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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
2004-6-23
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pubmed:abstractText |
Many viruses have evolved fusion-mediating glycoproteins that couple the energy released from irreversible protein refolding to the work of membrane fusion. The viral fusion proteins require a triggering event to undergo a cascade of tightly regulated conformational changes. Different isolates of the paramyxovirus SV5 fusion (F) protein have either a short (20-residue) or long (42-residue) cytoplasmic tail (CT), and a long CT suppresses fusion activity in a sequence-specific manner. Addition of a domain to the F protein CT, which has the propensity to form a three-helix bundle, stabilizes the F protein and increases the energy required for fusion activation. Quantitative cell-cell fusion assays and measurement of ectodomain conformation by monoclonal antibody reactivity indicate that this suppression of fusion by the long CT or addition of a three-helix bundle occurs at a step preceding initial membrane merger. The data suggest that F protein activation involves CT signaling to the ectodomain.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-10675409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-10772976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-10966468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11038187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11062565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11395423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11483506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11533163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-11861835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-12359434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-12477822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-12502845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-12743308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-12919735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-14581458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-14694135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-15298170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-1602561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-2445904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-3865176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-6947213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8107239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8116239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8207836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8248779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8741847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-8970739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-9356337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15197264-9546217
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9217-22
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15197264-Amino Acid Sequence,
pubmed-meshheading:15197264-Animals,
pubmed-meshheading:15197264-Antibodies, Monoclonal,
pubmed-meshheading:15197264-Cattle,
pubmed-meshheading:15197264-Cell Line,
pubmed-meshheading:15197264-Cercopithecus aethiops,
pubmed-meshheading:15197264-Conserved Sequence,
pubmed-meshheading:15197264-Cricetinae,
pubmed-meshheading:15197264-Cytoplasm,
pubmed-meshheading:15197264-Giant Cells,
pubmed-meshheading:15197264-Humans,
pubmed-meshheading:15197264-Kidney,
pubmed-meshheading:15197264-Molecular Sequence Data,
pubmed-meshheading:15197264-Protein Conformation,
pubmed-meshheading:15197264-Recombinant Proteins,
pubmed-meshheading:15197264-Sequence Alignment,
pubmed-meshheading:15197264-Sequence Homology, Amino Acid,
pubmed-meshheading:15197264-Signal Transduction,
pubmed-meshheading:15197264-Transfection,
pubmed-meshheading:15197264-Vero Cells,
pubmed-meshheading:15197264-Viral Fusion Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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