Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP) (1997)
- Authors:
- USP affiliated authors: FERRO, EMER SUAVINHO - ICB ; CAMARGO, ANTONIO CARLOS MARTINS DE - ICB
- Unidade: ICB
- Subjects: HISTOLOGIA; FARMACOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Resumos
- Conference titles: Reunião Anual da Federação de Sociedades de Biologia Experimental
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ABNT
GOMES, M D et al. Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP). 1997, Anais.. São Paulo: FESBE, 1997. . Acesso em: 24 abr. 2024. -
APA
Gomes, M. D., Reichl, A. P., Jacchieri, S., Ferro, E. S., Hirata, I. Y., Juliano, L., & Camargo, A. C. M. de. (1997). Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP). In Resumos. São Paulo: FESBE. -
NLM
Gomes MD, Reichl AP, Jacchieri S, Ferro ES, Hirata IY, Juliano L, Camargo ACM de. Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP). Resumos. 1997 ;[citado 2024 abr. 24 ] -
Vancouver
Gomes MD, Reichl AP, Jacchieri S, Ferro ES, Hirata IY, Juliano L, Camargo ACM de. Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP). Resumos. 1997 ;[citado 2024 abr. 24 ] - 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
- Secretion of the endo-oligopeptidase 24.15 (3.4.24.15), a non signal-peptide containing protein
- 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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