{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T01:31:18Z","timestamp":1793410278424,"version":"4.5.0"},"reference-count":187,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,13]],"date-time":"2023-10-13T00:00:00Z","timestamp":1697155200000},"content-version":"am","delay-in-days":316,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI137056"],"award-info":[{"award-number":["R01AI137056"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cellular Signalling"],"published-print":{"date-parts":[[2022,12]]},"DOI":"10.1016\/j.cellsig.2022.110489","type":"journal-article","created":{"date-parts":[[2022,10,7]],"date-time":"2022-10-07T21:40:03Z","timestamp":1665178803000},"page":"110489","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"special_numbering":"C","title":["The manipulation of cell signaling and host cell biology by cholera toxin"],"prefix":"10.1016","volume":"100","author":[{"given":"Christopher","family":"White","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carly","family":"Bader","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken","family":"Teter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"36","key":"10.1016\/j.cellsig.2022.110489_bb0005","doi-asserted-by":"crossref","first-page":"21907","DOI":"10.1016\/S0021-9258(20)88271-4","article-title":"Mutations of GS alpha designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity","volume":"264","author":"Freissmuth","year":"1989","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0010","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/S0167-4889(02)00163-5","article-title":"Retrograde transport of protein toxins under conditions of COPI dysfunction","volume":"1589","author":"Chen","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0015","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1083\/jcb.143.3.601","article-title":"KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from the Golgi involves COPI, p23, and the COOH terminus of Erd2p","volume":"143","author":"Majoul","year":"1998","journal-title":"J. Cell Biol."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0020","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1091\/mbc.01-12-0592","article-title":"Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection","volume":"13","author":"Richards","year":"2002","journal-title":"Mol. Biol. Cell"},{"issue":"32","key":"10.1016\/j.cellsig.2022.110489_bb0025","doi-asserted-by":"crossref","first-page":"12122","DOI":"10.1074\/jbc.RA119.008568","article-title":"HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol","volume":"294","author":"Burress","year":"2019","journal-title":"J. Biol. Chem."},{"issue":"9835","key":"10.1016\/j.cellsig.2022.110489_bb0030","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1016\/S0140-6736(12)60436-X","article-title":"Cholera","volume":"379","author":"Harris","year":"2012","journal-title":"Lancet"},{"issue":"10101","key":"10.1016\/j.cellsig.2022.110489_bb0035","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1016\/S0140-6736(17)30559-7","volume":"390","author":"Clemens","year":"2017","journal-title":"Cholera. Lancet"},{"key":"10.1016\/j.cellsig.2022.110489_bb0040","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1016\/S0140-6736(22)00330-0","article-title":"Cholera","volume":"399","author":"Kanungo","year":"2022","journal-title":"Lancet"},{"key":"10.1016\/j.cellsig.2022.110489_bb0045","first-page":"S66","article-title":"Cholera - management and prevention","volume":"74","author":"Davies","year":"2017","journal-title":"J. Inf. Secur."},{"key":"10.1016\/j.cellsig.2022.110489_bb0050","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S1473-3099(07)70138-X","article-title":"The true burden and risk of cholera: implications for prevention and control","volume":"7","author":"Zuckerman","year":"2007","journal-title":"Lancet Infect. Dis."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0055","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0003832","article-title":"Updated global burden of cholera in endemic countries","volume":"9","author":"Ali","year":"2015","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0060","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1111\/j.1574-6976.2002.tb00605.x","article-title":"Vibrio cholerae and cholera: out of the water and into the host","volume":"26","author":"Reidl","year":"2002","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.cellsig.2022.110489_bb0065","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S1369-5274(02)00005-X","article-title":"Filamentous phages linked to virulence of vibrio cholerae","volume":"6","author":"Davis","year":"2003","journal-title":"Curr. Opin. Microbiol."},{"issue":"9","key":"10.1016\/j.cellsig.2022.110489_bb0070","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1007\/s00018-008-7496-5","article-title":"Cholera toxin structure, gene regulation and pathophysiological and immunological aspects","volume":"65","author":"Sanchez","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0075","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1080\/09687680410001663267","article-title":"Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (review)","volume":"21","author":"De Haan","year":"2004","journal-title":"Mol. Membr. Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0080","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":"10.1016\/j.cellsig.2022.110489_bb0085","doi-asserted-by":"crossref","first-page":"2132","DOI":"10.3390\/toxins2082132","article-title":"Toxin mediated diarrhea in the 21st century: the pathophysiology of intestinal ion transport in the course of ETEC, V. cholerae and rotavirus infection","volume":"2","author":"Kopic","year":"2010","journal-title":"Toxins"},{"key":"10.1016\/j.cellsig.2022.110489_bb0090","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/335211a0","article-title":"Accounting for cystic fibrosis","volume":"335","author":"Baxter","year":"1988","journal-title":"Nature"},{"issue":"5182","key":"10.1016\/j.cellsig.2022.110489_bb0095","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1126\/science.7524148","article-title":"Cystic fibrosis heterozygote resistance to cholera toxin in the cystic fibrosis mouse model","volume":"266","author":"Gabriel","year":"1994","journal-title":"Science"},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0100","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."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0105","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1038\/clpt.2012.114","article-title":"CFTR inhibitors for treating diarrheal disease","volume":"92","author":"Thiagarajah","year":"2012","journal-title":"Clin. Pharmacol. Ther."