Linked Life Data

1599754

Source:http://linkedlifedata.com/resource/pubmed/id/1599754

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-7-16
pubmed:abstractText
Kinetic and thermodynamic aspects of the binding of sCD4 to intact virions of human immunodeficiency virus type 1 (HIV-1 RF), and of the subsequent induction of gp120 dissociation were studied. sCD4 binding to virions at 4 and 37 degrees C is half-maximal at approximately 40 and 10 nM, respectively. The transition between low-affinity and high-affinity binding of sCD4 to virions occurs over a narrow temperature range between 20 and 25 degrees C. Shedding of gp120 from virions after sCD4 binding is also temperature dependent, being initiated above approximately 20 degrees C. The minimum temperatures for the sCD4 affinity transition and gp120 shedding are, therefore, similar and we suggest how the two processes might be related mechanistically.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0889-2229
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Thermodynamic and kinetic analysis of sCD4 binding to HIV-1 virions and of gp120 dissociation.
pubmed:affiliation
Chester Beatty Laboratory, Institute of Cancer Research, London, England.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't