(Q27734289)

2

0 references

S Perrett

3

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C M Johnson

4

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F J Corrales

5

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R Golbik

6

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A R Fersht

Proceedings of the National Academy of Sciences of the United States of America

7

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language of work or name

English

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publication date

24 December 1996

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published in

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volume

93

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issue

26

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page(s)

15024-9

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cites work

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Detection, delineation, measurement and display of cavities in macromolecular structures

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Raster3D Version 2.0. A program for photorealistic molecular graphics

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Improved methods for building protein models in electron density maps and the location of errors in these models

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Residues in chaperonin GroEL required for polypeptide binding and release

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Protein folding in the cell: competing models of chaperonin function.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Hydrogen Exchange in Proteins

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Positive cooperativity in the functioning of molecular chaperone GroEL

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

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

2 June 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

PROCHECK: a program to check the stereochemical quality of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

AMoRe: an automated package for molecular replacement

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

Accurate bond and angle parameters for X-ray protein structure refinement

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.93.26.15024

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=26349

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

27 November 2018

1 reference

12 December 2020

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

12 December 2020

Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides

1 reference

12 December 2020

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

1 reference

12 December 2020

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1 reference

12 December 2020

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

12 December 2020

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

1 reference

12 December 2020

Refolding of barnase in the presence of GroE

1 reference

12 December 2020

Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.93.26.15024

1 reference

ADS bibcode

1996PNAS...9315024Z

0 references

1 reference

1 reference

PubMed publication ID

8986757

1 reference