Molecular charge dominates the inhibition of actomyosin in skinned muscle fibers by SH1 peptides.

No abstract is available for this paper.

• Publication year

  1991

• Venue

  Biophysical Journal

• Publication date

  1991-08-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0006-3495(91)82060-4PMID 1912278PMCID PMC1260071
• 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.

• Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain.

  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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  1989cited by this paper
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  1989cited by this paper
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  1989cited by this paper
• Location of a contact site between actin and myosin in the three-dimensional structure of the acto-S1 complex.

  1989cited by this paper
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  1988cited by this paper
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  1988cited by this paper
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  1988cited by this paper
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  1988cited by this paper
• Pathway for the communication between the ATPase and actin sites in myosin

  1988cited by this paper
• F-actin-binding synthetic heptapeptide having the amino acid sequence around the SH1 cysteinyl residue of myosin.

  1987influential reference
• Myosin structure and function in cell motility.

  1987cited by this paper
• Measurement of interprotein distances in the acto-subfragment 1 rigor complex.

  1987cited by this paper
• Spectroscopic probes of muscle cross-bridge rotation.

  1987cited by this paper
• Measurements on permeabilized skeletal muscle fibers during continuous activation.

  1987cited by this paper
• Actin-binding site of pig cardiac myosin.

  1987cited by this paper
• Location of the ATPase site of myosin determined by three-dimensional electron microscopy

  1987cited by this paper
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  1986cited by this paper
• Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1.

  1985cited by this paper
• Effect of various anions on the stability of the coiled coil of skeletal muscle myosin.

  1985cited by this paper
• Binding of F-actin to a region between SH1 and SH2 groups of myosin subfragment-1 which may determine the high affinity of acto-subfragment-1 complex at rigor.

  1984cited by this paper
• Interaction between myosin and F-actin. Correlation with actin-binding sites on subfragment-1.

  1984cited by this paper
• Control of sarcomere length in skinned muscle fibres of Rana temporaria during mechanical transients.

  1984cited by this paper
• Fluorescence energy transfer between probes on actin and probes on myosin.

  1984cited by this paper
• Rapid analysis of amino acids using pre-column derivatization.

  1984cited by this paper
• Quantitative determination of myosin and actin in rabbit skeletal muscle.

  1983cited by this paper
• Mapping of actin-binding sites on the heavy chain of myosin subfragment 1.

  1983cited by this paper
• Fluorescence energy transfer between the myosin subfragment-1 isoenzymes and F-actin in the absence and presence of nucleotides.

  1983cited by this paper
• Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers.

  1983cited by this paper
• An actin-binding site on the 20K fragment of myosin subfragment 1.

  1982cited by this paper
• Preparation of myofibrils.

  1982cited by this paper
• Special instrumentation and techniques for kinetic studies of contractile systems.

  1982cited by this paper
• Proteolytic approach to structure and function of actin recognition site in myosin heads.

  1981cited by this paper
• Structure of the actin–myosin interface

  1981cited by this paper
• Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.

  1979cited by this paper
• Amino acid sequence of a myosin fragment that contains SH-1, SH-2, and Ntau-methylhistidine.

  1977cited by this paper
• Tension in Skinned Frog Muscle Fibers in Solutions of Varying Ionic Strength and Neutral Salt Composition

  1973cited by this paper
• Proposed Mechanism of Force Generation in Striated Muscle

  1971cited by this paper

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  2002cites this paper
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  2000cites this paper
• The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo

  1995cites this paper
• Effects on Ca(2+)-activated tension due to a synthetic NH2-terminal actin peptide in single skeletal muscle fibers.

  1995cites this paper
• Faster force transient kinetics at submaximal Ca2+ activation of skinned psoas fibers from rabbit.

  1995cites this paper
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  1994cites this paper
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  1994cites this paper
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  1993cites this paper
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  1993cites this paper
• Antibody and peptide probes of interactions between the SH1-SH2 region of myosin subfragment 1 and actin's N-terminus.

  1992cites this paper