Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. (Q35914576)

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scientific article published in November 1996

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English	Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.	scientific article published in November 1996

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scholarly article

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Europe PubMed Central

PMC publication ID

452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

title

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

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Europe PubMed Central

PMC publication ID

452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

main subject

protein folding

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author

Franz-Ulrich Hartl

series ordinal

3

object named as

Hartl FU

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Europe PubMed Central

PMC publication ID

452432

retrieved

11 August 2017

stated in

Europe PubMed Central

PMC publication ID

452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

author name string

Hayer-Hartl MK

series ordinal

1

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Europe PubMed Central

PMC publication ID

452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

Weber F

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2

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Europe PubMed Central

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452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

language of work or name

English

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publication date

1 November 1996

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Europe PubMed Central

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452432

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retrieved

21 October 2019

published in

The EMBO Journal

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Europe PubMed Central

PMC publication ID

452432

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21 October 2019

volume

15

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Europe PubMed Central

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452432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

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21 October 2019

issue

22

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452432

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21 October 2019

page(s)

6111-6121

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452432

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21 October 2019

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The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis

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

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Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

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The role of molecular chaperones in protein folding

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To fold or not to fold....

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Residues in chaperonin GroEL required for polypeptide binding and release

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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27 July 2018

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

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27 July 2018

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin

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27 July 2018

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

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27 July 2018

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

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

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

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27 July 2018

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

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

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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

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

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Unfolding protein folding

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12 December 2020

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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Symmetric complexes of GroE chaperonins as part of the functional cycle

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Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

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12 December 2020

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On the role of groES in the chaperonin-assisted folding reaction. Three case studies

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https://pubmed.ncbi.nlm.nih.gov/8947033

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12 December 2020

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

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https://pubmed.ncbi.nlm.nih.gov/8947033

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12 December 2020

based on heuristic

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

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12 December 2020

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Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

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12 December 2020

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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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https://pubmed.ncbi.nlm.nih.gov/8947033

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12 December 2020

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Refolding of barnase in the presence of GroE

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12 December 2020

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Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside

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Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

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12 December 2020

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Identifiers

DOI

10.1002/J.1460-2075.1996.TB00999.X

1 reference

stated in

Europe PubMed Central

PMC publication ID

452432

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

retrieved

21 October 2019

PMC publication ID

452432

1 reference

stated in

Europe PubMed Central

PMC publication ID

452432

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

retrieved

21 October 2019

PubMed publication ID

8947033

1 reference

stated in

Europe PubMed Central

PMC publication ID

452432

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8947033%20AND%20SRC:MED&resulttype=core&format=json

retrieved

21 October 2019

 

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