Structural transitions modulate the chaperone activities of Grp94-Reference-Cited by-同舟云学术

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Structural transitions modulate the chaperone activities of Grp94

Published:2024-09 Issue:9 Volume:49 Page:752-753
ISSN:0968-0004
Container-title:Trends in Biochemical Sciences
language:en
Short-container-title:Trends in Biochemical Sciences

Author:

Mirikar Duhita^ORCID,Bushman Yevheniia^ORCID,Truman Andrew W.^ORCID

Funder

NIH

Publisher

Elsevier BV

Reference8 articles.

1. Molecular chaperone GRP94/GP96 in cancers: oncogenesis and therapeutic target;Duan;Front. Oncol.,2021

2. GRP94: an HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum;Marzec;Biochim. Biophys. Acta (BBA) Mol. Cell Res.,2012

3. Structural transitions modulate the chaperone activities of Grp94;Amankwah;Proc. Natl. Acad. Sci. U. S. A.,2024

4. Studying structure and function of membrane proteins with PELDOR/DEER spectroscopy – the crystallographers’ perspective;Glaenzer;Methods,2018

5. Structural and functional analysis of GRP94 in the closed state reveals an essential role for the pre-N domain and a potential client-binding site;Huck;Cell Rep.,2017

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