The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.
about
Sex-based differences in skeletal muscle kinetics and fiber-type compositionWarm-Up Strategies for Sport and Exercise: Mechanisms and Applications.Recent insights into muscle fatigue at the cross-bridge level.Myosin cleft closure determines the energetics of the actomyosin interaction.Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Micromechanical thermal assays of Ca2+-regulated thin-filament function and modulation by hypertrophic cardiomyopathy mutants of human cardiac troponinNucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiencyTranslational actomyosin research: fundamental insights and applications hand in hand.Sprint performance under heat stress: A review.Muscle fatigue and muscle weakness: what we know and what we wish we did.Heart failure drug changes the mechanoenzymology of the cardiac myosin powerstroke.Contractility parameters of human β-cardiac myosin with the hypertrophic cardiomyopathy mutation R403Q show loss of motor function.Phosphate and acidosis act synergistically to depress peak power in rat muscle fibers.A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.ATP and phosphocreatine utilization in single human muscle fibres during the development of maximal power output at elevated muscle temperatures.The mechanism of the reverse recovery step, phosphate release, and actin activation of Dictyostelium myosin II.Acute effects of heated resistance exercise in female and male power athletes.Modulators of actin-myosin dissociation: basis for muscle type functional differences during fatigue.The interrelation between mechanical characteristics of contracting muscle, cross-bridge internal structure, and the mechanism of chemomechanical energy transduction.Elite sprint swimming performance is enhanced by completion of additional warm-up activities.Functional responses of uremic single skeletal muscle fibers to redox imbalances.
P2860
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P2860
The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.
description
2004 nî lūn-bûn
@nan
2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The force exerted by a muscle ...... rength of the actomyosin bond.
@ast
The force exerted by a muscle ...... rength of the actomyosin bond.
@en
The force exerted by a muscle ...... rength of the actomyosin bond.
@nl
type
label
The force exerted by a muscle ...... rength of the actomyosin bond.
@ast
The force exerted by a muscle ...... rength of the actomyosin bond.
@en
The force exerted by a muscle ...... rength of the actomyosin bond.
@nl
prefLabel
The force exerted by a muscle ...... rength of the actomyosin bond.
@ast
The force exerted by a muscle ...... rength of the actomyosin bond.
@en
The force exerted by a muscle ...... rength of the actomyosin bond.
@nl
P2093
P2860
P1433
P1476
The force exerted by a muscle ...... rength of the actomyosin bond.
@en
P2093
Christina Karatzaferi
Marc K Chinn
Roger Cooke
P2860
P304
P356
10.1529/BIOPHYSJ.104.039909
P407
P577
2004-10-01T00:00:00Z