Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15) (1997)
- Authors:
- USP affiliated authors: CAMARGO, ANTONIO CARLOS MARTINS DE - ICB ; FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Assunto: FARMACOLOGIA
- Language: Inglês
- Imprenta:
- Publisher place: Colchester
- Date published: 1997
- Source:
- Título do periódico: Biochemical Journal
- Volume/Número/Paginação/Ano: v. 324, pt. 2, p. 517-522, 1997
-
ABNT
CAMARGO, Antonio Carlos Martins de et al. Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15). Biochemical Journal, v. 324, p. 517-522, 1997Tradução . . Acesso em: 23 abr. 2024. -
APA
Camargo, A. C. M. de, Gomes, M. D., Reichl, A. P., Ferro, E. S., Jacchieri, S., & Juliano, L. (1997). Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15). Biochemical Journal, 324, 517-522. -
NLM
Camargo ACM de, Gomes MD, Reichl AP, Ferro ES, Jacchieri S, Juliano L. Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15). Biochemical Journal. 1997 ; 324 517-522.[citado 2024 abr. 23 ] -
Vancouver
Camargo ACM de, Gomes MD, Reichl AP, Ferro ES, Jacchieri S, Juliano L. Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15). Biochemical Journal. 1997 ; 324 517-522.[citado 2024 abr. 23 ] - The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes
- Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP)
- Descoberta de duas novas atividades farmacológicas para peptídeos ricos em prolina presentes no veneno da serpente Bothrops jararaca
- Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein
- Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP)
- A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15)
- Intracellular oligopeptidase 24.15 (EC 3.4.24.15) inhibition during antigen presentation process
- Distinta distribuição subcelular da thimet oligopeptidase (EC 3.4.24.15) e neurolisina (EC 3.4.24.16) no cérebro de ratos
- Intracellular oligopeptidase 24.15 (EC 3.4.24.15) inhibition during antigen presentation process
- Stability of the MHC class I epitopes in the cytosol and the role of the thimet-oligopeptidase EC 3.4.24.151,2
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