Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein
dc.contributor.author | Caamano, Claudio A. | en_US |
dc.contributor.author | Zand, Robert | en_US |
dc.date.accessioned | 2006-04-07T20:46:00Z | |
dc.date.available | 2006-04-07T20:46:00Z | |
dc.date.issued | 1989-07 | en_US |
dc.identifier.citation | Caamano, 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.uri | http://www.sciencedirect.com/science/article/B6T36-447NVY9-1G6/2/87b9cc96472fc9938446313be13126c8 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/27860 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2474454&dopt=citation | en_US |
dc.description.abstract | Recent 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.extent | 293496 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-2099, USA | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-2099, USA | en_US |
dc.identifier.pmid | 2474454 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/27860/1/0000273.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0014-5793(89)80894-4 | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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