Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP) (2002)
- Authors:
- USP affiliated authors: CAMARGO, ANTONIO CARLOS MARTINS DE - ICB ; FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Subjects: FARMACOLOGIA; HISTOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
OLIVEIRA, Vitor et al. Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP). 2002, Anais.. São Paulo: SBBq, 2002. . Acesso em: 29 dez. 2025. -
APA
Oliveira, V., Gatti, R., Rioli, V., Ferro, E. S., Spisni, A., Camargo, A. C. M. de, et al. (2002). Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP). In Programa e Resumos. São Paulo: SBBq. -
NLM
Oliveira V, Gatti R, Rioli V, Ferro ES, Spisni A, Camargo ACM de, Juliano MA, Juliano L. Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP). Programa e Resumos. 2002 ;[citado 2025 dez. 29 ] -
Vancouver
Oliveira V, Gatti R, Rioli V, Ferro ES, Spisni A, Camargo ACM de, Juliano MA, Juliano L. Temperature and salts effects on peptidase activities of the recombinant metallo oligopeptidases neurolysin and thimet oligopeptidase (TOP). Programa e Resumos. 2002 ;[citado 2025 dez. 29 ] - 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
- The possible role cytosolic oligopeptidases in the processing and presentation of antigen class I epitopes
- 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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