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 (1997)
- Authors:
- USP affiliated authors: QUAGGIO, RONALDO BENTO - IQ ; FARAH, SHAKER CHUCK - IQ ; REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
VALÊNCIA, F E et al. 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. 1997, Anais.. São Paulo: SBBQ, 1997. . Acesso em: 19 abr. 2024. -
APA
Valência, F. E., Lee, M. F., Ramos, C. H. I., Quaggio, R. B., Farah, C. S., & Reinach, F. de C. (1997). 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. In . São Paulo: SBBQ. -
NLM
Valência FE, Lee MF, Ramos CHI, Quaggio RB, Farah CS, Reinach F de C. 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. 1997 ;[citado 2024 abr. 19 ] -
Vancouver
Valência FE, Lee MF, Ramos CHI, Quaggio RB, Farah CS, Reinach F de C. 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. 1997 ;[citado 2024 abr. 19 ] - Direct 'Ca POT.2+'-binding assays two special-probes of chicken troponin-C
- Parallel measurement of 'Ca POT. 2+' binding and fluorescence emission upon 'Ca POT. 2+' titration of recombinant skeletal muscle troponin C - Measurement of sequential calcium binding to the regulatory sites
- Xanthomonas genes associated with plant pathogenicity
- Structural and functional studies on troponin C interactions
- 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
- 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
- Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan
- Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
