Linked Life Data

11965361

Source:http://linkedlifedata.com/resource/pubmed/id/11965361

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2002-4-19
pubmed:abstractText
Deletion of phenylalanine at position 508 of the CFTR protein is associated with a severe form of cystic fibrosis. Biosynthetic arrest of the misfolded DeltaF508 CFTR protein in the endoplasmic reticulum is due to prolonged interaction with protein chaperones. In order to overcome this retention and thereby restore the delivery of the protein to the plasma membrane, a molecular mimic of the glycoprotein oligoside moiety has been designed and synthesized. Ability of this mimic to inhibit the binding of the natural Glc1Man9GlcNAc oligoside to calnexin has been measured.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1237-40
pubmed:dateRevised
2002-11-1
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Synthesis of a molecular mimic of the Glc1Man9 oligoside as potential inhibitor of calnexin binding to DeltaF508 CFTR protein.
pubmed:affiliation
UMR 176 CNRS-Institut Curie, Section de Recherche, 26 rue d'Ulm, 75248 Cedex 05, Paris, France.
pubmed:publicationType
Journal Article