Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.
about
The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.Controlling the cortical actin motor.Actinous enigma or enigmatic actin: Folding, structure, and functions of the most abundant eukaryotic protein.Native globular actin has a thermodynamically unstable quasi-stationary structure with elements of intrinsic disorder.A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions.A putative role of the Sup35p C-terminal domain in the cytoskeleton organization during yeast mitosis.A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin.A more precise characterization of chaperonin substrates.
P2860
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P2860
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Development of free-energy-bas ...... P-1 mediated folding of actin.
@en
Development of free-energy-bas ...... P-1 mediated folding of actin.
@nl
type
label
Development of free-energy-bas ...... P-1 mediated folding of actin.
@en
Development of free-energy-bas ...... P-1 mediated folding of actin.
@nl
prefLabel
Development of free-energy-bas ...... P-1 mediated folding of actin.
@en
Development of free-energy-bas ...... P-1 mediated folding of actin.
@nl
P2860
P356
P1476
Development of free-energy-bas ...... P-1 mediated folding of actin.
@en
P2093
Gabriel M Altschuler
Keith R Willison
P2860
P304
P356
10.1098/RSIF.2008.0185
P577
2008-12-01T00:00:00Z