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0110","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1111\/jphp.13344","article-title":"A comprehensive review of therapeutic approaches available for the treatment of cholera","volume":"72","author":"Sousa","year":"2020","journal-title":"J. Pharm. Pharmacol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0115","series-title":"Vibrio cholerae and Cholera: Molecular to Global Perspectives","first-page":"293","article-title":"Historical perspectives on pandemic cholera","author":"Blake","year":"1994"},{"key":"10.1016\/j.cellsig.2022.110489_bb0120","series-title":"Cholera","first-page":"1","article-title":"History of cholera","author":"Barua","year":"1992"},{"issue":"3\u20134","key":"10.1016\/j.cellsig.2022.110489_bb0125","doi-asserted-by":"crossref","first-page":"244","DOI":"10.2298\/SARH1204244R","article-title":"Cystic fibrosis","volume":"140","author":"Radlovic","year":"2012","journal-title":"Srp. Arh. Celok. Lek."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0130","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0306-9877(91)90144-N","article-title":"The cystic fibrosis heterozygote - advantage in surviving cholera?","volume":"36","author":"Rodman","year":"1991","journal-title":"Med. Hypotheses"},{"key":"10.1016\/j.cellsig.2022.110489_bb0135","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF00210660","article-title":"Why is the cystic fibrosis gene so frequent?","volume":"84","author":"Romeo","year":"1989","journal-title":"Hum. Genet."},{"issue":"1 Suppl","key":"10.1016\/j.cellsig.2022.110489_bb0140","doi-asserted-by":"crossref","first-page":"S23","DOI":"10.1152\/physrev.1999.79.1.S23","article-title":"Structure and function of the CFTR cholride channel","volume":"79","author":"Sheppard","year":"1999","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.cellsig.2022.110489_bb0145","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1016\/S0140-6736(20)32542-3","article-title":"Cystic fibrosis","volume":"397","author":"Shteinberg","year":"2021","journal-title":"Lancet"},{"issue":"Suppl. 1","key":"10.1016\/j.cellsig.2022.110489_bb0150","first-page":"S5","article-title":"Increasing life expectancy in cystic fibrosis: advances and challenges","volume":"57","author":"McBennett","year":"2022","journal-title":"Pediatr. Pulmonol."},{"issue":"23","key":"10.1016\/j.cellsig.2022.110489_bb0155","doi-asserted-by":"crossref","first-page":"4635","DOI":"10.1182\/blood-2010-01-261859","article-title":"The relationship between blood groups and disease","volume":"115","author":"Anstee","year":"2010","journal-title":"Blood"},{"issue":"44","key":"10.1016\/j.cellsig.2022.110489_bb0160","doi-asserted-by":"crossref","first-page":"17471","DOI":"10.1073\/pnas.0705390104","article-title":"Blood group O protects against severe Plasmodium falciparum malaria through the mechanism of reduced rosetting","volume":"104","author":"Rowe","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0165","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005567","article-title":"High-resolution crystal structures elucidate the molecular basis of cholera blood group dependence","volume":"12","author":"Heggelund","year":"2016","journal-title":"PLoS Pathog."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0170","doi-asserted-by":"crossref","first-page":"440","DOI":"10.4269\/ajtmh.16-0161","article-title":"Blood group O-dependent cellular responses to cholera toxin: parallel clinical and epidemiological links to severe cholera","volume":"95","author":"Kuhlmann","year":"2016","journal-title":"Am. J. Trop. Med. Hyg."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0175","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1093\/oxfordjournals.aje.a114050","article-title":"Predisposition for cholera of individuals with O blood group. Possible evolutionary significance","volume":"121","author":"Glass","year":"1985","journal-title":"Am. J. Epidemiol."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0180","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20061307","article-title":"Toxins utilize the endoplasmic reticulum-associated protein degradation pathway in their intoxication process","volume":"20","author":"Nowakowska-Go\u0142acka","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cellsig.2022.110489_bb0185","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/bs.pmbts.2017.11.010","article-title":"Protein toxins that utilize gangliosides as host receptors","volume":"156","author":"Zuverink","year":"2018","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"10.1016\/j.cellsig.2022.110489_bb0190","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."},{"issue":"51","key":"10.1016\/j.cellsig.2022.110489_bb0195","article-title":"Insights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins","volume":"2","author":"Cho","year":"2012","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0200","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.semcdb.2004.03.005","article-title":"Glycosphingolipids as toxin receptors","volume":"15","author":"Smith","year":"2004","journal-title":"Semin. Cell Dev. Biol."},{"issue":"16","key":"10.1016\/j.cellsig.2022.110489_bb0205","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."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0210","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1083\/jcb.93.3.860","article-title":"Internalization and degradation of cholera toxin by cultured cells: relationship to toxin action","volume":"93","author":"Fishman","year":"1982","journal-title":"J. Cell Biol."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0215","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1083\/jcb.141.4.905","article-title":"Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains","volume":"141","author":"Orlandi","year":"1998","journal-title":"J. Cell Biol."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0220","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."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0225","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."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0230","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1083\/jcb.117.6.1197","article-title":"Mechanism of cholera toxin action on a polarized human intestinal epithelial cell line: role of vesicular traffic","volume":"117","author":"Lencer","year":"1992","journal-title":"J. Cell Biol."