The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes (1998)
- Authors:
- USP affiliated authors: CAMARGO, ANTONIO CARLOS MARTINS DE - ICB ; FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Subjects: FARMACOLOGIA; HISTOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Resumos
- Conference titles: Reunião Anual da Federação de Sociedades de Biologia Experimental
-
ABNT
CAMARGO, Antonio Carlos Martins de et al. The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes. 1998, Anais.. São Paulo: FESBE, 1998. . Acesso em: 30 dez. 2025. -
APA
Camargo, A. C. M. de, Portaro, F. C. V., Silva, C. L., Gomes, M. D., Juliano, M. A., Juliano, L., & Ferro, E. S. (1998). The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes. In Resumos. São Paulo: FESBE. -
NLM
Camargo ACM de, Portaro FCV, Silva CL, Gomes MD, Juliano MA, Juliano L, Ferro ES. The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes. Resumos. 1998 ;[citado 2025 dez. 30 ] -
Vancouver
Camargo ACM de, Portaro FCV, Silva CL, Gomes MD, Juliano MA, Juliano L, Ferro ES. The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes. Resumos. 1998 ;[citado 2025 dez. 30 ] - 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)
- Descoberta de duas novas atividades farmacológicas para peptídeos ricos em prolina presentes no veneno da serpente Bothrops jararaca
- Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP)
- Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15)
- 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
- Intracellular oligopeptidase 24.15 (EC 3.4.24.15) inhibition during antigen presentation process
- A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15)
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