GroEL Ring Separation and Exchange in the Chaperonin Reaction-Reference-Cited by-同舟云学术

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GroEL Ring Separation and Exchange in the Chaperonin Reaction

Published:2018-01 Issue:3 Volume:172 Page:605-617.e11
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Yan Xiao,Shi Qiaoyun,Bracher Andreas,Miličić Goran,Singh Amit K.,Hartl F. Ulrich,Hayer-Hartl Manajit

Funder

Minerva Foundation

Munich Center for Integrated Protein Science

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference70 articles.

1. MASSIF-1: a beamline dedicated to the fully automatic characterization and data collection from crystals of biological macromolecules;Bowler;J. Synchrotron Radiat.,2015

2. Release of both native and non-native proteins from a cis-only GroEL ternary complex;Burston;Nature,1996

3. Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K;Cabo-Bilbao;J. Struct. Biol.,2006

4. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics;Chaudhry;EMBO J.,2003

5. MolProbity: all-atom structure validation for macromolecular crystallography;Chen;Acta Crystallogr. D Biol. Crystallogr.,2010

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1. Visualizing chaperonin function in situ by cryo-electron tomography;Nature;2024-08-21

2. Entering deeper into the mysteries of the GroEL–GroES nanomachine;Current Opinion in Microbiology;2024-06

3. Structural insights into thermophilic chaperonin complexes;Structure;2024-06

4. Dicarboxylic acids synergize with yeast and human Hsp60/10 systems to mimic GroEL/ES;2024-05-15

5. Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies;Trends in Biochemical Sciences;2024-01

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