A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin. (Q46138539)

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20 January 2020

title

A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin (English)

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20 January 2020

6

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20 January 2020

author name string

G M Altschuler

1

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20 January 2020

C Dekker

2

1 reference

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20 January 2020

E A McCormack

3

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20 January 2020

E P Morris

4

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20 January 2020

D R Klug

5

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20 January 2020

language of work or name

English

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publication date

5 February 2009

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20 January 2020

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20 January 2020

volume

583

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20 January 2020

issue

4

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20 January 2020

page(s)

782-786

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Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin

20 January 2020

cites work

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Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT.

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Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin

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Actin interacts with CCT via discrete binding sites: a binding transition-release model for CCT-mediated actin folding

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Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies

21 January 2018

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Atomic structure of the actin:DNase I complex

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