A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization-Reference-Cited by-同舟云学术

A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization

Published:2021-12 Issue:12 Volume:29 Page:1357-1370.e6
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Okumura Masaki^ORCID,Kanemura Shingo^ORCID,Matsusaki Motonori,Kinoshita Misaki,Saio Tomohide,Ito Dai,Hirayama Chihiro,Kumeta Hiroyuki^ORCID,Watabe Mai,Amagai Yuta^ORCID,Lee Young-Ho,Akiyama Shuji,Inaba Kenji^ORCID

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference45 articles.

1. Quality control of protein standards for molecular mass determinations by small-angle X-ray scattering;Akiyama;J. Appl. Crystallogr.,2010

2. Local unfolding of the HSP27 monomer regulates chaperone activity;Alderson;Nat. Commun.,2019

3. Analysis of chaperone function using citrate synthase as nonnative substrate protein;Buchner;Methods Enzymol.,1998

4. Multiple ways to make disulfides;Bulleid;Trends Biochem. Sci.,2011

5. The inhibitory effect of PDIA6 downregulation on bladder cancer cell proliferation and invasion;Cheng;Oncol. Res.,2017

Cited by 13 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A functional chaperone condensate in the endoplasmic reticulum;2024-08-20

2. Ca²⁺-driven PDIA6 phase separation to ensure proinsulin quality control;2024-07-30

3. Client recognition differences between PDI and ERp46 to guide oxidative folding;2024-03-08

4. Characterization of ATP hydrolysis in the Hsp70 BiP nucleotide binding domain;2024-03-07

5. Enzymatic and synthetic regulation of polypeptide folding;Chemical Science;2024