pubmed-article:9844627 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1622537 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1417857 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1420270 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1153543 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:9844627 | lifeskim:mentions | umls-concept:C1177045 | lld:lifeskim |
pubmed-article:9844627 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:9844627 | pubmed:dateCreated | 1998-12-24 | lld:pubmed |
pubmed-article:9844627 | pubmed:abstractText | The structure of 20 S particles, consisting of NSF, SNAPs, and SNARE complexes, was analyzed by electron microscopy and fluorescence resonance energy transfer. Structural changes associated with the binding of alpha-SNAP and NSF to SNARE complexes define the contribution of each component to the 20 S particle structure. The synaptic SNARE complex forms a 2.5 x 15 nm rod. alpha-SNAP binds laterally to the rod, increasing its width but not its length. NSF binds to one end of the SNAP/SNARE complex; the resulting 20 S particles measure 22 nm in length and vary in width from 6 nm at their narrowest point to 13.5 nm at their widest. The transmembrane domains of VAMP and syntaxin emerge together at the NSF-distal end of 20 S particles, adjacent to the amino terminus of alpha-SNAP. | lld:pubmed |
pubmed-article:9844627 | pubmed:language | eng | lld:pubmed |
pubmed-article:9844627 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9844627 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9844627 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9844627 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:EngelhardtHH | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:RothmanJ EJE | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:WimmerCC | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:ParlatiFF | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:SöllnerT HTH | lld:pubmed |
pubmed-article:9844627 | pubmed:author | pubmed-author:HohlT MTM | lld:pubmed |
pubmed-article:9844627 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9844627 | pubmed:volume | 2 | lld:pubmed |
pubmed-article:9844627 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9844627 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9844627 | pubmed:pagination | 539-48 | lld:pubmed |
pubmed-article:9844627 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9844627 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9844627 | pubmed:articleTitle | Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. | lld:pubmed |
pubmed-article:9844627 | pubmed:affiliation | Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA. | lld:pubmed |
pubmed-article:9844627 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9844627 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9844627 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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