Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation - Wikidata - wikimedia - TriplyDB

Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation

Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation

http://www.wikidata.org/entity/Q36015047

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The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads Micromechanical architecture of the endothelial cell cortex Single-molecule measurement of the stiffness of the rigor myosin head Mechanotransduction in skeletal muscle Sorting of a nonmuscle tropomyosin to a novel cytoskeletal compartment in skeletal muscle results in muscular dystrophy Correlative nanoscale imaging of actin filaments and their complexes Complexity of the tensegrity structure for dynamic energy and force distribution of cytoskeleton during cell spreading MEDYAN: Mechanochemical Simulations of Contraction and Polarity Alignment in Actomyosin Networks A biomechanical perspective on stress fiber structure and function Tensile mechanics of alanine-based helical polypeptide: force spectroscopy versus computer simulations.Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit Cooperative effects of Rho and mechanical stretch on stress fiber organization.Viscoelastic retraction of single living stress fibers and its impact on cell shape, cytoskeletal organization, and extracellular matrix mechanics.Cytoskeletal bundle mechanics.α-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly.Force generation in the outer hair cell of the cochlea.Dynamic and elastic properties of F-actin: a normal-modes analysis Effects of polymerization and nucleotide identity on the conformational dynamics of the bacterial actin homolog MreB.Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover.Mechanical interplay between invadopodia and the nucleus in cultured cancer cells Hidden-Markov methods for the analysis of single-molecule actomyosin displacement data: the variance-Hidden-Markov method Refinement of F-actin model against fiber diffraction data by long-range normal modes.Mechanical properties of single myosin molecules probed with the photonic force microscope.Thin-foil magnetic force system for high-numerical-aperture microscopy.Sarcomere lattice geometry influences cooperative myosin binding in muscle.Mechanical properties of actin stress fibers in living cells.Length dependence of active force production in skeletal muscle.Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes Effect of diamide on force generation and axial stiffness of the cochlear outer hair cell.Theoretical considerations on myofibril stiffness.Sorting of tropomyosin isoforms in synchronised NIH 3T3 fibroblasts: evidence for distinct microfilament populations.Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.On the theory of muscle contraction: filament extensibility and the development of isometric force and stiffness Micropipette suction for measuring piconewton forces of adhesion and tether formation from neutrophil membranes.Nonlinear displacement of ventral stress fibers under externally applied lateral force by an atomic force microscope.Compliance of thin filaments in skinned fibers of rabbit skeletal muscle.Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibers Compliant realignment of binding sites in muscle: transient behavior and mechanical tuning.Direct tests of muscle cross-bridge theories: predictions of a Brownian dumbbell model for position-dependent cross-bridge lifetimes and step sizes with an optically trapped actin filament.A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers.

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P2860

Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation

http://www.wikidata.org/entity/Q36015047

description

1994 nî lūn-bûn

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1994年学术文章

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1994年學術文章

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1994年學術文章

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1994年學術文章

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Direct measurement of stiffnes ...... n by in vitro nanomanipulation

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Direct measurement of stiffnes ...... n by in vitro nanomanipulation

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Direct measurement of stiffnes ...... n by in vitro nanomanipulation

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Ishijima A

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Kojima H

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Yanagida T

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P2860

The double array of filaments in cross-striated muscle

Atomic structure of the actin:DNase I complex

Atomic model of the actin filament

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

Measurement of sarcomere shortening in skinned fibers from frog muscle by white light diffraction.

ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.

FILAMENT LENGTHS IN STRIATED MUSCLE.

Fluorescent phallotoxin, a tool for the visualization of cellular actin.

Force measurements by micromanipulation of a single actin filament by glass needles.

Proposed mechanism of force generation in striated muscle.

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