Literature DB >> 3002861

Autophosphorylation of calmodulin kinase II: functional aspects.

J M Bronstein, D B Farber, C G Wasterlain.   

Abstract

Autophosphorylation of purified calmodulin kinase II dramatically inhibited protein kinase activity and enhanced substrate selectivity. Inhibition was observed over a wide range of calmodulin concentrations but calmodulin binding was unaffected. Autophosphorylation of calmodulin kinase II may be a mechanism for limiting phosphorylation to physiological substrates and terminating some of calcium's actions in synaptic events.

Entities:  

Mesh:

Substances:

Year:  1986        PMID: 3002861     DOI: 10.1016/0014-5793(86)80228-9

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


  1 in total

1.  Decreased calmodulin kinase activity after status epilepticus.

Authors:  J Bronstein; D Farber; C Wasterlain
Journal:  Neurochem Res       Date:  1988-01       Impact factor: 3.996

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.