Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle. - Wikidata - wikimedia - TriplyDB

Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle.

Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle.

http://www.wikidata.org/entity/Q43070024

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Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin molecules N-Terminus of Cardiac Myosin Essential Light Chain Modulates Myosin Step-Size.MEMLET: An Easy-to-Use Tool for Data Fitting and Model Comparison Using Maximum-Likelihood Estimation.Mechanical heterogeneity favors fragmentation of strained actin filaments High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Structural basis for drug-induced allosteric changes to human β-cardiac myosin motor activity A Perspective on the Role of Myosins as Mechanosensors A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion Kinetic Adaptations of Myosins for Their Diverse Cellular Functions Review: The ATPase mechanism of myosin and actomyosin.Modeling the Actin.myosin ATPase Cross-Bridge Cycle for Skeletal and Cardiac Muscle Myosin Isoforms.In vitro actin motility velocity varies linearly with the number of myosin impellers.How to Measure Load-Dependent Kinetics of Individual Motor Molecules Without a Force-Clamp.Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.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.Overview of the mechanism of cytoskeletal motors based on structure.Dilated cardiomyopathy myosin mutants have reduced force-generating capacity.Single cardiac ventricular myosins are autonomous motors.Myosin MgADP release rate decreases at longer sarcomere length to prolong myosin attachment time in skinned rat myocardium.Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?Genetic and Tissue Engineering Approaches to Modeling the Mechanics of Human Heart Failure for Drug Discovery Positive cardiac inotrope omecamtiv mecarbil activates muscle despite suppressing the myosin working stroke Controlling load-dependent kinetics of β-cardiac myosin at the single-molecule level

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Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle.

http://www.wikidata.org/entity/Q43070024

description

2014 nî lūn-bûn

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2014年の論文

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2014年学术文章

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2014年学术文章

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2014年学术文章

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2014年学术文章

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2014年学术文章

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2014年学术文章

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2014年學術文章

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2014年學術文章

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name

Inherent force-dependent prope ...... elationship of cardiac muscle.

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Inherent force-dependent prope ...... elationship of cardiac muscle.

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Inherent force-dependent prope ...... elationship of cardiac muscle.

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Inherent force-dependent prope ...... elationship of cardiac muscle.

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Inherent force-dependent prope ...... elationship of cardiac muscle.

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Inherent force-dependent prope ...... elationship of cardiac muscle.

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J.BPJ.2014.11.005

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Biophysical Journal

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Inherent force-dependent prope ...... relationship of cardiac muscle

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E Michael Ostap

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Henry Shuman

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Single-molecule mechanics of R403Q cardiac myosin isolated from the mouse model of familial hypertrophic cardiomyopathy

Models for the specific adhesion of cells to cells

Hypertrophic and dilated cardiomyopathy mutations differentially affect the molecular force generation of mouse alpha-cardiac myosin in the laser trap assay.

Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.

Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin

Single myosin molecule mechanics: piconewton forces and nanometre steps.

Force generation in single conventional actomyosin complexes under high dynamic load

Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.

Kinetic schemes for post-synchronized single molecule dynamics.

Identification of functional differences between recombinant human α and β cardiac myosin motors.

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L41-L44

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scholarly article

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10.1016/J.BPJ.2014.11.005

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Michael J Greenberg

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2014-12-01T00:00:00Z

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