A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle-Reference-Cited by-同舟云学术

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A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle

Published:2023-09 Issue:17 Volume:83 Page:3108-3122.e13
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

McQuown Alexander J.,Nelliat Anjali R.,Reif Dvir,Sabbarini Ibrahim M.,Membreno Britnie Santiago,Wu Colin Chih-Chien,Denic Vladimir

Funder

Harvard University

National Science Foundation

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference65 articles.

1. In vivo aspects of protein folding and quality control;Balchin;Science,2016

2. Defining the essential function of yeast Hsf1 reveals a compact transcriptional program for maintaining eukaryotic proteostasis;Solís;Mol. Cell,2016

3. The Hsp70 chaperone network;Rosenzweig;Nat. Rev. Mol. Cell Biol.,2019

4. The HSP90 chaperone machinery;Schopf;Nat. Rev. Mol. Cell Biol.,2017

5. Genetic and epigenetic determinants establish a continuum of Hsf1 occupancy and activity across the yeast genome;Pincus;Mol. Biol. Cell,2018

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1. A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A;2024-02-22

2. Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis;Nature Communications;2024-02-15

3. Ca-dimers, solvent layering, and dominant electrochemically active species in Ca(BH4)2 in THF;Nature Communications;2024-02-15

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