Complete sequence of the mouse skeletal muscle myosin binding protein h (mybp-h) (1996)
- Authors:
- Autor USP: REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Assunto: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reuniao Anual da Sociedade Brasileira de Bioquimica e Biologia Molecular
-
ABNT
RAMOS, C e FISCHMAN, D A e REINACH, Fernando de Castro. Complete sequence of the mouse skeletal muscle myosin binding protein h (mybp-h). 1996, Anais.. São Paulo: Sbbq, 1996. . Acesso em: 21 maio 2024. -
APA
Ramos, C., Fischman, D. A., & Reinach, F. de C. (1996). Complete sequence of the mouse skeletal muscle myosin binding protein h (mybp-h). In Programa e Resumos. São Paulo: Sbbq. -
NLM
Ramos C, Fischman DA, Reinach F de C. Complete sequence of the mouse skeletal muscle myosin binding protein h (mybp-h). Programa e Resumos. 1996 ;[citado 2024 maio 21 ] -
Vancouver
Ramos C, Fischman DA, Reinach F de C. Complete sequence of the mouse skeletal muscle myosin binding protein h (mybp-h). Programa e Resumos. 1996 ;[citado 2024 maio 21 ] - Complete sequence of human fast-type and slow-type muscle myosin -binding-protein c (mybp-c)
- The effect of regulatory ' Ca POT. 2+' on the in situ structures of troponin C and troponin I: a neutron scattering study
- Engineering the calcium binding sites of myosin light chain and skeletal muscle
- Construction, bacterial expression, and purification of deletion mutants of troponin i
- Construction of a regulatory myosin light chain capable regulation of myosin
- Sequences of complete cdnas encoding four variants of chicken skeletal muscle troponin t
- Glu 88 is involved in troponin - c interactions with the regulatory proteins of the thin filament in vertebrate skeletal muscle fibers
- Hybrid myosin regulatory light chain containing a troponin c metal binding site
- Study of the inhibitory mechanism of troponin i by site-directed mutagenesis
- Sequenciamento de dna
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas