Single myosin molecule mechanics: piconewton forces and nanometre steps (Q34338098)

1 August 2017

Single myosin molecule mechanics: piconewton forces and nanometre steps (English)

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1 August 2017

Finer JT

1

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1 August 2017

Simmons RM

series ordinal

2

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1 August 2017

Spudich JA

series ordinal

3

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1 August 2017

language of work or name

English

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publication date

1 March 1994

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1 August 2017

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1 August 2017

368

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1 August 2017

6467

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1 August 2017

113-119

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https://scigraph.springernature.com/pub.10.1038/368113a0

1 August 2017

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cites work

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The mechanism of muscular contraction

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Proposed mechanism of force generation in striated muscle

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Tension responses to sudden length change in stimulated frog muscle fibres near slack length

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The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay

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Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin.

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Quantized velocities at low myosin densities in an in vitro motility assay

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Direct observation of molecular motility by light microscopy

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Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay

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7 January 2021

Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle.

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7 January 2021

Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres

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7 January 2021

Sub-piconewton force fluctuations of actomyosin in vitro

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7 January 2021

Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle

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7 January 2021

Rapid regeneration of the actin-myosin power stroke in contracting muscle

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Crossbridge behaviour during muscle contraction

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7 January 2021

Rotational dynamics of actin-bound myosin heads in active myofibrils

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Myosin heads have a broad orientational distribution during isometric muscle contraction: time-resolved EPR studies using caged ATP.

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7 January 2021

Movement of microtubules by single kinesin molecules

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

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Bead movement by single kinesin molecules studied with optical tweezers

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Force of single kinesin molecules measured with optical tweezers

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Direct observation of kinesin stepping by optical trapping interferometry

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Fluorescent actin filaments move on myosin fixed to a glass surface

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Mechanism of Actomyosin Atpase and the Problem of Muscle Contractio

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7 January 2021

Polarity and velocity of sliding filaments: control of direction by actin and of speed by myosin

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7 January 2021

Direction and speed of actin filaments moving along thick filaments isolated from molluscan smooth muscle

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7 January 2021

Energetics and mechanism of actomyosin adenosine triphosphatase

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7 January 2021

Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5'-triphosphate

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7 January 2021

Characterization of radial force and radial stiffness in Ca(2+)-activated skinned fibres of the rabbit psoas muscle

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X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle

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7 January 2021

7 Preparation of myosin and its subfragments from rabbit skeletal muscle

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7 January 2021

Myosin subfragment-1 is sufficient to move actin filaments in vitro

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Optical diffraction study of muscle fibers. II. Electro-optical properties of muscle fibers

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The relation between stiffness and filament overlap in stimulated frog muscle fibres

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7 January 2021

Identifiers

DOI

10.1038/368113A0

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Dimensions Publication ID

1 August 2017

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