pubmed-article:6224488 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C0008537 | lld:lifeskim |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C0103408 | lld:lifeskim |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
pubmed-article:6224488 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:6224488 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:6224488 | pubmed:dateCreated | 1983-9-9 | lld:pubmed |
pubmed-article:6224488 | pubmed:abstractText | The calcium dependence of the binding of synexin to isolated chromaffin granules has been investigated. The calcium dependence was found to be pH sensitive, binding occurring at higher Ca2+ concentrations at lower values of pH. At pH 7.2 half-maximal binding occurred at 4 microM Ca2+. This is a lower Ca2+ concentration than the 200 microM that is required to give half-maximal self-association of synexin or membrane aggregation by synexin. The data therefore suggest that in the chromaffin cell stimulated to release catecholamines and proteins by exocytosis synexin first binds to membranes and then associates with itself to draw membranes together in preparation for fusion. | lld:pubmed |
pubmed-article:6224488 | pubmed:language | eng | lld:pubmed |
pubmed-article:6224488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6224488 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6224488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6224488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6224488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6224488 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6224488 | pubmed:month | Jul | lld:pubmed |
pubmed-article:6224488 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:6224488 | pubmed:author | pubmed-author:CreutzC ECE | lld:pubmed |
pubmed-article:6224488 | pubmed:author | pubmed-author:SternerD CDC | lld:pubmed |
pubmed-article:6224488 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6224488 | pubmed:day | 18 | lld:pubmed |
pubmed-article:6224488 | pubmed:volume | 114 | lld:pubmed |
pubmed-article:6224488 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6224488 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6224488 | pubmed:pagination | 355-64 | lld:pubmed |
pubmed-article:6224488 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:6224488 | pubmed:year | 1983 | lld:pubmed |
pubmed-article:6224488 | pubmed:articleTitle | Calcium dependence of the binding of synexin to isolated chromaffin granules. | lld:pubmed |
pubmed-article:6224488 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6224488 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:6224488 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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