},{"issue":"20","key":"10.1016\/j.cellsig.2022.110489_bb0235","doi-asserted-by":"crossref","first-page":"12148","DOI":"10.1016\/S0021-9258(18)33691-3","article-title":"Mechanism of action of cholera toxin on intact cells. Generation of A1 peptide and activation of adenylate cyclase","volume":"257","author":"Kassis","year":"1982","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0240","doi-asserted-by":"crossref","first-page":"4783","DOI":"10.1091\/mbc.e03-06-0354","article-title":"Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm","volume":"14","author":"Fujinaga","year":"2003","journal-title":"Mol. Biol. Cell"},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0245","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0018825","article-title":"A therapeutic chemical chaperone inhibits cholera intoxication and unfolding\/translocation of the cholera toxin A1 subunit","volume":"6","author":"Taylor","year":"2011","journal-title":"PLoS One"},{"issue":"25","key":"10.1016\/j.cellsig.2022.110489_bb0250","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."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0255","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1016\/j.jmb.2009.09.013","article-title":"Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication","volume":"393","author":"Massey","year":"2009","journal-title":"J. Mol. Biol."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0260","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."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0265","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"},{"issue":"13","key":"10.1016\/j.cellsig.2022.110489_bb0270","doi-asserted-by":"crossref","first-page":"3772","DOI":"10.1021\/bi0360152","article-title":"Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism","volume":"43","author":"O\u2019Neal","year":"2004","journal-title":"Biochemistry"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0275","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/S0021-9258(17)43512-5","article-title":"Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin","volume":"259","author":"Van Dop","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cellsig.2022.110489_bb0280","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1038\/340692a0","article-title":"GTPase inhibiting mutations activate the \u03b1 chain of Gs and stimulate adenylyl cyclase in human pituitary tumours","volume":"340","author":"Landis","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.cellsig.2022.110489_bb0285","doi-asserted-by":"crossref","first-page":"G1549","DOI":"10.1152\/ajpgi.00388.2006","article-title":"Synaptotagmin I binds intestinal epithelial NHE3 and mediates cAMP- and Ca2+\u2212induced endocytosis by recruitment of AP2 and clathrin","volume":"292","author":"Musch","year":"2007","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0290","doi-asserted-by":"crossref","first-page":"jcs218610","DOI":"10.1242\/jcs.218610","article-title":"Cholera toxin inhibits SNX27-retromer-mediated delivery of cargo proteins to the plasma membrane","volume":"131","author":"Singh","year":"2018","journal-title":"J. Cell Sci."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0295","doi-asserted-by":"crossref","first-page":"2187","DOI":"10.1172\/JCI118273","article-title":"Activation of protein kinase A acutely inhibits and phosphorylates Na\/H exchanger NHE-3","volume":"96","author":"Moe","year":"1995","journal-title":"J. Clin. Invest."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0300","first-page":"67","article-title":"Conversion of apical plasma membrane sphingomyelin to ceramide attenuates the intoxication of host cells by cholera toxin","volume":"10","author":"Saslowsky","year":"2008","journal-title":"Cell. Microbiol."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0305","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1038\/sj.embor.7400152","article-title":"Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells","volume":"5","author":"Feng","year":"2004","journal-title":"EMBO Rep."},{"issue":"5961","key":"10.1016\/j.cellsig.2022.110489_bb0310","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1126\/science.1174621","article-title":"Lipid rafts as a membrane-organizing principle","volume":"327","author":"Lingwood","year":"2010","journal-title":"Science"},{"issue":"543","key":"10.1016\/j.cellsig.2022.110489_bb0315","article-title":"Cholera toxin as a probe for membrane biology","volume":"13","author":"Kenworthy","year":"2021","journal-title":"Toxins"},{"issue":"23","key":"10.1016\/j.cellsig.2022.110489_bb0320","doi-asserted-by":"crossref","first-page":"17221","DOI":"10.1074\/jbc.R000005200","article-title":"Structure and function of sphingolipid- and cholesterol-rich membrane rafts","volume":"275","author":"Brown","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cellsig.2022.110489_bb0325","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/S1937-6448(10)82003-9","article-title":"Lipid rafts, caveolae, and their endocytosis","volume":"282","author":"Lajoie","year":"2010","journal-title":"Int. Rev. Cell Mol. Biol."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0330","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/35036052","article-title":"Lipid rafts and signal transduction","volume":"1","author":"Simons","year":"2000","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"18","key":"10.1016\/j.cellsig.2022.110489_bb0335","doi-asserted-by":"crossref","first-page":"16249","DOI":"10.1074\/jbc.M109834200","article-title":"Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol","volume":"277","author":"Wolf","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0340","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1073\/pnas.72.7.2520","article-title":"Interaction of cholera toxin and membrane GM1 ganglioside of small intestine","volume":"72","author":"Holmgren","year":"1975","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0345","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1128\/iai.8.2.208-214.1973","article-title":"Tissue receptor for cholera exotoxin: postulated structure from studies with GM1 ganglioside and related glycolipids","volume":"8","author":"Holmgren","year":"1973","journal-title":"Infect. Immun."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0350","doi-asserted-by":"crossref","first-page":"2112","DOI":"10.1091\/mbc.e07-01-0071","article-title":"Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling","volume":"18","author":"Fujita","year":"2007","journal-title":"Mol. Biol. Cell"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0355","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1002\/pro.5560030202","article-title":"Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide","volume":"3","author":"Merritt","year":"1994","journal-title":"Protein Sci."