Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein. - Wikidata - awgldk - TriplyDB

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

http://www.wikidata.org/entity/Q37713810

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Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression Structure of the thioredoxin-fold domain of human phosducin-like protein 2 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning The molecular architecture of the eukaryotic chaperonin TRiC/CCT Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly.Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex.PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.Dynamics, flexibility, and allostery in molecular chaperonins Modulation of phosducin-like protein 3 (PhLP3) levels promotes cytoskeletal remodelling in a MAPK and RhoA-dependent manner.Disruption of the chaperonin containing TCP-1 function affects protein networks essential for rod outer segment morphogenesis and survival.Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Introduction to 3D reconstruction of macromolecules using single particle electron microscopy.Assembly and trafficking of heterotrimeric G proteins Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins The Mechanism and Function of Group II Chaperonins.The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin.The phosducin-like protein PhLP1 is essential for G{beta}{gamma} dimer formation in Dictyostelium discoideum.PHLP2 is essential and plays a role in ciliogenesis and microtubule assembly in Tetrahymena thermophila.In response: conservation versus functional diversification of nuclear receptors: an academic perspective.Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90.

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Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

http://www.wikidata.org/entity/Q37713810

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 06 December 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@en

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@nl

type

label

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@en

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@nl

prefLabel

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@en

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

@nl

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PNAS.0405070101

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Proceedings of the National Academy of Sciences of the United States of America

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Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein

@en

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Barry M Willardson

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Joseph N McLaughlin

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José L Carrascosa

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Paul J Ludtke

http://www.w3.org/2001/XMLSchema#string

Sara Bertrand

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Ting Hu

http://www.w3.org/2001/XMLSchema#string

P2860

Determination of the G beta gamma-binding domain of phosducin. A regulatable modulator of G beta gamma signaling

Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.

Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex

Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.

Phosducin-like protein: an ethanol-responsive potential modulator of guanine nucleotide-binding protein function

Improved methods for building protein models in electron density maps and the location of errors in these models

A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin

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

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17410-17415

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scholarly article

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10.1073/PNAS.0405070101

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P433

50

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101

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José María Valpuesta

J Martín-Benito

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2004-12-06T00:00:00Z

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8145058

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15583139

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protein structure

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536017

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