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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-2-7
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pubmed:abstractText |
Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. Binding was independent of the conformation of the glycoprotein. Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively as a lectin.
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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/4-nitrophenyl-alpha-glucosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosyl-Glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide-N4-(N-acetyl-beta-glucosamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Diphosphate Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease B
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-38
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9019402-Amidohydrolases,
pubmed-meshheading:9019402-Animals,
pubmed-meshheading:9019402-Calcium-Binding Proteins,
pubmed-meshheading:9019402-Calnexin,
pubmed-meshheading:9019402-Cattle,
pubmed-meshheading:9019402-Dogs,
pubmed-meshheading:9019402-Glucosyltransferases,
pubmed-meshheading:9019402-Glycosylation,
pubmed-meshheading:9019402-Hexosaminidases,
pubmed-meshheading:9019402-Isomerases,
pubmed-meshheading:9019402-Mannose,
pubmed-meshheading:9019402-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:9019402-Models, Chemical,
pubmed-meshheading:9019402-Oligosaccharides,
pubmed-meshheading:9019402-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:9019402-Protein Binding,
pubmed-meshheading:9019402-Protein Conformation,
pubmed-meshheading:9019402-Protein Disulfide-Isomerases,
pubmed-meshheading:9019402-Protein Folding,
pubmed-meshheading:9019402-Rats,
pubmed-meshheading:9019402-Ribonucleases,
pubmed-meshheading:9019402-Substrate Specificity,
pubmed-meshheading:9019402-Uridine Diphosphate Glucose,
pubmed-meshheading:9019402-alpha-Glucosidases
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pubmed:year |
1997
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pubmed:articleTitle |
Conformation-independent binding of monoglucosylated ribonuclease B to calnexin.
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pubmed:affiliation |
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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