Phosphorylation of myosin light chain kinase by the multifunctional calmodulin-dependent protein kinase II in smooth muscle cells
- Author
- TANSEY, M. G1 ; WORD, R. A; HIDAKA, H; SINGER, H. A; SCHWORER, C. M; KAMM, K. E; STULL, J. T
[1] Univ. Texas Southwestern medical cent., dep. physiology, Dallas TX 75235, United States - Source
The Journal of biological chemistry (Print). 1992, Vol 267, Num 18, pp 12511-12516 ; ref : 28 ref
- CODEN
- JBCHA3
- ISSN
- 0021-9258
- Scientific domain
- Biochemistry, molecular biology, biophysics; Biotechnology
- Publisher
- American Society for Biochemistry and Molecular Biology, Bethesda, MD
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Bovin Calcium Chaîne peptidique légère Enzyme Kinase Muscle lisse Myosine Phosphorylation Ca,calmodulin-dependent protein kinase Artiodactyla Mammalia Ungulata Vertebrata
- Keyword (en)
- Bovine Calcium light-Peptide chain Enzyme Kinase Smooth muscle Myosin Phosphorylation Artiodactyla Mammalia Ungulata Vertebrata
- Keyword (es)
- Bovino Calcio Cadena peptídica ligera Enzima Kinase Músculo liso Miosina Fosforilación Artiodactyla Mammalia Ungulata Vertebrata
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02E Enzymes and enzyme inhibitors / 002A02E03 Transferases
- Discipline
- Analytical, structural and metabolic biochemistry
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 5451094
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1016/S0021-9258(18)42307-1 
https://dx.doi.org/10.1016/S0021-9258(18)42307-1
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