Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity (Q41542224)

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scientific article published on December 1, 1992

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English	Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity	scientific article published on December 1, 1992

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scholarly article

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2 October 2017

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

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2 October 2017

protein folding

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Franz-Ulrich Hartl

5

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Hartl FU

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2 October 2017

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T. Langer

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1361169

18 September 2022

G. Pfeifer

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18 September 2022

J. Martin

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18 September 2022

W. Baumeister

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18 September 2022

F. U. Hartl

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18 September 2022

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1 December 1992

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2 October 2017

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https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1361169/?tool=EBI

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18 September 2022

https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1361169/pdf/?tool=EBI

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18 September 2022

https://europepmc.org/articles/PMC556951

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18 September 2022

https://europepmc.org/articles/PMC556951?pdf=render

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18 September 2022

The EMBO Journal

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2 October 2017

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2 October 2017

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2 October 2017

4757-4765

1 reference

Europe PubMed Central

PMC publication ID

2 October 2017

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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Purification and properties of the groES morphogenetic protein of Escherichia coli

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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Luminescent immunodetection of western-blotted proteins from coomassie-stained polyacrylamide gel.

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The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

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Electron microscopy and image analysis reveal common principles of organization in two large protein complexes: groEL-type proteins and proteasomes.

1 reference

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6 June 2018

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding

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Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast

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Protein folding in the cell

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6 June 2018

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

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6 June 2018

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

1 reference

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6 June 2018

GroE prevents the accumulation of early folding intermediates of pre-beta-lactamase without changing the folding pathway.

1 reference

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Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60

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Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum

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Renaturation of citrate synthase: influence of denaturant and folding assistants

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6 June 2018

Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL

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6 June 2018

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

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6 June 2018

Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

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Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro

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Positive cooperativity in the functioning of molecular chaperone GroEL

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Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring

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Proteins as molecular chaperones.

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Reversible folding of rhodanese. Presence of intermediate(s) at equilibrium

1 reference

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The "EM" program system

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Assay of proteins in the presence of interfering materials

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Unfolding protein folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

https://pubmed.ncbi.nlm.nih.gov/1361169

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/J.1460-2075.1992.TB05581.X

1 reference

National Center for Biotechnology Information

PubMed publication ID

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1361169

18 September 2022

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 October 2017

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