Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity (2000)
- Authors:
- USP affiliated authors: FARAH, SHAKER CHUCK - IQ ; REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; ESCHERICHIA COLI; TROPONINA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Biological Chemistry
- ISSN: 0021-9258
- Volume/Número/Paginação/Ano: v. 275, n. 36, p. 27513-27519, 2000
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ABNT
OLIVEIRA, Daniela Mara de; NAKAIE, Clovis Ryuichi; SOUSA, Aurea D; FARAH, Chuck Shaker; REINACH, Fernando de Castro. Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity. Journal of Biological Chemistry, Bethesda, v. 275, n. 36, p. 27513-27519, 2000. -
APA
Oliveira, D. M. de, Nakaie, C. R., Sousa, A. D., Farah, C. S., & Reinach, F. de C. (2000). Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity. Journal of Biological Chemistry, 275( 36), 27513-27519. -
NLM
Oliveira DM de, Nakaie CR, Sousa AD, Farah CS, Reinach F de C. Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity. Journal of Biological Chemistry. 2000 ; 275( 36): 27513-27519. -
Vancouver
Oliveira DM de, Nakaie CR, Sousa AD, Farah CS, Reinach F de C. Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity. Journal of Biological Chemistry. 2000 ; 275( 36): 27513-27519. - Fluorescence and regulatory properties of reconbinant tropomyosins containing 5-hydroxytryptophan: `Ca POT.2+'-binding to troponin results in conformational change in region of tropomyosin well away from the troponin binding site
- Regulatory properties of the 'N''H IND.2' and 'COOH' terminal domains of troponin T: ATPase activation and binding to TnI and TnC
- Structural and functional studies on troponin C interactions
- Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan
- Study of `Ca POT 2+´-independent interaction of TnT with tropomyosin using a tropomyosin with a intrinsic fluorescent 5-hydroxytryotophan probe
- Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin
- Regulatory properties of recombinant tropomyosins containing 5-hydroxytryptophan: ´Ca POT. 2+´-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site
- Looking at 'Ca POT.2+' binding properties of troponin-C, Troponin and thin filaments using the fluorescence of a 5-OH-tryptophan probe incorporated into troponin-C
- Determinants of affinity and specificity in the EF-HAND site of the smooth muscle myosin regulatory light chain
- Probing the calcium induced switch in troponin complex: two new intrinsic spectral probes of troponin I
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