Tropomyosin fragments: interactions with troponin and actin (1999)
- Autores:
- Autor USP: FARAH, SHAKER CHUCK - IQ
- Unidade: IQ
- Assuntos: BIOQUÍMICA; PROTEÍNAS
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Programa e Resumos
- Nome do evento: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
PAULUCCI, Adriana A. e FARAH, Chuck Shaker. Tropomyosin fragments: interactions with troponin and actin. 1999, Anais.. São Paulo: SBBq, 1999. . Acesso em: 19 set. 2024. -
APA
Paulucci, A. A., & Farah, C. S. (1999). Tropomyosin fragments: interactions with troponin and actin. In Programa e Resumos. São Paulo: SBBq. -
NLM
Paulucci AA, Farah CS. Tropomyosin fragments: interactions with troponin and actin. Programa e Resumos. 1999 ;[citado 2024 set. 19 ] -
Vancouver
Paulucci AA, Farah CS. Tropomyosin fragments: interactions with troponin and actin. Programa e Resumos. 1999 ;[citado 2024 set. 19 ] - Stability of troponin I and T investigated by a hydrophobic fluorescent probe
- A tropomyosin mutant containing a intrinsic fluorescent probe may be used to study head-to-tail interaction thermodynamics
- Structural genomics of the phytopathogen Xanthomonas axonopodis pv citri
- Ca2+-induced rolling of tropomyosin in muscle thin filaments - The alpha- and beta-band hypothesis revisited
- A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization
- New protein fold from Xanthomonas axonopodis pv citri YaeQ
- Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen
- High-throughput screening of Xanthomonas axonopodis pv citri targets for structural proteomics using NMR
- Strategy for determining the binding site of tropomyosin on actin
- Deciphering the head-to-tail complex of 'alpha'-tropomyosin using double mutant cycles and molecular docking
Como citar
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
