Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme (2003)
- Authors:
- USP affiliated authors: KRIEGER, JOSE EDUARDO - FM ; FERRO, EMER SUAVINHO - ICB
- Unidades: FM; ICB
- Assunto: HISTOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Biological Chemistry
- ISSN: 0021-9258
- Volume/Número/Paginação/Ano: v. 278, n. 10, p. 8547-55, 2003
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ABNT
RIOLI, V. et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Journal of Biological Chemistry, v. 278, n. 10, p. 8547-55, 2003Tradução . . Acesso em: 26 jan. 2026. -
APA
Rioli, V., Gozzo, F. C., Heimann, A. S., Linardi, A., Krieger, J. E., Shida, C. S., et al. (2003). Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Journal of Biological Chemistry, 278( 10), 8547-55. -
NLM
Rioli V, Gozzo FC, Heimann AS, Linardi A, Krieger JE, Shida CS, Almeida PC, Hyslop S, Eberlin MN, Ferro ES. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Journal of Biological Chemistry. 2003 ; 278( 10): 8547-55.[citado 2026 jan. 26 ] -
Vancouver
Rioli V, Gozzo FC, Heimann AS, Linardi A, Krieger JE, Shida CS, Almeida PC, Hyslop S, Eberlin MN, Ferro ES. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Journal of Biological Chemistry. 2003 ; 278( 10): 8547-55.[citado 2026 jan. 26 ] - Novel natural peptide substrates for endopeptidase 24.15, neurolysin and angiotensin-converting enzyme
- ACE gene titration in mice uncovers a new mechanism for ACE on the control of body weight
- Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)
- A novel bradykinin potentiating peptide isolated from "Bothrops Jararacussu" venom using catallytically inactive oligopeptidase EP24.15
- The tellurium compound RF-17 is a selective inhibitor of thimet oligopeptidase
- Catalytic properties of thimet oligopeptidase H600A mutante
- Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain
- The intracellular pharmacokinetics of terminally capped peptides
- Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC3.4.24.16) comparison with thimet oligopeptidase (EC3.4.24.15) and neprilysin (EC3.4.24.11)
- Substrate binding and catalysis of the neuropeptide processing enzyme EC3.4.24.15 (EP24.15) and regulation of the neurome
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