| pubmed-article:225539 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0036638 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0392918 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0178774 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0035544 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C0443220 | lld:lifeskim |
| pubmed-article:225539 | lifeskim:mentions | umls-concept:C1522605 | lld:lifeskim |
| pubmed-article:225539 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:225539 | pubmed:dateCreated | 1979-11-28 | lld:pubmed |
| pubmed-article:225539 | pubmed:abstractText | Contacts among the three polypeptide species in the flexible helical nucleocapsids of a paramyxovirus were examined with bifunctional protein cross-linking reagents. Polypeptides L and P, minor components of Sendai virus nucleocapsids implicated in viral RNA polymerase activity, were efficiently cross-linked into large complexes, indicating that they enjoy abundant contacts with neighboring protein molecules in the helix. Less reactivity was found in the case of the major structural polypeptide, NP; about half of all molecules of NP formed large cross-linked complexes, most of the rest remaining as monomers along with a small proportion of homodimers and low-order oligomers. Marked heterogeneity in the cross-linking reactivity of NP molecules, which may reflect the conformational quasi-equivalence inherent in a flexible helix, was indicated by the production of several conformers of homodimers and other low-order oligomers of NP, and by failure of the kinetics of NP cross-linking to conform to a simple statistical model of random polmerization. The validity of the statistical model was shown by cross-linking experiments with the rigid helical virus, tobacco mosaic virus. | lld:pubmed |
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| pubmed-article:225539 | pubmed:language | eng | lld:pubmed |
| pubmed-article:225539 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:225539 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:225539 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:225539 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:225539 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:225539 | pubmed:author | pubmed-author:GeorgeSS | lld:pubmed |
| pubmed-article:225539 | pubmed:author | pubmed-author:KingsburyD... | lld:pubmed |
| pubmed-article:225539 | pubmed:author | pubmed-author:PortnerAA | lld:pubmed |
| pubmed-article:225539 | pubmed:author | pubmed-author:RaghowRR | lld:pubmed |
| pubmed-article:225539 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:225539 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:225539 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:225539 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:225539 | pubmed:pagination | 701-10 | lld:pubmed |
| pubmed-article:225539 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:225539 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:225539 | pubmed:articleTitle | Topography of a flexible ribonucleoprotein helix: protein-protein contacts in Sendai virus nucleocapsids. | lld:pubmed |
| pubmed-article:225539 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:225539 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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