Ligand Interactions in the Adenosine Nucleotide-binding Domain of the Hsp90 Chaperone, GRP94
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference69 articles.
1. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.
2. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
3. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells.
4. A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
5. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation.
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