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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
1996-8-20
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pubmed:abstractText |
Calnexin (CNX) is a membrane-bound molecular chaperone that associates with newly synthesized proteins in the endoplasmic reticulum. Although several studies have indicated that it interacts exclusively with glycoproteins that carry monoglucosylated N-linked oligosaccharides, others have reported that it can bind to proteins that have no glycans. To address this discrepancy, we translated wild-type vesicular stomatitis virus G protein and nonglycosylated mutant forms in the presence of microsomes and examined their association with CNX. Individual G protein molecules were found to efficiently associate with CNX when both glycans were present and less efficiently if there was only a single glycan. Nonglycosylated G protein also interacted with CNX, but only when misfolded and present in high molecular weight aggregates. The results indicated that CNX can interact with G protein in two ways: through an oligosaccharide-dependent mechanism that involves individual substrate proteins; and in an oligosaccharide-independent association with large aggregates.
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pubmed:grant |
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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 |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14280-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8662990-Amino Acid Sequence,
pubmed-meshheading:8662990-Animals,
pubmed-meshheading:8662990-Calcium-Binding Proteins,
pubmed-meshheading:8662990-Calnexin,
pubmed-meshheading:8662990-Consensus Sequence,
pubmed-meshheading:8662990-Glycoproteins,
pubmed-meshheading:8662990-Glycosylation,
pubmed-meshheading:8662990-Membrane Glycoproteins,
pubmed-meshheading:8662990-Microsomes,
pubmed-meshheading:8662990-Molecular Chaperones,
pubmed-meshheading:8662990-Molecular Sequence Data,
pubmed-meshheading:8662990-Mutagenesis,
pubmed-meshheading:8662990-Plasmids,
pubmed-meshheading:8662990-Point Mutation,
pubmed-meshheading:8662990-Protein Biosynthesis,
pubmed-meshheading:8662990-Protein Folding,
pubmed-meshheading:8662990-Rabbits,
pubmed-meshheading:8662990-Recombinant Proteins,
pubmed-meshheading:8662990-Reticulocytes,
pubmed-meshheading:8662990-Sequence Deletion,
pubmed-meshheading:8662990-Transcription, Genetic,
pubmed-meshheading:8662990-Transfection,
pubmed-meshheading:8662990-Vesicular stomatitis Indiana virus,
pubmed-meshheading:8662990-Viral Envelope Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin.
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pubmed:affiliation |
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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