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0360","doi-asserted-by":"crossref","first-page":"e00401","DOI":"10.1128\/mBio.00401-12","article-title":"A single native ganglioside GM1-binding site is sufficient for cholera toxin to bind to cells and complete the intoxication pathway","volume":"3","author":"Jobling","year":"2012","journal-title":"MBio"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0365","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/0167-4889(94)90240-2","article-title":"Interaction of a cholera toxin derivative containing a reduced number of receptor binding sites with intact cells in culture","volume":"1223","author":"De Wolf","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0370","doi-asserted-by":"crossref","first-page":"1476","DOI":"10.1128\/IAI.01286-07","article-title":"Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules","volume":"76","author":"Wolf","year":"2008","journal-title":"Infect. Immun."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0375","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0167-4889(82)90010-6","article-title":"Detergent extraction of cholera toxin and gangliosides from cultured cells and isolated membranes","volume":"720","author":"Hagmann","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"issue":"9","key":"10.1016\/j.cellsig.2022.110489_bb0380","doi-asserted-by":"crossref","first-page":"3272","DOI":"10.1073\/pnas.0408215102","article-title":"Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes","volume":"102","author":"Bacia","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0385","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1016\/j.bpj.2016.11.008","article-title":"Glycolipid crosslinking is required for cholera toxin to partition into and stabilize ordered domains","volume":"111","author":"Raghunathan","year":"2016","journal-title":"Biophys. J."},{"issue":"26","key":"10.1016\/j.cellsig.2022.110489_bb0390","doi-asserted-by":"crossref","first-page":"14978","DOI":"10.1073\/pnas.2001119117","article-title":"Structured clustering of the glycosphingolipid GM1 is required for membrane curvature induced by cholera toxin","volume":"117","author":"Kabbani","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0395","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1152\/physrev.1997.77.3.759","article-title":"Endocytosis","volume":"77","author":"Mukherjee","year":"1997","journal-title":"Physiol. Rev."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0400","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1038\/nrm1315","article-title":"Endocytic recycling","volume":"5","author":"Maxfield","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0405","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1034\/j.1600-0854.2000.010302.x","article-title":"Role of membrane organization and membrane domains in endocytic lipid trafficking","volume":"1","author":"Mukherjee","year":"2000","journal-title":"Traffic"},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0410","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1042\/bj2710107","article-title":"Cyclic AMP accumulation in HeLa cells induced by cholera toxin. Involvement of the ceramide moiety of GM1 ganglioside","volume":"271","author":"Masserini","year":"1990","journal-title":"Biochem. J."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0415","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.devcel.2012.08.002","article-title":"Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1","volume":"23","author":"Chinnapen","year":"2012","journal-title":"Dev. Cell"},{"key":"10.1016\/j.cellsig.2022.110489_bb0420","doi-asserted-by":"crossref","first-page":"2526","DOI":"10.1016\/j.bbamem.2009.09.018","article-title":"Differential endocytic trafficking of neuropathy-associated antibodies to GM1 ganglioside and cholera toxin in epithelial and neural cells","volume":"1788","author":"Iglesias-Bartolome","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0425","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1046\/j.1471-4159.2001.00489.x","article-title":"Cholesterol depletion by methyl-beta-cyclodextrin blocks cholera toxin transport from endosomes to the Golgi apparatus in hippocampal neurons","volume":"78","author":"Shogomori","year":"2001","journal-title":"J. Neurochem."},{"key":"10.1016\/j.cellsig.2022.110489_bb0430","first-page":"C1453","article-title":"Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton","volume":"287","author":"Badizadegan","year":"2004","journal-title":"Am. J. Phys. Cell Phys."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0435","doi-asserted-by":"crossref","first-page":"4399","DOI":"10.1172\/JCI42958","article-title":"Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin\/reggie proteins but not Derlin-1 or \u22122","volume":"120","author":"Saslowsky","year":"2010","journal-title":"J. Clin. Invest."},{"issue":"Pt 23","key":"10.1016\/j.cellsig.2022.110489_bb0440","doi-asserted-by":"crossref","first-page":"3933","DOI":"10.1242\/jcs.092015","article-title":"The roles of flotillin microdomains\u2014endocytosis and beyond","volume":"124","author":"Otto","year":"2011","journal-title":"J. Cell Sci."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0445","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/0092-8674(89)90685-5","article-title":"Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER","volume":"56","author":"Lippincott-Schwartz","year":"1989","journal-title":"Cell"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0450","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/0092-8674(91)90534-6","article-title":"Brefeldin A\u2019s effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic","volume":"67","author":"Lippincott-Schwartz","year":"1991","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0455","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1002\/jcp.1041540203","article-title":"Involvement of the Golgi region in the intracellular trafficking of cholera toxin","volume":"154","author":"Nambiar","year":"1993","journal-title":"J. Cell. Physiol."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0460","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20181320","article-title":"Protein disulfide isomerase does not act as an unfoldase in the disassembly of cholera toxin","volume":"38","author":"Cherubin","year":"2018","journal-title":"Biosci. Rep."},{"issue":"jcs250100","key":"10.1016\/j.cellsig.2022.110489_bb0465","article-title":"Molecular basis for KDEL-mediated retrieval of escaped ER-resident proteins - SWEET talking the COPs","volume":"133","author":"Newstead","year":"2020","journal-title":"J. Cell Sci."