Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers
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Ablation of myosin-binding protein-C accelerates force development in mouse myocardiumAcceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chainInter-sarcomere coordination in muscle revealed through individual sarcomere response to quick stretch.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Prolonged space flight-induced alterations in the structure and function of human skeletal muscle fibres.Regulatory mechanism of length-dependent activation in skinned porcine ventricular muscle: role of thin filament cooperative activation in the Frank-Starling relation.History-dependent mechanical properties of permeabilized rat soleus muscle fibers.Interplay of troponin- and Myosin-based pathways of calcium activation in skeletal and cardiac muscle: the use of W7 as an inhibitor of thin filament activation.Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle.The role of thin filament cooperativity in cardiac length-dependent calcium activation.Effect of Ca2+ binding properties of troponin C on rate of skeletal muscle force redevelopment.Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscleThe effects of Ca2+ and MgADP on force development during and after muscle length changesWeekly versus monthly testosterone administration on fast and slow skeletal muscle fibers in older adult males.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Length and PKA Dependence of Force Generation and Loaded Shortening in Porcine Cardiac MyocytesCongenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular functionMolecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-CContribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculaeDivergent effects of α- and β-myosin heavy chain isoforms on the N terminus of rat cardiac troponin T.Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashionContributions of stretch activation to length-dependent contraction in murine myocardium.Acting on an impulse (or two): Advantages of high-frequency tetanic onset in skeletal muscle.Phosphate and acidosis act synergistically to depress peak power in rat muscle fibers.Calcium-independent activation of skinned cardiac muscle by secophalloidin.Engineering competitive magnesium binding into the first EF-hand of skeletal troponin C.Transmural variation in myosin heavy chain isoform expression modulates the timing of myocardial force generation in porcine left ventricle.Cardiac troponin C (TnC) and a site I skeletal TnC mutant alter Ca2+ versus crossbridge contribution to force in rabbit skeletal fibres.The effects of the myosin-II inhibitor N-benzyl-p-toluene sulphonamide on fatigue in mouse single intact toe muscle fibres.Expression of cardiac troponin T with COOH-terminal truncation accelerates cross-bridge interaction kinetics in mouse myocardium.Altered vascular smooth muscle cell differentiation in the endometrial vasculature in menorrhagia.Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres.Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle.Length dependence of force generation exhibit similarities between rat cardiac myocytes and skeletal muscle fibres.Differential roles of regulatory light chain and myosin binding protein-C phosphorylations in the modulation of cardiac force development.
P2860
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P2860
Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@ast
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@en
type
label
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@ast
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@en
prefLabel
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@ast
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@en
P2093
P2860
P356
P1476
Cooperative mechanisms in the ...... skinned skeletal muscle fibers
@en
P2093
D P Fitzsimons
K S Campbell
P2860
P304
P356
10.1085/JGP.117.2.133
P577
2001-02-01T00:00:00Z