In vivo and in vitro function of GroEL mutants with impaired allosteric properties (Q38308570)

2 September 2017

In vivo and in vitro function of GroEL mutants with impaired allosteric properties (English)

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2 September 2017

Fridmann Y

1

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2 September 2017

Ulitzur S

series ordinal

2

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2 September 2017

Horovitz A

series ordinal

3

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2 September 2017

language of work or name

English

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publication date

1 December 2000

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Journal of Biological Chemistry

2 September 2017

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2 September 2017

275

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2 September 2017

48

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2 September 2017

37951-37956

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Principles of protein folding in the cellular environment

2 September 2017

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https://api.crossref.org/works/10.1074%2FJBC.M007594200

Structural aspects of GroEL function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Coupling between protein folding and allostery in the GroE chaperonin system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

In vivo activities of GroEL minichaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

GroEL-GroES-mediated protein folding requires an intact central cavity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Detection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 degrees C but not at 43 degrees C.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

The emergence of the chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). II. The propagation of phage lambda

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Host participation in bacteriophage lambda head assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Cleavage of head and tail proteins during bacteriophage T5 assembly: Selective host involvement in the cleavage of a tail protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

A factor preventing the major head protein of bacteriophage T4 from random aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Evidence that GroEL, not sigma 32, is involved in transcriptional regulation of the Vibrio fischeri luminescence genes in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

GroESL proteins facilitate binding of externally added inducer by LuxR protein-containing E. coli cells.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Structure and function in GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007594200

21 January 2018

Identifiers

DOI

10.1074/JBC.M007594200

1 reference

2 September 2017

1 reference