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0470","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1083\/jcb.131.4.951","article-title":"Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDEL","volume":"131","author":"Lencer","year":"1995","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0475","doi-asserted-by":"crossref","first-page":"a033928","DOI":"10.1101\/cshperspect.a033928","article-title":"Chaperoning endoplasmic reticulum-associated degradation (ERAD) and protein conformational diseases","volume":"11","author":"Needham","year":"2019","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.cellsig.2022.110489_bb0480","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1016\/j.molcel.2022.03.025","article-title":"Reshaping endoplasmic reticulum quality control through the unfolded protein response","volume":"82","author":"Wiseman","year":"2022","journal-title":"Mol. Cell"},{"issue":"2\u20133","key":"10.1016\/j.cellsig.2022.110489_bb0485","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/S0014-5793(96)01447-0","article-title":"Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum","volume":"401","author":"Majoul","year":"1997","journal-title":"FEBS Lett."},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0490","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."},{"issue":"8","key":"10.1016\/j.cellsig.2022.110489_bb0495","doi-asserted-by":"crossref","first-page":"pii: E458","DOI":"10.3390\/toxins11080458","article-title":"Quercetin-3-rutinoside blocks the disassembly of cholera toxin by protein disulfide isomerase","volume":"11","author":"Guyette","year":"2019","journal-title":"Toxins"},{"issue":"13","key":"10.1016\/j.cellsig.2022.110489_bb0500","doi-asserted-by":"crossref","first-page":"5855","DOI":"10.1016\/S0021-9258(18)50491-9","article-title":"Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition","volume":"254","author":"Mekalanos","year":"1979","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0505","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1111\/j.1432-1033.1979.tb12862.x","article-title":"The role of the reactive disulfide bond in the interaction of cholera-toxin functional regions","volume":"93","author":"Tomasi","year":"1979","journal-title":"Eur. J. Biochem."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0510","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"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0515","doi-asserted-by":"crossref","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."},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0520","doi-asserted-by":"crossref","first-page":"3962","DOI":"10.1074\/jbc.274.7.3962","article-title":"Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity","volume":"274","author":"Rodighiero","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"34","key":"10.1016\/j.cellsig.2022.110489_bb0525","article-title":"Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin","volume":"12","author":"Serrano","year":"2022","journal-title":"Sci. Rep."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0530","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1021\/jp506509c","article-title":"Biophysical characteristics of cholera toxin and Escherichia coli heat-labile enterotoxin structure and chemistry lead to differential toxicity","volume":"119","author":"Craft","year":"2015","journal-title":"J. Phys. Chem. B"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0535","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1006\/jmbi.1993.1209","article-title":"Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin","volume":"230","author":"Sixma","year":"1993","journal-title":"J. Mol. Biol."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0540","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1021\/bi00406a035","article-title":"Thermal stability and intersubunit interactions of cholera toxin in solution and in association with its cell-surface receptor ganglioside GM1","volume":"27","author":"Goins","year":"1988","journal-title":"Biochemistry"},{"issue":"35","key":"10.1016\/j.cellsig.2022.110489_bb0545","doi-asserted-by":"crossref","first-page":"8106","DOI":"10.1021\/bi00487a017","article-title":"Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy","volume":"29","author":"Surewicz","year":"1990","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0550","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/j.jmb.2007.12.075","article-title":"Order-disorder-order transitions mediate the activation of cholera toxin","volume":"377","author":"Ampapathi","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0555","doi-asserted-by":"crossref","first-page":"2674","DOI":"10.3390\/toxins7072674","article-title":"A conformational shift in the dissociated cholera toxin A1 subunit prevents reassembly of the cholera holotoxin","volume":"7","author":"Taylor","year":"2015","journal-title":"Toxins"},{"issue":"18","key":"10.1016\/j.cellsig.2022.110489_bb0560","doi-asserted-by":"crossref","first-page":"4825","DOI":"10.1111\/j.1742-4658.2007.06008.x","article-title":"Lipopolyamine treatment increases the efficacy of intoxication with saporin and an anticancer saporin conjugate","volume":"274","author":"Geden","year":"2007","journal-title":"FEBS J."},{"issue":"11","key":"10.1016\/j.cellsig.2022.110489_bb0565","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."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0570","doi-asserted-by":"crossref","first-page":"3388","DOI":"10.1128\/IAI.00732-16","article-title":"Thermal unfolding of the pertussis toxin S1 subunit facilitates toxin translocation to the cytosol by the mechanism of endoplasmic reticulum-associated degradation","volume":"84","author":"Banerjee","year":"2016","journal-title":"Infect. Immun."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0575","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/0006-291X(89)91660-4","article-title":"Domain-specific bias in arginine\/lysine usage by protein toxins","volume":"160","author":"London","year":"1989","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"37","key":"10.1016\/j.cellsig.2022.110489_bb0580","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"},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0585","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."},{"issue":"10","key":"10.1016\/j.cellsig.2022.110489_bb0590","doi-asserted-by":"crossref","first-page":"3405","DOI":"10.1021\/bi011580v","article-title":"The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol","volume":"41","author":"Deeks","year":"2002","journal-title":"Biochemistry"},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0595","doi-asserted-by":"crossref","first-page":"2946","DOI":"10.1128\/IAI.02011-06","article-title":"Evading the proteasome: absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation","volume":"75","author":"Worthington","year":"2007","journal-title":"Infect. Immun."