Linked Life Data

12009869

Source:http://linkedlifedata.com/resource/pubmed/id/12009869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-15
pubmed:abstractText
The nucleocapsid protein (NC) of retroviruses is involved in viral RNA packaging and initiation of reverse transcription. NC also mediates interactions between Gag and actin filaments. We found that residues at the amino terminus of NC are involved in efficient actin binding. When alanine residues were substituted for the arginine and lysine at positions 10 and 11 of NC in HIV(NL4-3), these mutations decreased actin binding but had only a modest effect on virus infectivity. A similarly mutated virus based on the HXB2 clone of HIV was not infectious. Mutational analysis of NL4-3 NC residues demonstrated that NC polymorphisms modulated the phenotype of NC mutations. Conservative amino acid differences between HXB2 and NL4-3 NCs were sufficient to explain the difference in infectivity of viruses carrying the R10A and K11A mutations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Human immunodeficiency virus nucleocapsid protein polymorphisms modulate the infectivity of RNA packaging mutants.
pubmed:affiliation
Department of Pediatrics, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1732, USA. pkrogstad@mednet.ucla.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't