(Q36020146)

English

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

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scholarly article

1 reference

Europe PubMed Central

11 August 2017

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

1 reference

Europe PubMed Central

11 August 2017

author name string

Aharoni A

1

1 reference

Europe PubMed Central

11 August 2017

Horovitz A

2

1 reference

Europe PubMed Central

11 August 2017

language of work or name

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publication date

1 March 1997

1 reference

Europe PubMed Central

11 August 2017

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

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Europe PubMed Central

11 August 2017

94

1 reference

Europe PubMed Central

11 August 2017

1698-1702

1 reference

Europe PubMed Central

11 August 2017

5

1 reference

Europe PubMed Central

11 August 2017

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Hydrogen bonding stabilizes globular proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

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=19979

2 October 2017

Molecular chaperones in protein folding and translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Role of the major heat shock proteins as molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Are buried salt bridges important for protein stability and conformational specificity?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Strength and co-operativity of contributions of surface salt bridges to protein stability

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

2 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

11 July 2018

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

11 July 2018

Additivity of mutational effects in proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

11 July 2018

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

11 July 2018

Positive cooperativity in the functioning of molecular chaperone GroEL

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

11 July 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=19979

23 September 2018

GroE structures galore

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Residue lysine-34 in GroES modulates allosteric transitions in GroEL

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.94.5.1698

21 January 2018

Identifiers

10.1073/PNAS.94.5.1698

1 reference

Europe PubMed Central

11 August 2017

1997PNAS...94.1698A

0 references

1 reference

Europe PubMed Central

11 August 2017

1 reference

Europe PubMed Central

11 August 2017

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