Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group (1994)
- Authors:
- Autor USP: REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; ESCHERICHIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Biological Chemistry
- Volume/Número/Paginação/Ano: v.269, n.14, p.10461-6, 1994
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ABNT
MONTEIRO, P B et al. Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group. Journal of Biological Chemistry, v. 269, n. 14, p. 10461-6, 1994Tradução . . Acesso em: 15 mar. 2026. -
APA
Monteiro, P. B., Lataro, R. C., Ferro, J. A., & Reinach, F. de C. (1994). Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group. Journal of Biological Chemistry, 269( 14), 10461-6. -
NLM
Monteiro PB, Lataro RC, Ferro JA, Reinach F de C. Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group. Journal of Biological Chemistry. 1994 ;269( 14): 10461-6.[citado 2026 mar. 15 ] -
Vancouver
Monteiro PB, Lataro RC, Ferro JA, Reinach F de C. Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group. Journal of Biological Chemistry. 1994 ;269( 14): 10461-6.[citado 2026 mar. 15 ] - 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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