Identification of functional differences between recombinant human α and β cardiac myosin motors.
about
The superfast human extraocular myosin is kinetically distinct from the fast skeletal IIa, IIb, and IId isoforms.Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.Magnesium modulates actin binding and ADP release in myosin motors.Modulating Beta-Cardiac Myosin Function at the Molecular and Tissue Levels.The C-terminus of troponin T is essential for maintaining the inactive state of regulated actinTransgenic mouse α- and β-cardiac myosins containing the R403Q mutation show isoform-dependent transient kinetic differencesA Perspective on the Role of Myosins as MechanosensorsMolecular consequences of the R453C hypertrophic cardiomyopathy mutation on human β-cardiac myosin motor function.To understand muscle you must take it apart.Hypertrophic and dilated cardiomyopathy: four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases.Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil.Heart failure drug changes the mechanoenzymology of the cardiac myosin powerstroke.Small molecule-mediated refolding and activation of myosin motor function.Hypothesis and theory: mechanical instabilities and non-uniformities in hereditary sarcomere myopathies.Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle.A small-molecule modulator of cardiac myosin acts on multiple stages of the myosin chemomechanical cycle.Measuring the Kinetic and Mechanical Properties of Non-processive Myosins Using Optical Tweezers.A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Mechanistic insights into the active site and allosteric communication pathways in human nonmuscle myosin-2C.A Cardiomyopathy Mutation in the Myosin Essential Light Chain Alters Actomyosin Structure.Dilated cardiomyopathy myosin mutants have reduced force-generating capacity.Hypertrophic cardiomyopathy mutations increase myofilament Ca2+ buffering, alter intracellular Ca2+ handling and stimulate Ca2+ dependent signalling.Genetic and Tissue Engineering Approaches to Modeling the Mechanics of Human Heart Failure for Drug Discovery
P2860
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P2860
Identification of functional differences between recombinant human α and β cardiac myosin motors.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
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2012年论文
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name
Identification of functional d ...... α and β cardiac myosin motors.
@ast
Identification of functional d ...... α and β cardiac myosin motors.
@en
type
label
Identification of functional d ...... α and β cardiac myosin motors.
@ast
Identification of functional d ...... α and β cardiac myosin motors.
@en
prefLabel
Identification of functional d ...... α and β cardiac myosin motors.
@ast
Identification of functional d ...... α and β cardiac myosin motors.
@en
P2093
P2860
P1476
Identification of functional d ...... α and β cardiac myosin motors.
@en
P2093
Heresh Rezavandi
John C Deacon
Leslie A Leinwand
Marieke J Bloemink
Michael A Geeves
P2860
P2888
P304
P356
10.1007/S00018-012-0927-3
P577
2012-02-16T00:00:00Z