Single myosin molecule mechanics: piconewton forces and nanometre steps

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Nature

• Publication date

  1994-03-10

• Fields of study

  Biology, Medicine, Physics, Chemistry

• Identifiers
  DOI 10.1038/368113A0PMID 8139653
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The mechanism of muscular contraction.

  2002cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1992cited by this paper
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  1991cited by this paper
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  1991cited by this paper
• Quantized velocities at low myosin densities in an in vitro motility

  1991cited by this paper
• Kinetic studies on the association and dissociation of myosin subfragment 1 and actin.

  1991cited by this paper
• Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle.

  1991cited by this paper
• Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres

  1991cited by this paper
• Myosin heads have a broad orientational distribution during isometric muscle contraction: time-resolved EPR studies using caged ATP.

  1990cited by this paper
• Bead movement by single kinesin molecules studied with optical tweezers

  1990cited by this paper
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  1990cited by this paper
• Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay.

  1990cited by this paper
• Polarity and velocity of sliding filaments: control of direction by actin and of speed by myosin.

  1990cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1989cited by this paper
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  1988cited by this paper
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  1988cited by this paper
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  1987cited by this paper
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  1986cited by this paper
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  1986cited by this paper
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  1985cited by this paper
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  1985cited by this paper
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  1985cited by this paper
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  1982cited by this paper
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