| pubmed-article:194063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C1623048 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C1428114 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:194063 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:194063 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:194063 | pubmed:dateCreated | 1977-7-18 | lld:pubmed |
| pubmed-article:194063 | pubmed:abstractText | To delineate the proximity and spatial arrangement of the major structural proteins of intact vesicular stomatitis (VS) virions, protein complexes formed by oxidation or by bivalent cross-linkers were analyzed by two-dimensional electrophoresis on polyacrylamide slab gels. H2O2 oxidation of VS virions produced an N-polypeptide dimer (molecular weight, approximately equal to 110,000) on a first dimension gel that could be reduced to N monomers (molecular weight, approximately equal to 50,000). Proteins extracted from unreduced and unoxidized VS virions contained dimeric and trimeric forms of M-protein complexes as well as a heterodimer of M and N protein. Qualitatively similar VS viral protein complexes were generated by exposing VS virions to the reversible protein cross-linkers methyl-4-mercaptobutyrimidate (MMB), tartryl diazide (TDA), and dithiobis(succinimidyl proprionate) (DTBSP); cross-linked complexes on first-dimension gels were cleaved by reduction with 2-mercaptoethanol (MMB or DTBSP cross-linked) or by periodate oxidation (TDA cross-linked). In addition to covalently linked homodiamers of M and N proteins and a protein M-N heterodimer, the protein cross-linkers also generated homo-oligomers of G protein and a G-M heterodimer. These data suggest that the glycoprotein spike of VS virus is composed of more than one G protein. The existence of N-M and G-M heterodimers is consistent with the hypothesis that the matrix (M) protein may serve as a bridge between the G and N proteins in assembly of the VS virion. | lld:pubmed |
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| pubmed-article:194063 | pubmed:language | eng | lld:pubmed |
| pubmed-article:194063 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:194063 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:194063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:194063 | pubmed:month | May | lld:pubmed |
| pubmed-article:194063 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:194063 | pubmed:author | pubmed-author:WagnerR RRR | lld:pubmed |
| pubmed-article:194063 | pubmed:author | pubmed-author:DuboviE JEJ | lld:pubmed |
| pubmed-article:194063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:194063 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:194063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:194063 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:194063 | pubmed:pagination | 500-9 | lld:pubmed |
| pubmed-article:194063 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:194063 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:194063 | pubmed:articleTitle | Spatial relationships of the proteins of vesicular stomatitis virus: induction of reversible oligomers by cleavable protein cross-linkers and oxidation. | lld:pubmed |
| pubmed-article:194063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:194063 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:194063 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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