Literature DB >> 8203019

Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.

J J Bergeron1, M B Brenner, D Y Thomas, D B Williams.   

Abstract

Calnexin is a new type of molecular chaperone that interacts with many nascent membrane and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular chaperones of the Hsp60, Hsp70 and Hsp90 families, and is further distinguished from them in that it is an integral membrane protein. One of its demonstrated functions is the retention of incorrectly or incompletely folded proteins, suggesting that calnexin is a component of the quality control system of the endoplasmic reticulum.

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Year:  1994        PMID： 8203019     DOI： 10.1016/0968-0004(94)90205-4

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN： 0968-0004            Impact factor:   13.807


  146 in total

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8.  The Binding Protein Associates with Monomeric Phaseolin.

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9.  Type I transglutaminase accumulation in the endoplasmic reticulum may be an underlying cause of autosomal recessive congenital ichthyosis.

Authors:  Haibing Jiang; Ralph Jans; Wen Xu; Ellen A Rorke; Chen-Yong Lin; Ya-Wen Chen; Shengyun Fang; Yongwang Zhong; Richard L Eckert
Journal:  J Biol Chem       Date:  2010-07-27       Impact factor: 5.157

10.  Synthesis of fluorine substituted oligosaccharide analogues of monoglucosylated glycan chain, a proposed ligand of lectin-chaperone calreticulin and calnexin.

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Journal:  Glycoconj J       Date:  2004       Impact factor: 2.916
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