Linked Life Data

8623521

Source:http://linkedlifedata.com/resource/pubmed/id/8623521

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-6-19
pubmed:abstractText
The Sindbis virus glycoproteins E1 and E2 are organized into 80 trimers of heterodimers within the virus envelope. Using pulse-chase protocols and chemical crosslinkers, we have found that E1 and E2 precursor, PE2, rapidly assemble into heterodimers and then into trimers of heterodimers after translocation into the endoplasmic reticulum. E1 folds into its mature conformation within the endoplasmic reticulum via at least three intermediates differing in the configurations of their disulfide bonds. PE2 can pair with the second of these E1 folding intermediates. The remaining E1 folding steps, therefore, occur after E1-PE2 multimers begin to form. Quaternary interactions between E1 and PE2 may help guide the folding of E1. While no PE2 folding intermediates have yet been detected, we have found that PE2 transiently enters into large, noncovalent complexes or aggregates with other PE2 molecules and/or with unknown host factors prior to pairing with E1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
219
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Assembly of the Sindbis virus spike protein complex.
pubmed:affiliation
Department of Microbiology, University of Texas at Austin 78713-7640, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't