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0600","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1042\/BJ20061890","article-title":"The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation)","volume":"404","author":"Brodsky","year":"2007","journal-title":"Biochem. J."},{"issue":"11","key":"10.1016\/j.cellsig.2022.110489_bb0605","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."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0610","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"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0615","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":"10.1016\/j.cellsig.2022.110489_bb0620","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1091\/mbc.E15-01-0014","article-title":"The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation","volume":"26","author":"Williams","year":"2015","journal-title":"Mol. Biol. Cell"},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0625","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.tibs.2016.10.005","article-title":"A case for Sec61 channel involvement in ERAD","volume":"42","author":"Romisch","year":"2017","journal-title":"Trends Biochem. Sci."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0630","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1083\/jcb.148.6.1203","article-title":"Cholera toxin is exported from microsomes by the Sec61p complex","volume":"148","author":"Schmitz","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0635","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1083\/jcb.200409174","article-title":"The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum","volume":"168","author":"Alder","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0640","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1042\/BCJ20160582","article-title":"The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation","volume":"474","author":"Preston","year":"2017","journal-title":"Biochem. J."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0645","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1091\/mbc.e07-08-0755","article-title":"Derlin-1 facilitates the retro-translocation of cholera toxin","volume":"19","author":"Bernardi","year":"2008","journal-title":"Mol. Biol. Cell"},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0650","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1091\/mbc.e09-07-0586","article-title":"The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation","volume":"21","author":"Bernardi","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.cellsig.2022.110489_bb0655","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.ceb.2018.04.004","article-title":"Mechanistic insights into ER-associated protein degradation","volume":"53","author":"Wu","year":"2018","journal-title":"Curr. Opin. Cell Biol."},{"issue":"41","key":"10.1016\/j.cellsig.2022.110489_bb0660","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."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0665","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S1074-7613(00)00013-3","article-title":"Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel","volume":"13","author":"Koopmann","year":"2000","journal-title":"Immunity"},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0670","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/S0014-5793(99)01222-3","article-title":"Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast","volume":"459","author":"Simpson","year":"1999","journal-title":"FEBS Lett."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0675","doi-asserted-by":"crossref","first-page":"2524","DOI":"10.1128\/IAI.73.4.2524-2532.2005","article-title":"Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone HEDJ\/ERdj3","volume":"73","author":"Yu","year":"2005","journal-title":"Infect. Immun."},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0680","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0041119","article-title":"Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p","volume":"7","author":"Li","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.cellsig.2022.110489_bb0685","article-title":"TorsinA participates in endoplasmic reticulum-associated degradation","volume":"2(393","author":"Nery","year":"2011","journal-title":"Nat. Commun."},{"issue":"30","key":"10.1016\/j.cellsig.2022.110489_bb0690","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."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0695","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."},{"issue":"48","key":"10.1016\/j.cellsig.2022.110489_bb0700","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."},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0705","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1034\/j.1600-0854.2003.00070.x","article-title":"A class of mutant CHO cells resistant to cholera toxin rapidly degrades the catalytic polypeptide of cholera toxin and exhibits increased endoplasmic reticulum-associated degradation","volume":"4","author":"Teter","year":"2003","journal-title":"Traffic"},{"issue":"10","key":"10.1016\/j.cellsig.2022.110489_bb0710","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.13074","article-title":"A binding motif for Hsp90 in the A chains of ADP-ribosylating toxins that move from the endoplasmic reticulum to the cytosol","volume":"21","author":"Kellner","year":"2019","journal-title":"Cell. Microbiol."},{"issue":"39","key":"10.1016\/j.cellsig.2022.110489_bb0715","doi-asserted-by":"crossref","first-page":"16363","DOI":"10.1073\/pnas.1108372108","article-title":"Heat shock protein 90 (HSP90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells","volume":"108","author":"Imai","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.cellsig.2022.110489_bb0720","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.molimm.2015.05.002","article-title":"Are ERAD components involved in cross-presentation?","volume":"68","author":"Grotzke","year":"2015","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.cellsig.2022.110489_bb0725","doi-asserted-by":"crossref","first-page":"3770","DOI":"10.1073\/pnas.89.9.3770","article-title":"What drives the translocation of proteins?","volume":"89","author":"Simon","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0730","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/S0006-3495(93)81035-X","article-title":"Cellular motions and thermal fluctuations: the Brownian ratchet","volume":"65","author":"Peskin","year":"1993","journal-title":"Biophys. J."