Fluorescence quenching studies of tropomyosin mutants: interactions with actin and troponin (2000)
- Authors:
- USP affiliated authors: ITO, AMANDO SIUITI - IF ; FARAH, SHAKER CHUCK - IQ
- Unidades: IF; IQ
- Subjects: BIOQUÍMICA; PROTEÍNAS; TROPONINA
- Language: Inglês
- Imprenta:
- Source:
- Título: Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
HOLTHAUZEN, Luís Marcelo F. e ITO, Amando S. e FARAH, Chuck Shaker. Fluorescence quenching studies of tropomyosin mutants: interactions with actin and troponin. 2000, Anais.. São Paulo: SBBq, 2000. . Acesso em: 12 jul. 2025. -
APA
Holthauzen, L. M. F., Ito, A. S., & Farah, C. S. (2000). Fluorescence quenching studies of tropomyosin mutants: interactions with actin and troponin. In Resumos. São Paulo: SBBq. -
NLM
Holthauzen LMF, Ito AS, Farah CS. Fluorescence quenching studies of tropomyosin mutants: interactions with actin and troponin. Resumos. 2000 ;[citado 2025 jul. 12 ] -
Vancouver
Holthauzen LMF, Ito AS, Farah CS. Fluorescence quenching studies of tropomyosin mutants: interactions with actin and troponin. Resumos. 2000 ;[citado 2025 jul. 12 ] - Stability of troponin I and T investigated by a hydrophobic fluorescent probe
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- A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization
- Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen
- 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
- Solution structure of ApaG from Xanthomonas axonopodis pv. citri reveals a fibronectin-3 fold
- Identification of the flagellar chaperone FlgN in the phytopathogen Xanthomonas axonopodis pathovar citri by its interaction with hook-associated FlgK
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