Literature DB >> 2942420

Phosphorylation of myosin in non-muscle and smooth muscle cells. Possible rules and evolutionary trends.

J Kuźnicki.   

Abstract

Reversible phosphorylation of myosin subunits is observed in almost all eukaryotic cells. The data concerning sites and effects of phosphorylation on actin-activated ATPase activity of myosin and on its filament formation are described. These observations are discussed in terms of possible evolutionary trends and rules which may govern the process of myosin phosphorylation.

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Year:  1986        PMID： 2942420     DOI： 10.1016/0014-5793(86)80806-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  3 in total

1.  Evidence for a role of endothelin 1 and protein kinase C in nitroglycerin tolerance.

Authors:  T Münzel; A Giaid; S Kurz; D J Stewart; D G Harrison
Journal:  Proc Natl Acad Sci U S A       Date:  1995-05-23       Impact factor: 11.205

2.  Phosphorylatable serine residues are located in a non-helical tailpiece of a catch muscle myosin.

Authors:  L Castellani; B W Elliott; C Cohen
Journal:  J Muscle Res Cell Motil       Date:  1988-12       Impact factor: 2.698

3.  Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein.

Authors:  R Yabkowitz; D R Burgess
Journal:  J Cell Biol       Date:  1987-08       Impact factor: 10.539
  3 in total

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