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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5296
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pubmed:dateCreated |
1997-1-17
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pubmed:abstractText |
Calnexin and calreticulin interact specifically with newly synthesized glycoproteins in the endoplasmic reticulum (ER) and function as molecular chaperones. The carbohydrate-specific interactions between ER components and glycoproteins synthesized in isolated canine pancreatic microsomes were analyzed using a cross-linking approach. A carbohydrate-dependent interaction between newly synthesized glycoproteins, the thiol-dependent reductase ERp57, and either calnexin or calreticulin was identified. The interaction between ERp57 and the newly synthesized glycoproteins required trimming of the N-linked oligosaccharide side chain. Thus, it is likely that ERp57 functions as part of the glycoprotein-specific quality control machinery operating in the lumen of the ER.
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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/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indolizines,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/MF alpha protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Prolactin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/castanospermine
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
86-8
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:8974399-Animals,
pubmed-meshheading:8974399-Calcium-Binding Proteins,
pubmed-meshheading:8974399-Calnexin,
pubmed-meshheading:8974399-Calreticulin,
pubmed-meshheading:8974399-Dogs,
pubmed-meshheading:8974399-Endoplasmic Reticulum,
pubmed-meshheading:8974399-Enzyme Inhibitors,
pubmed-meshheading:8974399-Fungal Proteins,
pubmed-meshheading:8974399-Glucose,
pubmed-meshheading:8974399-Glucosidases,
pubmed-meshheading:8974399-Glycoproteins,
pubmed-meshheading:8974399-Glycosylation,
pubmed-meshheading:8974399-Heat-Shock Proteins,
pubmed-meshheading:8974399-Indolizines,
pubmed-meshheading:8974399-Isomerases,
pubmed-meshheading:8974399-Microsomes,
pubmed-meshheading:8974399-Molecular Weight,
pubmed-meshheading:8974399-Oxidoreductases,
pubmed-meshheading:8974399-Pancreas,
pubmed-meshheading:8974399-Prolactin,
pubmed-meshheading:8974399-Protein Precursors,
pubmed-meshheading:8974399-Ribonucleoproteins,
pubmed-meshheading:8974399-Saccharomyces cerevisiae Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins.
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pubmed:affiliation |
School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester M13 9PT, UK. shigh@fs2.scg.man.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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