(Q41634708)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7915827%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

title

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

1 reference

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cryogenic electron microscopy

28 October 2019

main subject

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6

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28 October 2019

author name string

Chen S

1

1 reference

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28 October 2019

Roseman AM

2

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28 October 2019

Hunter AS

3

1 reference

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28 October 2019

Wood SP

4

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28 October 2019

Burston SG

5

1 reference

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28 October 2019

Clarke AR

7

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28 October 2019

Saibil HR

8

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28 October 2019

language of work or name

English

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publication date

1 September 1994

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28 October 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7915827%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

volume

371

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28 October 2019

issue

6494

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28 October 2019

page(s)

261-264

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https://scigraph.springernature.com/pub.10.1038/371261a0

28 October 2019

exact match

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cites work

Molecular chaperone functions of heat-shock proteins

1 reference

7 January 2021

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

1 reference

7 January 2021

Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 reference

7 January 2021

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

1 reference

7 January 2021

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

1 reference

7 January 2021

Proper and improper folding of proteins in the cellular environment

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

7 January 2021

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

1 reference

7 January 2021

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

1 reference

7 January 2021

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

1 reference

7 January 2021

Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

1 reference

7 January 2021

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

1 reference

7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

7 January 2021

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

1 reference

7 January 2021

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

1 reference

7 January 2021

Identifiers

DOI

10.1038/371261A0

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7915827%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

28 October 2019

0 references

1 reference