Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL-Reference-Cited by-同舟云学术

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Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL

Published:2019-01 Issue:1 Volume:116 Page:42-48
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Bandyopadhyay Boudhayan,Mondal Tridib,Unger Ron,Horovitz Amnon

Funder

Minerva Foundation

Federal German Ministry for Education and Research

US-Israel Binational Science Foundation

Israel Science Foundation

Publisher

Elsevier BV

Subject

Biophysics

Reference33 articles.

1. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP;Goloubinoff;Nature,1989

2. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis;Ostermann;Nature,1989

3. Structure and allostery of the chaperonin GroEL;Saibil;J. Mol. Biol,2013

4. The GroEL-GroES chaperonin machine: a nano-cage for protein folding;Hayer-Hartl;Trends Biochem. Sci,2016

5. Allosteric mechanisms in chaperonin machines;Gruber;Chem. Rev,2016

Cited by 11 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. Synonymous and non‐synonymous codon substitutions can alleviate dependence on GroEL for folding;Protein Science;2024-07-29

2. Bis-sulfonamido-2-phenylbenzoxazoles Validate the GroES/EL Chaperone System as a Viable Antibiotic Target;Journal of the American Chemical Society;2024-07-23

3. Prediction of chaperonin GroE substrates using small structural patterns of proteins;FEBS Open Bio;2023-03-14

4. In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution;Frontiers in Molecular Biosciences;2023-02-10

5. Friends in need: How chaperonins recognize and remodel proteins that require folding assistance;Frontiers in Molecular Biosciences;2022-11-21

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