},{"issue":"8","key":"10.1016\/j.cellsig.2022.110489_bb0735","doi-asserted-by":"crossref","first-page":"2546","DOI":"10.1091\/mbc.12.8.2546","article-title":"Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol","volume":"12","author":"Shamu","year":"2001","journal-title":"Mol. Biol. Cell"},{"issue":"8","key":"10.1016\/j.cellsig.2022.110489_bb0740","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1034\/j.1600-0854.2002.30803.x","article-title":"Protein dislocation from the endoplasmic reticulum\u2014pulling out the suspect","volume":"3","author":"Jarosch","year":"2002","journal-title":"Traffic"},{"issue":"36","key":"10.1016\/j.cellsig.2022.110489_bb0745","doi-asserted-by":"crossref","first-page":"33369","DOI":"10.1074\/jbc.M112337200","article-title":"Detoxification of cholera toxin without removal of its immunoadjuvanticity by the addition of (STa-related) peptides to the catalytic subunit. A potential new strategy to generate immunostimulants for vaccination","volume":"277","author":"Sanchez","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0750","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1021\/bi00053a022","article-title":"Effects of temperature on ADP-ribosylation factor stimulation of cholera toxin activity","volume":"32","author":"Murayama","year":"1993","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.cellsig.2022.110489_bb0755","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1111\/mmi.12807","article-title":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide","volume":"94","author":"Banerjee","year":"2014","journal-title":"Mol. Microbiol."},{"issue":"10","key":"10.1016\/j.cellsig.2022.110489_bb0760","doi-asserted-by":"crossref","first-page":"6228","DOI":"10.1016\/S0021-9258(20)82130-9","article-title":"Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin","volume":"259","author":"Kahn","year":"1984","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.cellsig.2022.110489_bb0765","doi-asserted-by":"crossref","first-page":"12327","DOI":"10.1074\/jbc.270.21.12327","article-title":"Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes","volume":"270","author":"Moss","year":"1995","journal-title":"J. Biol. Chem."},{"issue":"5737","key":"10.1016\/j.cellsig.2022.110489_bb0770","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1126\/science.1113398","article-title":"Structural basis for the activation of cholera toxin by human ARF6-GTP","volume":"309","author":"O\u2019Neal","year":"2005","journal-title":"Science"},{"issue":"36","key":"10.1016\/j.cellsig.2022.110489_bb0775","doi-asserted-by":"crossref","first-page":"30395","DOI":"10.1074\/jbc.M112.385575","article-title":"Lipid rafts alter the stability and activity of the cholera toxin A1 subunit","volume":"287","author":"Ray","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0780","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.00447-20","article-title":"cAMP-independent activation of the unfolded protein response by cholera toxin","volume":"89","author":"Banerjee","year":"2021","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cellsig.2022.110489_bb0785","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1146\/annurev.cellbio.21.122303.120200","article-title":"Intracellular signaling by the unfolded protein response","volume":"22","author":"Bernales","year":"2006","journal-title":"Annu. Rev. Cell Dev. Biol."},{"issue":"6","key":"10.1016\/j.cellsig.2022.110489_bb0790","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1093\/jb\/mvp166","article-title":"Signalling pathways in the unfolded protein response: development from yeast to mammals","volume":"146","author":"Mori","year":"2009","journal-title":"J. Biochem."},{"issue":"3","key":"10.1016\/j.cellsig.2022.110489_bb0795","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0092-8674(00)80835-1","article-title":"Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation","volume":"101","author":"Travers","year":"2000","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0800","doi-asserted-by":"crossref","first-page":"163","DOI":"10.3181\/0705-RM-132","article-title":"Cholera toxin up-regulates endoplasmic reticulum proteins that correlate with sensitivity to the toxin","volume":"233","author":"Dixit","year":"2008","journal-title":"Exp. Biol. Med. (Maywood)"},{"issue":"22","key":"10.1016\/j.cellsig.2022.110489_bb0805","doi-asserted-by":"crossref","first-page":"12339","DOI":"10.1073\/pnas.93.22.12339","article-title":"Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum","volume":"93","author":"Sandvig","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"19","key":"10.1016\/j.cellsig.2022.110489_bb0810","doi-asserted-by":"crossref","first-page":"7260","DOI":"10.1073\/pnas.85.19.7260","article-title":"Cholera toxin potentiates IgE-coupled inositol phospholipid hydrolysis and mediator secretion by RBL-2H3 cells","volume":"85","author":"McCloskey","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"36","key":"10.1016\/j.cellsig.2022.110489_bb0815","doi-asserted-by":"crossref","first-page":"19626","DOI":"10.1016\/S0021-9258(19)77682-0","article-title":"Cholera toxin increases the rate of antigen-stimulated calcium influx in rat basophilic leukemia cells","volume":"263","author":"Narasimhan","year":"1988","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0820","first-page":"102","article-title":"Cholera toxin induces expression of the immediate-early response gene JE via a cyclic AMP-independent signaling pathway","volume":"11","author":"Qureshi","year":"1991","journal-title":"Mol. Cell. Biol."},{"issue":"22","key":"10.1016\/j.cellsig.2022.110489_bb0825","doi-asserted-by":"crossref","first-page":"7475","DOI":"10.1073\/pnas.82.22.7475","article-title":"Cholera toxin inhibits chemotaxis by a cAMP-independent mechanism","volume":"82","author":"Aksamit","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.cellsig.2022.110489_bb0830","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1111\/j.1365-313X.2011.04788.x","article-title":"AtIRE1A\/AtIRE1B and AGB1 independently control two essential unfolded protein response pathways in Arabidopsis","volume":"69","author":"Chen","year":"2012","journal-title":"Plant J."},{"issue":"10","key":"10.1016\/j.cellsig.2022.110489_bb0835","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1073\/pnas.0611735104","article-title":"Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response","volume":"104","author":"Wang","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.cellsig.2022.110489_bb0840","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/S0960-9822(03)00330-0","article-title":"A new mode of Ca2+ signaling by G protein-coupled receptors: gating of IP3 receptor Ca2+ release channels by G\u03b2\u03b3","volume":"13","author":"Zeng","year":"2003","journal-title":"Curr. Biol."