The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. The p88 molecular chaperone is identical to the endoplasmic reticulum membrane protein, calnexin.
2. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.
3. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
4. Differential distribution and modulation of expression of alpha 1/beta 1 integrin on human endothelial cells.
5. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.
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