Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.
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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 assemblyActivities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisationFunctional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progressionStructure of the thioredoxin-fold domain of human phosducin-like protein 2The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperoninsThe Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional PartitioningThe molecular architecture of the eukaryotic chaperonin TRiC/CCTRole 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 chaperoninsModulation 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 foldingStructures 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 proteinsHuman 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 proteinsThe 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.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 06 December 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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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
P2093
P2860
P356
P1476
Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein
@en
P2093
Barry M Willardson
Joseph N McLaughlin
José L Carrascosa
Paul J Ludtke
Sara Bertrand
P2860
P304
17410-17415
P356
10.1073/PNAS.0405070101
P407
P577
2004-12-06T00:00:00Z