},{"issue":"5 Pt 1","key":"10.1016\/j.cellsig.2022.110489_bb0845","first-page":"C1193","article-title":"Caco-2 intestinal cell differentiation is associated with G1 arrest and suppression of CDK2 and CDK4","volume":"275","author":"Ding","year":"1998","journal-title":"Am. J. Phys."},{"key":"10.1016\/j.cellsig.2022.110489_bb0850","series-title":"Vibrio cholerae and Cholera: Molecular to Global Perspectives","first-page":"145","article-title":"Toxins of Vibrio cholerae","author":"Kaper","year":"1994"},{"issue":"1","key":"10.1016\/j.cellsig.2022.110489_bb0855","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1128\/CMR.8.1.48","article-title":"Cholera","volume":"8","author":"Kaper","year":"1995","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.cellsig.2022.110489_bb0860","series-title":"Microbial Pathogenesis and the Intestinal Epithelial Cell","first-page":"385","article-title":"Trafficking of cholera toxin and related bacterial enterotoxins: pathways and endpoints","author":"Rodighiero","year":"2003"},{"issue":"10","key":"10.1016\/j.cellsig.2022.110489_bb0865","doi-asserted-by":"crossref","first-page":"5352","DOI":"10.1016\/S0021-9258(18)83552-9","article-title":"Cholera toxin induces cAMP-independent degradation of Gs","volume":"264","author":"Chang","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cellsig.2022.110489_bb0870","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1042\/bj2620643","article-title":"Cholera toxin treatment produces down-regulation of the \u03b1-subunit of the stimulatory guanine-nucleotide-binding protein (Gs)","volume":"262","author":"Milligan","year":"1989","journal-title":"Biochem. J."},{"issue":"5","key":"10.1016\/j.cellsig.2022.110489_bb0875","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1083\/jcb.119.5.1297","article-title":"Activation of the \u03b1 subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity","volume":"119","author":"Levis","year":"1992","journal-title":"J. Cell Biol."},{"issue":"18","key":"10.1016\/j.cellsig.2022.110489_bb0880","doi-asserted-by":"crossref","first-page":"2932","DOI":"10.1111\/febs.14078","article-title":"ADP-ribosylation: new facets of an ancient modification","volume":"284","author":"Palazzo","year":"2017","journal-title":"FEBS J."},{"issue":"5\u20136","key":"10.1016\/j.cellsig.2022.110489_bb0885","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1101\/gad.334631.119","article-title":"(ADP-ribosyl)hydrolases: structure, function, and biology","volume":"34","author":"Rack","year":"2020","journal-title":"Genes Dev."},{"key":"10.1016\/j.cellsig.2022.110489_bb0890","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.dnarep.2014.03.005","article-title":"Structure and function of the ARH family of ADP-ribosyl-acceptor hydrolases","volume":"23","author":"Mashimo","year":"2014","journal-title":"DNA Repair"},{"issue":"7","key":"10.1016\/j.cellsig.2022.110489_bb0895","doi-asserted-by":"crossref","first-page":"3050","DOI":"10.1073\/pnas.75.7.3050","article-title":"ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase","volume":"75","author":"Gill","year":"1978","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"10.1016\/j.cellsig.2022.110489_bb0900","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1016\/S0021-9258(18)93347-8","article-title":"Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis","volume":"243","author":"Honjo","year":"1968","journal-title":"J. Biol. Chem."},{"issue":"19","key":"10.1016\/j.cellsig.2022.110489_bb0905","doi-asserted-by":"crossref","first-page":"11879","DOI":"10.1016\/S0021-9258(17)44314-6","article-title":"Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein)","volume":"258","author":"Moss","year":"1983","journal-title":"J. Biol. Chem."},{"issue":"15","key":"10.1016\/j.cellsig.2022.110489_bb0910","doi-asserted-by":"crossref","first-page":"5534","DOI":"10.1128\/MCB.00302-07","article-title":"Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice","volume":"27","author":"Kato","year":"2007","journal-title":"Mol. Cell. Biol."},{"issue":"11","key":"10.1016\/j.cellsig.2022.110489_bb0915","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0207693","article-title":"Enhanced sensitivity to cholera toxin in female ADP-ribosylarginine hydrolase (ARH1)-deficient mice","volume":"13","author":"Watanabe","year":"2018","journal-title":"PLoS One"},{"issue":"9","key":"10.1016\/j.cellsig.2022.110489_bb0920","doi-asserted-by":"crossref","first-page":"6145","DOI":"10.1074\/jbc.M109.062067","article-title":"N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol","volume":"285","author":"Wernick","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cellsig.2022.110489_bb0925","series-title":"The cytopathic activity of cholera toxin requires a threshold quantity of cytosolic toxin","author":"Bader","year":"2022"},{"key":"10.1016\/j.cellsig.2022.110489_bb0930","doi-asserted-by":"crossref","first-page":"484","DOI":"10.3762\/bjoc.14.34","article-title":"Carbohydrate inhibitors of cholera toxin","volume":"14","author":"Kumar","year":"2018","journal-title":"Beilstein J. Org. Chem."},{"issue":"9","key":"10.1016\/j.cellsig.2022.110489_bb0935","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0073390","article-title":"Grape extracts inhibit multiple events in the cell biology of cholera intoxication","volume":"8","author":"Reddy","year":"2013","journal-title":"PLoS One"}],"container-title":["Cellular Signalling"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0898656822002510?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0898656822002510?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T11:11:05Z","timestamp":1760267465000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0898656822002510"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12]]},"references-count":187,"alternative-id":["S0898656822002510"],"URL":"https:\/\/doi.org\/10.1016\/j.cellsig.2022.110489","relation":{},"ISSN":["0898-6568"],"issn-type":[{"value":"0898-6568","type":"print"}],"subject":[],"published":{"date-parts":[[2022,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The manipulation of cell signaling and host cell biology by cholera toxin","name":"articletitle","label":"Article Title"},{"value":"Cellular Signalling","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cellsig.2022.110489","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"110489"}}