A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15) (1998)
- Authors:
- USP affiliated authors: FERRO, EMER SUAVINHO - ICB ; SILVA, CELIO LOPES - FMRP ; CAMARGO, ANTONIO CARLOS MARTINS DE - ICB
- Unidades: ICB; FMRP
- Assunto: HISTOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Resumos
- Conference titles: Reunião Anual da Federação de Sociedades de Biologia Experimental
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ABNT
PORTARO, F C V et al. A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15). 1998, Anais.. São Paulo: FESBE, 1998. . Acesso em: 24 abr. 2024. -
APA
Portaro, F. C. V., Silva, C. L., Gomes, M. D., Juliano, M. A., Juliano, L., Ferro, E. S., & Camargo, A. C. M. de. (1998). A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15). In Resumos. São Paulo: FESBE. -
NLM
Portaro FCV, Silva CL, Gomes MD, Juliano MA, Juliano L, Ferro ES, Camargo ACM de. A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15). Resumos. 1998 ;[citado 2024 abr. 24 ] -
Vancouver
Portaro FCV, Silva CL, Gomes MD, Juliano MA, Juliano L, Ferro ES, Camargo ACM de. A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15). Resumos. 1998 ;[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
- Structural features which make oligopeptides suscetible to hydrolysis by recombinant timet-oligopeptidase 24.15 (TOP)
- The mycobacterium leprae hsp65 displays proteolytic activity: Mutagenesis studies indicate that the M. leprae hsp65 proteolytic activity is catalytically related to the HslVU protease
- A novel protein on the route of MHC class-I antigen presentation
- Thimet oligopeptidase (EC 3.4.24.15), a novel protein on the route of MHC class I antigenpresentation
- Intracellular oligopeptidase 24.15 (EC 3.4.24.15) inhibition during antigen presentation process
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