The neuropeptide processing enzyme EC 3.2.24.15 is modulated by protein kinase A phosphorilation (2000)
- Authors:
- USP affiliated authors: FERRO, EMER SUAVINHO - ICB
- Unidades: ICB
- Subjects: HISTOLOGIA
- Language: Inglês
-
ABNT
TULLAI, John W; CUMMINS, Philip M; PABON, Amanda; et al. The neuropeptide processing enzyme EC 3.2.24.15 is modulated by protein kinase A phosphorilation. [S.l.], 2000. -
APA
Tullai, J. W., Cummins, P. M., Pabon, A., Roberts, J. L., Lopingco, M. C., Shrimpton, C. N., et al. (2000). The neuropeptide processing enzyme EC 3.2.24.15 is modulated by protein kinase A phosphorilation. -
NLM
Tullai JW, Cummins PM, Pabon A, Roberts JL, Lopingco MC, Shrimpton CN, Smith AI, Martignetti JA, Ferro ES, Glucksman MJ. The neuropeptide processing enzyme EC 3.2.24.15 is modulated by protein kinase A phosphorilation. 2000 ; -
Vancouver
Tullai JW, Cummins PM, Pabon A, Roberts JL, Lopingco MC, Shrimpton CN, Smith AI, Martignetti JA, Ferro ES, Glucksman MJ. The neuropeptide processing enzyme EC 3.2.24.15 is modulated by protein kinase A phosphorilation. 2000 ; - Além da conquista de Rocha e Silva. [Entrevista] por Daniela Pinto Senador
- Análise funcional da endopeptidases 24.15 (EC 3.4.24.15) e de seus mutantes com capacidade reduzida de interação à membrana plasmática
- Análise molecular da endopeptidase 24.25 (EC 3.4.24.15) nuclear
- Requisitos estruturais para a dimerização do receptor AT1 da angiotensina II
- Endopeptidase 24.15 (EC 3.4.24.15) detection in the imune system
- Peptidase activities and expression in spontaneously hypertensive rats
- Site specific determinants of protein oxidative oligomerization
- Intracellullar peptides as putative natural regulators of protein interactions
- Activation of the protease thimet-oligopeptidase E.C.3.4.24.15 by cytochrome C
- Substrate binding and catalysis of the neuropeptide processing enzyme EC3.4.24.15 (EP24.15) and regulation of the neurome
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