Linked Life Data

11886273

Source:http://linkedlifedata.com/resource/pubmed/id/11886273

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-3-11
pubmed:abstractText
Gag polyprotein precursors play an essential role in the assembly of the HIV particle by polymerizing into a spherical shell at the plasma membrane. In order to define the domains within Gag responsible for this homotypic interaction, we have coupled the technology of the yeast two-hybrid system with the technology of a gene-based, semirandom library. By this method, we have identified a minimal region of Gag capable of efficient self-interaction. This region consists of the N-terminal portion of the nucleocapsid protein (NC), including the first zinc finger and the previously described interaction, or I, domain. In parallel with this randomized approach, individual HIV Gag domains, and combinations of these domains, were tested for potential homotypic and heterotypic interactions in the yeast two-hybrid system. Consistent with the results from the semirandom library screen, only combinations of species containing NC were strongly interacting.
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:copyrightInfo
(C)2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-50
pubmed:dateRevised
2011-5-2
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Identification of a minimal HIV-1 gag domain sufficient for self-association.
pubmed:affiliation
Department of Microbiology and Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73190, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.