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rdf:type |
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lifeskim:mentions |
umls-concept:C0017968,
umls-concept:C0021051,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0086418,
umls-concept:C0178539,
umls-concept:C0243126,
umls-concept:C0682323,
umls-concept:C1325725,
umls-concept:C1524062,
umls-concept:C1704675
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pubmed:issue |
1
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pubmed:dateCreated |
1998-12-17
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pubmed:abstractText |
We examined the concepts of whether cellular surface glycoprotein overexpressed in heterologous cells can be efficiently incorporated into lentiviral particles and whether incorporation is blocked when a natural interaction partner is coexpressed. Human CD4 and a truncated version lacking the cytoplasmic C terminus, expressed in 293T cells, were efficiently incorporated into Env-defective human immunodeficiency virus type 1 virus-like particles. However, on coexpression of p56(lck), the natural binding partner of the CD4 C-terminal domain in T lymphocytes, incorporation of the wild-type CD4 was completely abolished, whereas incorporation of the C-terminally truncated mutant remained unaffected. Confocal microscopy and detergent solubility assays did not reveal any significant difference in the distribution of wild-type CD4 at the plasma membrane in the presence or absence of p56(lck). These results give some insight into the processes governing protein incorporation into the lipid bilayer of lentiviruses.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, env,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, gag,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/germ-cell AP isoenzyme
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1998 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16-21
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9813198-Alkaline Phosphatase,
pubmed-meshheading:9813198-Antigens, CD4,
pubmed-meshheading:9813198-Blotting, Western,
pubmed-meshheading:9813198-Cell Line,
pubmed-meshheading:9813198-Cell Membrane,
pubmed-meshheading:9813198-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:9813198-Gene Products, env,
pubmed-meshheading:9813198-Gene Products, gag,
pubmed-meshheading:9813198-Glycoproteins,
pubmed-meshheading:9813198-HIV-1,
pubmed-meshheading:9813198-Humans,
pubmed-meshheading:9813198-Isoenzymes,
pubmed-meshheading:9813198-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:9813198-Octoxynol,
pubmed-meshheading:9813198-Sequence Deletion,
pubmed-meshheading:9813198-Solubility,
pubmed-meshheading:9813198-Transfection,
pubmed-meshheading:9813198-Virion
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pubmed:year |
1998
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pubmed:articleTitle |
Inhibition of cellular glycoprotein incorporation into human immunodeficiency virus-like particles by coexpression of additional cellular interaction partner.
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pubmed:affiliation |
Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, Heidelberg, 69120, Germany.
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pubmed:publicationType |
Journal Article
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