Cooperativity in F-actin: chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament.
about
Poorly understood aspects of striated muscle contractionRemodeling of actin filaments by ADF/cofilin proteinsActin filaments as tension sensors.Structural polymorphism in F-actin.Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.Coarse-graining provides insights on the essential nature of heterogeneity in actin filamentsCardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Molecular origins of cofilin-linked changes in actin filament mechanics.Conformational dynamics of actin: effectors and implications for biological function.Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Long-term storage of surface-adsorbed protein machines.The structural dynamics of actin during active interaction with myosin depends on the isoform of the essential light chain.Bending flexibility of actin filaments during motor-induced slidingAcceleration of the sliding movement of actin filaments with the use of a non-motile mutant myosin in in vitro motility assays driven by skeletal muscle heavy meromyosin.Critical review of the swinging crossbridge theory and of the cardinal active role of water in muscle contraction.Analysis of flexural rigidity of actin filaments propelled by surface adsorbed myosin motors.Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation.Motor-driven dynamics in actin-myosin networks.A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant.Effects of denervation and muscle inactivity on the organization of F-actin.
P2860
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P2860
Cooperativity in F-actin: chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament.
description
1993 nî lūn-bûn
@nan
1993 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@ast
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@en
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@nl
type
label
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@ast
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@en
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@nl
prefLabel
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@ast
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@en
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@nl
P2093
P2860
P1433
P1476
Cooperativity in F-actin: chem ...... rs in the same actin filament.
@en
P2093
D D Thomas
E Katayama
E Prochniewicz
T Yanagida
P2860
P304
P356
10.1016/S0006-3495(93)81057-9
P407
P577
1993-07-01T00:00:00Z