The crystal structure of the GroES co-chaperonin at 2.8 Å resolution (Q59072776)

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14 October 2019

title

The crystal structure of the GroES co-chaperonin at 2.8 A resolution (English)

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14 October 2019

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3

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14 October 2019

author name string

Hunt JF

1

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14 October 2019

Weaver AJ

2

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14 October 2019

Gierasch L

4

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14 October 2019

Deisenhofer J

5

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14 October 2019

language of work or name

English

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publication date

1 January 1996

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14 October 2019

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14 October 2019

volume

379

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14 October 2019

issue

6560

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14 October 2019

page(s)

37-45

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Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.

14 October 2019

cites work

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

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Characterization of a functionally important mobile domain of GroES.

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Refolding of barnase in the presence of GroE

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

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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The detection of sub-units within the crystallographic asymmetric unit

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7 January 2021

Monomer-Heptamer Equilibrium of the Escherichia coli Chaperonin GroES

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Identifiers

DOI

10.1038/379037A0

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8538739%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

14 October 2019

1044840084

0 references

1 reference