Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein (1996)
- Authors:
- USP affiliated authors: CAMARGO, ANTONIO CARLOS MARTINS DE - ICB ; FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Assunto: FARMACOLOGIA
- Language: Inglês
- Source:
- Título do periódico: Brazilian Journal of Morphological Sciences
- Volume/Número/Paginação/Ano: v.13, n.1 , p.134, 1996
- Conference titles: Brazilian Congress of Cell Biology
-
ABNT
FERRO, Emer Suavinho et al. Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein. Brazilian Journal of Morphological Sciences. [S.l.]: Instituto de Ciências Biomédicas, Universidade de São Paulo. . Acesso em: 28 abr. 2024. , 1996 -
APA
Ferro, E. S., Glucksman, M. J., Tambourgi, D. V., Gomes, M. D., Juliano, L., Camargo, A. C. M. de, & Roberts, J. L. (1996). Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein. Brazilian Journal of Morphological Sciences. Instituto de Ciências Biomédicas, Universidade de São Paulo. -
NLM
Ferro ES, Glucksman MJ, Tambourgi DV, Gomes MD, Juliano L, Camargo ACM de, Roberts JL. Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein. Brazilian Journal of Morphological Sciences. 1996 ;13( 1 ): 134.[citado 2024 abr. 28 ] -
Vancouver
Ferro ES, Glucksman MJ, Tambourgi DV, Gomes MD, Juliano L, Camargo ACM de, Roberts JL. Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein. Brazilian Journal of Morphological Sciences. 1996 ;13( 1 ): 134.[citado 2024 abr. 28 ] - 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)
- Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15)
- Descoberta de duas novas atividades farmacológicas para peptídeos ricos em prolina presentes no veneno da serpente Bothrops jararaca
- 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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