Nucleotide sequence analysis of the A2 and B subunits of Vibrio cholerae enterotoxin.Lockman H., Kaper J.B.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 258:13722-13726 (1983)Cited in2
Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development.Mekalanos J.J., Swartz D.J., Pearson G.D.N., Harford N., Groyne F., de Wilde M.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]StrainATCC 39050 / El Tor Inaba 2125 / Serotype O1CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 306:551-557 (1983)Cited in2
Structure and arrangement of the cholera toxin genes in Vibrio cholerae O139.Lebens M., Holmgren J.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]Strain4260B / Serotype O139CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEMS Microbiol. Lett. 117:197-202 (1994)Cited in1
No title available.Dams E., de Wolf M., Dierick W.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]StrainATCC 39050 / El Tor Inaba 2125 / Serotype O1CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (MAY-1991)Cited in2
No title available.Yamamoto K., Do V.G.R.F., Xu M., Iida T., Miwatani T., Albert M.J., Honda T.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]Strain1854 / O139-BengalCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (MAY-1994)Cited in2
DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae.Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D.[...], Fraser C.M.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]StrainATCC 39315 / El Tor Inaba N16961CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 406:477-483 (2000)Cited in99+99+
Covalent structure of the beta chain of cholera enterotoxin.Kurosky A., Markel D.E., Peterson J.W.View abstractCited forPROTEIN SEQUENCE OF 22-124CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 252:7257-7264 (1977)Cited in1
Determination of the primary structure of cholera toxin B subunit.Lai C.-Y.View abstractCited forPROTEIN SEQUENCE OF 22-124CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 252:7249-7256 (1977)Cited in1
The arrangement of subunits in cholera toxin.Gill D.M.View abstractCited forSUBUNITCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 15:1242-1248 (1976)Cited in2
Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulum.Fujinaga Y., Wolf A.A., Rodighiero C., Wheeler H., Tsai B., Allen L., Jobling M.G., Rapoport T., Holmes R.K., Lencer W.I.View abstractCited forTRANSPORT OF CHOLERA TOXIN WITHIN THE INTESTINAL CELLSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Biol. Cell 14:4783-4793 (2003)Cited in2
Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide.Merritt E.A., Sarfaty S., van den Akker F., L'Hoir C., Martial J.A., Hol W.G.J.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 3:166-175 (1994)Cited in1
The 2.4 A crystal structure of cholera toxin B subunit pentamer: choleragenoid.Zhang R.-G., Westbrook M.L., Westbrook E.M., Scott D.L., Otwinowski Z., Maulik P.R., Reed R.A., Shipley G.G.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 251:550-562 (1995)Cited in1
Structural studies of receptor binding by cholera toxin mutants.Merritt E.A., Sarfaty S., Jobling M.G., Chang T., Holmes R.K., Hirst T.R., Hol W.G.J.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS)StrainOgawa 41 / Classical biotypeCategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 6:1516-1528 (1997)Cited in1
A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks immunomodulatory or toxic activity.Aman A.T., Fraser S., Merritt E.A., Rodigherio C., Kenny M., Ahn M., Hol W.G.J., Williams N.A., Lencer W.I., Hirst T.R.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-57CategoriesPhenotypes & Variants, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 98:8536-8541 (2001)Cited in1
Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes.Pickens J.C., Merritt E.A., Ahn M., Verlinde C.L.M.J., Hol W.G.J., Fan E.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITORCategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCChem. Biol. 9:215-224 (2002)Cited in2
Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin.Zhang Z., Merritt E.A., Ahn M., Roach C., Hou Z., Verlinde C.L.M.J., Hol W.G.J., Fan E.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Am. Chem. Soc. 124:12991-12998 (2002)Cited in1
The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site.Merritt E.A., Kuhn P., Sarfaty S., Erbe J.L., Holmes R.K., Hol W.G.View abstractCategoriesStructureSourcePDB: 3CHBPubMedEurope PMCJ Mol Biol 282:1043-1059 (1998)Mapped to1
Surprising leads for a cholera toxin receptor-binding antagonist: crystallographic studies of CTB mutants.Merritt E.A., Sarfaty S., Chang T.T., Palmer L.M., Jobling M.G., Holmes R.K., Hol W.G.View abstractCategoriesStructureSourcePDB: 1CHP, PDB: 1CHQPubMedEurope PMCStructure 3:561-570 (1995)Mapped to1
The three-dimensional crystal structure of cholera toxin.Zhang R.-G., Scott D.L., Westbrook M.L., Nance S., Spangler B.D., Shipley G.G., Westbrook E.M.View abstractCategoriesStructureSourcePDB: 1XTCPubMedEurope PMCJ. Mol. Biol. 251:563-573 (1995)Cited in1Mapped to1
Using <i>Vibrio natriegens</i> for High-Yield Production of Challenging Expression Targets and for Protein Perdeuteration.Mojica N., Kersten F., Montserrat-Canals M., Huhn Iii G.R., Tislevoll A.M., Cordara G., Teter K., Krengel U.View abstractCategoriesStructureSourcePDB: 8QREPubMedEurope PMCBiochemistry 63:587-598 (2024)Mapped to2
Cholera toxin B scaffolded, focused SIV V2 epitope elicits antibodies that influence the risk of SIV<sub>mac251</sub> acquisition in macaques.Rahman M.A., Becerra-Flores M., Patskovsky Y., Silva de Castro I., Bissa M., Basu S., Shen X., Williams L.D., Sarkis S.[...], Cardozo T.View abstractCategoriesStructureSourcePDB: 7LVBPubMedEurope PMCFront Immunol 14:1139402-1139402 (2023)Mapped to2
Crystal structures of cholera toxin in complex with fucosylated receptors point to importance of secondary binding site.Heim J.B., Hodnik V., Heggelund J.E., Anderluh G., Krengel U.View abstractCategoriesStructureSourcePDB: 6HJD, PDB: 6HMW, PDB: 6HMYPubMedEurope PMCSci Rep 9:12243-12243 (2019)Mapped to1
Directed Assembly of Homopentameric Cholera Toxin B-Subunit Proteins into Higher-Order Structures Using Coiled-Coil Appendages.Ross J.F., Wildsmith G.C., Johnson M., Hurdiss D.L., Hollingsworth K., Thompson R.F., Mosayebi M., Trinh C.H., Paci E.[...], Turnbull W.B.View abstractCategoriesStructureSourcePDB: 6HSVPubMedEurope PMCJ Am Chem Soc 141:5211-5219 (2019)Mapped to1
Towards new cholera prophylactics and treatment: Crystal structures of bacterial enterotoxins in complex with GM1 mimics.Heggelund J.E., Mackenzie A., Martinsen T., Heim J.B., Cheshev P., Bernardi A., Krengel U.View abstractCategoriesStructureSourcePDB: 5LZG, PDB: 5LZJPubMedEurope PMCSci Rep 7:2326-2326 (2017)Cited in1Mapped to2
High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence.Heggelund J.E., Burschowsky D., Bjornestad V.A., Hodnik V., Anderluh G., Krengel U.View abstractCategoriesStructureSourcePDB: 5ELC, PDB: 5ELE, PDB: 5ELFPubMedEurope PMCPLoS Pathog 12:e1005567-e1005567 (2016)Cited in2Mapped to1