Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution.
about
Poorly understood aspects of striated muscle contractionDistinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cyclingVariations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscleNew insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin IBasal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force developmentAltered kinetics of contraction in skeletal muscle fibers containing a mutant myosin regulatory light chain with reduced divalent cation bindingEffects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibresAblation of myosin-binding protein-C accelerates force development in mouse myocardiumEffects of sarcomere length and temperature on the rate of ATP utilisation by rabbit psoas muscle fibresAblation of the cardiac-specific gene leucine-rich repeat containing 10 (Lrrc10) results in dilated cardiomyopathyFunctional consequence of mutation in rat cardiac troponin T is affected differently by myosin heavy chain isoformsTroponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosinKinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth musclesEffect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle.Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers.Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA.ATP consumption and efficiency of human single muscle fibers with different myosin isoform compositionViscosity and solute dependence of F-actin translocation by rabbit skeletal heavy meromyosin.Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers.Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Myosin heavy chain and cardiac troponin T damage is associated with impaired myofibrillar ATPase activity contributing to sarcomeric dysfunction in Ca2+-paradox rat hearts.Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2).In vitro actin filament sliding velocities produced by mixtures of different types of myosin.Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.Nucleotide-dependent contractile properties of Ca(2+)-activated fast and slow skeletal muscle fibers.Diaphragm muscle weakness in an experimental porcine intensive care unit model.Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle cMyosin regulatory light chain modulates the Ca2+ dependence of the kinetics of tension development in skeletal muscle fibers.Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardiumIsometric force redevelopment of skinned muscle fibers from rabbit activated with and without Ca2+Mutation of the myosin converter domain alters cross-bridge elasticity.Calmidazolium alters Ca2+ regulation of tension redevelopment rate in skinned skeletal muscleMyosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscleDeletion of the titin N2B region accelerates myofibrillar force development but does not alter relaxation kineticsKinetic mechanism of myofibril ATPase.Biochemical kinetics of skeletal actosubfragment-1 at high subfragment-1 concentrations.Force generation and temperature-jump and length-jump tension transients in muscle fibers.Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force gen
P2860
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P2860
Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Rate of force generation in mu ...... n ATPase activity in solution.
@ast
Rate of force generation in mu ...... n ATPase activity in solution.
@en
type
label
Rate of force generation in mu ...... n ATPase activity in solution.
@ast
Rate of force generation in mu ...... n ATPase activity in solution.
@en
prefLabel
Rate of force generation in mu ...... n ATPase activity in solution.
@ast
Rate of force generation in mu ...... n ATPase activity in solution.
@en
P2860
P356
P1476
Rate of force generation in mu ...... n ATPase activity in solution.
@en
P2093
Eisenberg E
P2860
P304
P356
10.1073/PNAS.83.10.3542
P407
P577
1986-05-01T00:00:00Z