|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2007-7-2
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|
pubmed:abstractText |
Two types of NP-NP associations are shown to form in the influenza virus-infected cells. Early NP synthesis gives rise to NP associations stabilized by relatively weak bonds. These structures are designed as NP multimers. The high protease- and heat-sensitivities allow NP-multimers to be regarded as incompletely folded proteins. Post-translationally, NP-multimers transform to compact NP associations (NP oligomers) that are relatively highly heat-and protease-resistant. The NP-multimers untransformed to the folded compact NP-oligomers accumulate in the cells and partially degraded. Whether both types of NP-NP associations may be of significance is under discussion.
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pubmed:language |
rus
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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|
pubmed:issn |
0507-4088
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
52
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
9-12
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|
pubmed:dateRevised |
2008-11-21
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|
pubmed:meshHeading |
pubmed-meshheading:17601043-Animals,
pubmed-meshheading:17601043-Cell Line,
pubmed-meshheading:17601043-Hot Temperature,
pubmed-meshheading:17601043-Influenzavirus A,
pubmed-meshheading:17601043-Nucleoproteins,
pubmed-meshheading:17601043-Orthomyxoviridae Infections,
pubmed-meshheading:17601043-Peptide Hydrolases,
pubmed-meshheading:17601043-Protein Folding,
pubmed-meshheading:17601043-Protein Processing, Post-Translational,
pubmed-meshheading:17601043-RNA-Binding Proteins,
pubmed-meshheading:17601043-Species Specificity,
pubmed-meshheading:17601043-Viral Core Proteins
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|
pubmed:articleTitle |
[Two types of NP-NP associations in influenza virus-infected cells].
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pubmed:publicationType |
Journal Article,
English Abstract,
Research Support, Non-U.S. Gov't
|
