Action changes the association between calmodulin and brain myosin-v (1996)
- Authors:
- Autor USP: LARSON, ROY EDWARD - FMRP
- Unidade: FMRP
- Assunto: BIOLOGIA
- Language: Inglês
- Source:
- Título: Molecular Biology and Cellular
- Volume/Número/Paginação/Ano: v.7 , p.372, 1996
- Conference titles: Annual Meeting of the American Society for Cell Biology
-
ABNT
CAMERON, L C et al. Action changes the association between calmodulin and brain myosin-v. Molecular Biology and Cellular. [S.l.]: Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo. . Acesso em: 13 mar. 2026. , 1996 -
APA
Cameron, L. C., Carvalho, R. N., Araujo, J. R. V., Teixeira, F. M., Santos, A. C., Tauhata, S. F. B., et al. (1996). Action changes the association between calmodulin and brain myosin-v. Molecular Biology and Cellular. Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo. -
NLM
Cameron LC, Carvalho RN, Araujo JRV, Teixeira FM, Santos AC, Tauhata SFB, Larson RE, Sorensen MW. Action changes the association between calmodulin and brain myosin-v. Molecular Biology and Cellular. 1996 ;7 372.[citado 2026 mar. 13 ] -
Vancouver
Cameron LC, Carvalho RN, Araujo JRV, Teixeira FM, Santos AC, Tauhata SFB, Larson RE, Sorensen MW. Action changes the association between calmodulin and brain myosin-v. Molecular Biology and Cellular. 1996 ;7 372.[citado 2026 mar. 13 ] - 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
- Affinity chromatography of type i hexokinase from rat rain mitochondria
- Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay
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