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Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

dc.contributor.authorCaamano, Claudio A.en_US
dc.contributor.authorZand, Roberten_US
dc.date.accessioned2006-04-07T20:46:00Z
dc.date.available2006-04-07T20:46:00Z
dc.date.issued1989-07en_US
dc.identifier.citationCaamano, Claudio A., Zand, Robert (1989/07)."Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein." FEBS Letters 252(1-2): 88-90. <http://hdl.handle.net/2027.42/27860>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T36-447NVY9-1G6/2/87b9cc96472fc9938446313be13126c8en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/27860
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2474454&dopt=citationen_US
dc.description.abstractRecent reports that myelin basic protein (MBP) can be ADP-ribosylated and contains specific sites that bind GTP and GM1 ganglioside, have suggested an analogy to the properties of cholera toxin. Comparisons of pairs of sequences between these two proteins yielded two regions of homology between MBP and the cholera toxin B (chol B) subunit, and one region of homology with the cholera toxin A (chol A) subunit. The matching sites within chol B consisted of a 17 amino acid residue sequence (residues 30-46 in chol B and residues 102-118 in human-MBP, hMBP, pppE. coli toxin, the homology is also valid for the same sequences in this toxin. The highly antigenic behavior of MBP that is related to the induction of experimental allergic encephalomyelitis may be paralleled by comparable neural pathology from the homologous regions of cholera toxin.en_US
dc.format.extent293496 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleHomologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic proteinen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-2099, USAen_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-2099, USAen_US
dc.identifier.pmid2474454en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/27860/1/0000273.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0014-5793(89)80894-4en_US
dc.identifier.sourceFEBS Lettersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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