Calcium calmodulin regulation of atpase activity and endogenous phosphorylation of mammalian brain actomyosin (1987)
- Authors:
- Autor USP: LARSON, ROY EDWARD - FMRP
- Unidade: FMRP
- DOI: 10.1016/0006-291x(87)91567-1
- Subjects: CÁLCIO; CALMODULINA
- Language: Português
- Source:
- Título: Biochemical and Biophysical Research Communication
- Volume/Número/Paginação/Ano: v.145, p.1217-24, 1987
- Este artigo NÃO possui versão em acesso aberto
-
Status: Nenhuma versão em acesso aberto identificada -
ABNT
FERRO, J A e LARSON, R E. Calcium calmodulin regulation of atpase activity and endogenous phosphorylation of mammalian brain actomyosin. Biochemical and Biophysical Research Communication, v. 145, p. 1217-24, 1987Tradução . . Disponível em: https://doi.org/10.1016/0006-291x(87)91567-1. Acesso em: 15 mar. 2026. -
APA
Ferro, J. A., & Larson, R. E. (1987). Calcium calmodulin regulation of atpase activity and endogenous phosphorylation of mammalian brain actomyosin. Biochemical and Biophysical Research Communication, 145, 1217-24. doi:10.1016/0006-291x(87)91567-1 -
NLM
Ferro JA, Larson RE. Calcium calmodulin regulation of atpase activity and endogenous phosphorylation of mammalian brain actomyosin [Internet]. Biochemical and Biophysical Research Communication. 1987 ;145 1217-24.[citado 2026 mar. 15 ] Available from: https://doi.org/10.1016/0006-291x(87)91567-1 -
Vancouver
Ferro JA, Larson RE. Calcium calmodulin regulation of atpase activity and endogenous phosphorylation of mammalian brain actomyosin [Internet]. Biochemical and Biophysical Research Communication. 1987 ;145 1217-24.[citado 2026 mar. 15 ] Available from: https://doi.org/10.1016/0006-291x(87)91567-1 - Myosin motors
- Calcium regulation of the mechanochemical cycle of native myosin V
- Structural insights into functional overlapping and differentiation among myosin V motors
- Iq motif a putative consensus sequence for calmodulin binal sites that function in the absence of calcium
- Structural and functional studies of brain myosin
- Studies of brain myosin v (bmv) structure by hydrospatic pressure and fluorescence spectroscopy
- Selective proteolysis by calpain of an unconventional myosin from vertebrate brain generates head and tail domain
- Detection of two binding conformations of an iq motif with calmodulin
- Action changes the association between calmodulin and brain myosin-v
- Affinity chromatography of type i hexokinase from rat rain mitochondria
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