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
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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 ; - Comparative fine structural distribution of thimet oligopeptidase (EC3.4.24.15) and neurolysin (EC3.4.24.16) in rat brain
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- Análise molecular da via de secreção alternativa das endooligopeptidades thimet-oligopeptidase (EC3.4.24.15) e neurolisina (EC3. 4. 24.16)
- Initial peptide content characterization in mammalian tissues using LC-ESI-MS/MS
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- 14.3.3 plays important role on endopeptidase 24.15 (EC 3.4.24.15) secretion
- Análise molecular da endopeptidase 24.15 (EC 3.4.24.15) nuclear
- Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress
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