Theoretical model of the interactions between Ca2+, calmodulin and myosin light chain kinase

No abstract is available for this paper.

• Publication year

  2005

• Venue

  FEBS Letters

• Publication date

  2005-08-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.febslet.2005.06.076PMID 16051224
• 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.

• Platelet activation.

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• Ca2+ Activation of Smooth Muscle Contraction

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• EVIDENCE FOR THE INVOLVEMENT OF CALMODULIN THAT IS BOUND TO THE TRITON-INSOLUBLE FRACTION EVEN IN THE ABSENCE OF Ca 2 *

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• Differences in calmodulin and calmodulin-binding proteins in phasic and tonic smooth muscles.

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• Ca Activation of Smooth Muscle Contraction EVIDENCE FOR THE INVOLVEMENT OF CALMODULIN THAT IS BOUND TO THE TRITON-INSOLUBLE FRACTION EVEN IN THE ABSENCE OF Ca *

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• Activation of Myosin Light Chain Kinase Requires Translocation of Bound Calmodulin*

  2001cited by this paper
• Dedicated Myosin Light Chain Kinases with Diverse Cellular Functions*

  2001cited by this paper
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• Ca(2+)-dependent phosphorylation of myosin light chain kinase decreases the Ca2+ sensitivity of light chain phosphorylation within smooth muscle cells.

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• Ca2+, caldesmon, and myosin light chain kinase exchange with calmodulin.

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• A molecular mechanism for autoinhibition of myosin light chain kinases.

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• The kinetics of linear systems with special reference to periodic reactions

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