pubmed-article:3872456 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C1155003 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C0054946 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C1417326 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C1706319 | lld:lifeskim |
pubmed-article:3872456 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
pubmed-article:3872456 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:3872456 | pubmed:dateCreated | 1985-5-3 | lld:pubmed |
pubmed-article:3872456 | pubmed:abstractText | A 35-kDa polypeptide, Bp35, expressed on the surface of all B cells, plays a role in B-cell activation. Monoclonal antibodies to Bp35 stimulate human tonsillar B cells to proliferate. The activation induced by anti-Bp35 is similar to anti-Ig-mediated in several ways: the activation does not require T cells but is augmented by T-cell-derived allogeneic factors; monovalent Fab fragments to Bp35 do not trigger proliferation but instead block activation by whole antibody, indicating that cross-linking is required; and induction by anti-Bp35, like the induction by anti-Ig, is inhibited by monoclonal anti-IgM via an Fc domain-dependent mechanism. However, several features of anti-Bp35-mediated proliferation are clearly different from activation by anti-Ig: anti-Bp35 monoclonal antibodies do not require attachment to beads to function, the proliferation induced by anti-Bp35 and anti-Ig is additive, and Fab fragments of anti-Bp35 augment proliferation induced by anti-Ig. Models for the possible function of the Bp35 polypeptide as either a "bridge" or a "second signal" with surface Ig in B-cell activation are discussed. | lld:pubmed |
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pubmed-article:3872456 | pubmed:language | eng | lld:pubmed |
pubmed-article:3872456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3872456 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3872456 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3872456 | pubmed:month | Mar | lld:pubmed |
pubmed-article:3872456 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:3872456 | pubmed:author | pubmed-author:ClarkE AEA | lld:pubmed |
pubmed-article:3872456 | pubmed:author | pubmed-author:LedbetterJ... | lld:pubmed |
pubmed-article:3872456 | pubmed:author | pubmed-author:SimPP | lld:pubmed |
pubmed-article:3872456 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3872456 | pubmed:volume | 82 | lld:pubmed |
pubmed-article:3872456 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3872456 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3872456 | pubmed:pagination | 1766-70 | lld:pubmed |
pubmed-article:3872456 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:3872456 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:3872456 | pubmed:articleTitle | Role of the Bp35 cell surface polypeptide in human B-cell activation. | lld:pubmed |
pubmed-article:3872456 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3872456 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:3872456 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:3872456 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3872456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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