Linked Life Data

9765412

Source:http://linkedlifedata.com/resource/pubmed/id/9765412

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1998-11-5
pubmed:abstractText
Calnexin is an endoplasmic reticulum (ER)-associated molecular chaperone proposed to promote folding and assembly of glycoproteins that traverse the secretory pathway in eukaryotic cells. In this study we examined if calnexin interacts with the ER-associated luminal (VP7) and transmembrane (NSP4) proteins of rotavirus. Only glycosylated NSP4 interacted with calnexin and did so in a time-dependent manner (half-life, 20 min). In vitro translation experiments programmed with gene 10 of rhesus rotavirus confirmed that calnexin recognizes only glycosylated NSP4. Castanospermine (a glucosidase I and II inhibitor) experiments established that calnexin associates only with partly deglucosylated (di- or monoglucosylated) NSP4. Furthermore, enzymatic removal of the remaining glucose residues on the N-linked glycan units was essential to disengage the NSP4-calnexin complex. Novel experiments with castanospermine revealed that glucose trimming and the calnexin-NSP4 interaction were not critical for the assembly of infectious virus.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-1322608, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-1582407, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-1900540, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2431540, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2457279, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2538241, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2545040, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2548854, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2552139, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2556635, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2826493, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2995404, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-2999159, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-3896128, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-6313296, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-6327729, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7541532, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7592804, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7626608, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7729412, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7736594, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7745732, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7822419, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7876241, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-7939687, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8027184, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8035518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8049518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8102790, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8254749, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8302866, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8534914, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8600515, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8610447, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8642648, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8662990, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8670797, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8672443, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8763990, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8794341, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-8824414, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-9348279, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-9371607, http://linkedlifedata.com/resource/pubmed/commentcorrection/9765412-9557673
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrophenyl-alpha-glucosidase, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calnexin, http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/NS28 protein, rotavirus, http://linkedlifedata.com/resource/pubmed/chemical/Toxins, Biological, http://linkedlifedata.com/resource/pubmed/chemical/VP7 protein, Rotavirus, http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins, http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8705-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
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