Conformational rearrangements of an archaeal chaperonin upon ATPase cycling. (Q53898895)

22 May 2018

title

Conformational rearrangements of an archaeal chaperonin upon ATPase cycling. (English)

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22 May 2018

author name string

Gutsche I

1

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22 May 2018

Holzinger J

2

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22 May 2018

Rössle M

3

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22 May 2018

Heumann H

4

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22 May 2018

Baumeister W

5

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22 May 2018

May RP

6

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22 May 2018

language of work or name

English

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publication date

1 April 2000

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22 May 2018

number of pages

4

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inferred from page(s)

published in

Current Biology

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22 May 2018

volume

10

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22 May 2018

issue

7

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22 May 2018

page(s)

405-408

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22 May 2018

Structure and function in GroEL-mediated protein folding

cites work

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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

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The thermosome: chaperonin with a built-in lid

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Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

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Structural Changes of theEscherichia coliGroEL–GroES Chaperonins upon Complex Formation in Solution: A Neutron Small Angle Scattering Study

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Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

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The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering 1 1Edited by M. F. Moody

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Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

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Identifiers

DOI

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22 May 2018

PubMed ID

10753750

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22 May 2018