Calcium-induced dimerization of troponin c: mode of interaction and use of trifluorethanol as a denaturant of quaternary structure (1995)
- Authors:
- Autor USP: REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 1995
- Source:
- Título: Biochemistry
- Volume/Número/Paginação/Ano: v.34, n.22, p.7365-75, 1995
-
ABNT
SLUPSKY, C M et al. Calcium-induced dimerization of troponin c: mode of interaction and use of trifluorethanol as a denaturant of quaternary structure. Biochemistry, v. 34, n. 22, p. 7365-75, 1995Tradução . . Acesso em: 04 mar. 2026. -
APA
Slupsky, C. M., Kay, C. M., Reinach, F. de C., Smillie, L. B., & Sykes, B. D. (1995). Calcium-induced dimerization of troponin c: mode of interaction and use of trifluorethanol as a denaturant of quaternary structure. Biochemistry, 34( 22), 7365-75. -
NLM
Slupsky CM, Kay CM, Reinach F de C, Smillie LB, Sykes BD. Calcium-induced dimerization of troponin c: mode of interaction and use of trifluorethanol as a denaturant of quaternary structure. Biochemistry. 1995 ;34( 22): 7365-75.[citado 2026 mar. 04 ] -
Vancouver
Slupsky CM, Kay CM, Reinach F de C, Smillie LB, Sykes BD. Calcium-induced dimerization of troponin c: mode of interaction and use of trifluorethanol as a denaturant of quaternary structure. Biochemistry. 1995 ;34( 22): 7365-75.[citado 2026 mar. 04 ] - Complete sequence of human fast-type and slow-type muscle myosin -binding-protein c (mybp-c)
- The interface between MyBP-C and myosin: site-directed mutagenesis of the CX myosin-binding domain of MyBP-C
- Determinants of ion specificity in the smooth muscle myosin light chain 'CA POT.2+' / 'MG POT.2+' binding site
- Fluorescence studies of the troponin i - troponin c interaction
- Site-directed mutagenesis in the 'CA POT.2+' / 'MG POT.2+'-binding site of smooth muscle myosin regulatory light chain
- Study of the inhibitory mechanism of troponin i by site-directed mutagenesis
- Studies on the regulation of muscle contraction by troponin-tropomyosin
- Distinct regions of troponin i regulate 'CA POT.2+' dependent activation and 'CA POT.2+' sensitivity of the acto-s1-tm atpase activity of the thin filament
- Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene
- Myosin-binding domain of skeletal muscle mybp-c (c protein) resides in the c-terminal immunoglobulin c2 motif
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