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  • 1
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    Transfer of experimental allergic encephalomyelitis with guinea pig peritoneal exudate cells (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: Incubation with specific antigen, myelin basic protein, greatly enhances the ability of guinea pig peritoneal exudate cells to transfer experimental allergic encephalomyelitis. Reproducibly successful transfers are obtained with 10(7) cells. With this relatively small number of cells, in vitro studies to determine the immunologic mechanisms involved in the disease process are now possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Driscoll, B F -- Kies, M W -- Alvord, E C Jr -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):547-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/83676" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens ; Ascitic Fluid/*cytology/immunology ; Cell Adhesion ; Cell Division ; Encephalomyelitis, Autoimmune, Experimental/immunology/*transmission ; Exudates and Transudates/immunology ; Guinea Pigs ; Immunization, Passive ; Male ; Myelin Basic Protein/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Species restriction of a monoclonal antibody reacting with residues 130 to 137 in encephalitogenic myelin basic protein (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-02
    Description: A monoclonal antibody (immunoglobulin G1) has been produced that reacts against myelin basic protein present in or extracted from the brains of many mammals-with certain important exceptions. Because of known species differences in amino acid sequences of basic protein and of certain peptide fragments, the binding site for this particular antibody appeared likely to include residues 130 to 137. Confirmation of this hypothesis was obtained by amino acid composition of the major immunoreactive peptides produced by thermolysin digestion of human basic protein and isolated by high-performance liquid chromatography.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sires, L R -- Hruby, S -- Alvord, E C Jr -- Hellstrom, I -- Hellstrom, K E -- Kies, M W -- Martemspm, R -- Deibler, G E -- Beckman, E D -- Casnellie, J E -- CA-19148/CA/NCI NIH HHS/ -- CA-25558/CA/NCI NIH HHS/ -- CA-26584/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 2;214(4516):87-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6169147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cattle ; Chickens ; Epitopes ; Guinea Pigs ; Humans ; Macaca ; Myelin Basic Protein/*immunology ; Peptide Fragments/immunology ; Rabbits ; Rats ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Sequence homology between certain viral proteins and proteins related to encephalomyelitis and neuritis (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-19
    Description: Post-infectious or post-vaccinal demyelinating encephalomyelitis and neuritis may be due to immunological cross-reactions evoked by specific viral antigenic determinants (epitopes) that are homologous to regions in the target myelins of the central and peripheral nervous systems. Such homologies have been found by computer searches in which decapeptides in two human myelin proteins were compared with proteins of viruses known to infect humans. These viruses include measles, Epstein-Barr, influenza A and B, and others that cause upper respiratory infections. Several regions identified in myelin basic protein and P2 protein can be related to experimental allergic encephalomyelitis or neuritis in laboratory animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jahnke, U -- Fischer, E H -- Alvord, E C Jr -- AM07902/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):282-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Encephalomyelitis/etiology/immunology/*metabolism ; Epitopes ; Guinea Pigs ; Haplorhini ; Humans ; Measles/metabolism ; Myelin Basic Protein/genetics ; Myelin P2 Protein ; Neuritis/etiology/immunology/*metabolism ; Rabbits ; Rats ; Rats, Inbred Lew ; Viral Proteins/*genetics ; Viral Vaccines/adverse effects/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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