(Q24290435)

GOA release 2020-03-11

unfolded protein binding

1 reference

GOA release 2020-03-11

author name string

A Richardson

1

0 references

F Schwager

2

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S J Landry

3

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C Georgopoulos

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

16 February 2001

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published in

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volume

276

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issue

7

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page(s)

4981-7

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cites work

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The ins and outs of a molecular chaperone machine.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Purification and properties of groE, a host protein involved in bacteriophage assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

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.M008628200

ATP induces large quaternary rearrangements in a cage-like chaperonin structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The lid that shapes the pot: structure and function of the chaperonin GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Molecular chaperones. Opening and closing the Anfinsen cage.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

A single ring is sufficient for productive chaperonin-mediated folding in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Characterization of a functionally important mobile domain of GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Interplay of structure and disorder in cochaperonin mobile loops

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Host participation in bacteriophage lambda head assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Studies on transformation of Escherichia coli with plasmids

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Physiological Studies of Conditional Lethal Mutants of Bacteriophage T4D

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Molecular cloning of the DNA ligase gene from bacteriophage T4. I. Characterisation of the recombinants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

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.M008628200

Renaturation of citrate synthase: influence of denaturant and folding assistants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Conserved sequence motifs in bacterial and bacteriophage chaperonins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

BIACORE analysis of histidine-tagged proteins using a chelating NTA sensor chip

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

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.M008628200

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.M008628200

Context is a major determinant of β-sheet propensity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Structure and function in GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

The complete primary structure of rat chaperonin 10 reveals a putative beta alpha beta nucleotide-binding domain with homology to p21ras

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

inferred from DOI database lookup

7 January 2021

based on heuristic

In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

inferred from DOI database lookup

7 January 2021

based on heuristic

A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008628200

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M008628200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11050098

1 reference

Consolidated OpenCitations Corpus – April 2017