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Literature DB >> 28880864

Identification of an allosteric network that influences assembly and function of group II chaperonins.

Mingliang Jin¹, Yao Cong¹.

Abstract

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Substances：

Year: 2017 PMID： 28880864 DOI： 10.1038/nsmb.3459

Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369

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20 in total

1. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis.

Authors: Dalia Rivenzon-Segal; Sharon G Wolf; Liat Shimon; Keith R Willison; Amnon Horovitz
Journal: Nat Struct Mol Biol Date: 2005-02-06 Impact factor: 15.369

2. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.

Authors: Stefanie Reissmann; Charles Parnot; Christopher R Booth; Wah Chiu; Judith Frydman
Journal: Nat Struct Mol Biol Date: 2007-04-29 Impact factor: 15.369

Review 3. In vivo aspects of protein folding and quality control.

Authors: David Balchin; Manajit Hayer-Hartl; F Ulrich Hartl
Journal: Science Date: 2016-07-01 Impact factor: 47.728

4. The molecular architecture of the eukaryotic chaperonin TRiC/CCT.

Authors: Alexander Leitner; Lukasz A Joachimiak; Andreas Bracher; Leonie Mönkemeyer; Thomas Walzthoeni; Bryan Chen; Sebastian Pechmann; Susan Holmes; Yao Cong; Boxue Ma; Steve Ludtke; Wah Chiu; F Ulrich Hartl; Ruedi Aebersold; Judith Frydman
Journal: Structure Date: 2012-04-12 Impact factor: 5.006

5. Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.

Authors: Yunxiang Zang; Mingliang Jin; Huping Wang; Zhicheng Cui; Liangliang Kong; Caixuan Liu; Yao Cong
Journal: Nat Struct Mol Biol Date: 2016-10-24 Impact factor: 15.369

6. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

Authors: O Yifrach; A Horovitz
Journal: J Mol Biol Date: 1994-10-28 Impact factor: 5.469

Identification of an allosteric network that influences assembly and function of group II chaperonins.

1. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis.

2. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.

Review 3. In vivo aspects of protein folding and quality control.

4. The molecular architecture of the eukaryotic chaperonin TRiC/CCT.

5. Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.

6. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

7. Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.

8. Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.

9. Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.

10. Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC.