"Crit. Rev. Biochem. Mol. Biol"},{"key":"10.1074\/jbc.RA119.008568_bib46","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1126\/science.6238408","article-title":"Cyclophilin: a specific cytosolic binding protein for cyclosporin A","volume":"226","author":"Handschumacher","year":"1984","journal-title":"Science"},{"key":"10.1074\/jbc.RA119.008568_bib47","doi-asserted-by":"crossref","first-page":"294","DOI":"10.3390\/toxins3030294","article-title":"Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process","volume":"3","author":"Murphy","year":"2011","journal-title":"Toxins (Basel)"},{"key":"10.1074\/jbc.RA119.008568_bib48","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1111\/j.1462-5822.2010.01539.x","article-title":"Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen","volume":"13","author":"Dmochewitz","year":"2011","journal-title":"Cell Microbiol"},{"key":"10.1074\/jbc.RA119.008568_bib49","doi-asserted-by":"crossref","first-page":"22090","DOI":"10.1074\/jbc.M111.237966","article-title":"Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit","volume":"286","author":"Taylor","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib50","doi-asserted-by":"crossref","first-page":"11155","DOI":"10.1016\/S0021-9258(19)78104-6","article-title":"Characterization of the protein-protein interactions determining the heat shock protein (hsp90\u00b7hsp70\u00b7hsp56) heterocomplex","volume":"269","author":"Czar","year":"1994","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib51","series-title":"Lipid-Protein Interactions: Methods and Protocols","first-page":"177","article-title":"Structural characterization of membrane proteins and peptides by FTIR and ATR-FTIR spectroscopy","author":"Tatulian","year":"2013"},{"key":"10.1074\/jbc.RA119.008568_bib52","doi-asserted-by":"crossref","first-page":"4739","DOI":"10.1128\/IAI.05503-11","article-title":"Structural and functional interactions between the cholera toxin A1 subunit and ERdj3\/HEDJ, a chaperone of the endoplasmic reticulum","volume":"79","author":"Massey","year":"2011","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA119.008568_bib53","doi-asserted-by":"crossref","first-page":"4591","DOI":"10.1016\/S0021-9258(19)67333-3","article-title":"Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line","volume":"272","author":"Orlandi","year":"1997","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib54","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/S0014-5793(03)01217-1","article-title":"BiP-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes","volume":"554","author":"Winkeler","year":"2003","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA119.008568_bib55","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1091\/mbc.e12-07-0522","article-title":"The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation","volume":"24","author":"Williams","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA119.008568_bib56","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1074\/jbc.274.2.781","article-title":"An evolutionarily conserved family of Hsp70\/Hsc70 molecular chaperone regulators","volume":"274","author":"Takayama","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.008568_bib57","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1021\/acschembio.7b01039","article-title":"Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity","volume":"13","author":"Kundel","year":"2018","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA119.008568_bib58","doi-asserted-by":"crossref","first-page":"20301","DOI":"10.1038\/srep20301","article-title":"A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens \u03b9 toxin","volume":"6","author":"Ernst","year":"2016","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA119.008568_bib59","doi-asserted-by":"crossref","first-page":"2724","DOI":"10.1038\/s41598-017-02882-y","article-title":"Hsp70 facilitates trans-membrane transport of bacterial ADP-ribosylating toxins into the cytosol of mammalian cells","volume":"7","author":"Ernst","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA119.008568_bib60","doi-asserted-by":"crossref","first-page":"17408","DOI":"10.1073\/pnas.0809013105","article-title":"Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum","volume":"105","author":"Spooner","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.008568_bib61","doi-asserted-by":"crossref","first-page":"12647","DOI":"10.1111\/cmi.12647","article-title":"Hsp90 is involved in the entry of clostridial neurotoxins into the cytosol of nerve terminals","volume":"19","author":"Tehran","year":"2017","journal-title":"Cell Microbiol"},{"key":"10.1074\/jbc.RA119.008568_bib62","doi-asserted-by":"crossref","first-page":"8839","DOI":"10.1021\/bi101201c","article-title":"Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit","volume":"49","author":"Banerjee","year":"2010","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA119.008568_bib63","first-page":"e3686","article-title":"Detection of toxin translocation into the host cytosol by surface plasmon resonance","volume":"59","author":"Taylor","year":"2012","journal-title":"J. Visual. Exp"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820301629?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820301629?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA119.008568","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T03:54:41Z","timestamp":1641268481000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820301629"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,8]]},"references-count":63,"journal-issue":{"issue":"32","published-print":{"date-parts":[[2019,8]]}},"alternative-id":["S0021925820301629"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra119.008568","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2019,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA119.008568","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Burress et al.","name":"copyright","label":"Copyright"}]}}