Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol (1999)
- Authors:
- USP affiliated authors: FERNANDES, BEATRIZ LIEBLICH - ICB ; SILVA, CELIO LOPES - FMRP ; FERRO, EMER SUAVINHO - ICB
- Unidades: ICB; FMRP
- Subjects: HISTOLOGIA; MICROBIOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Biochemical and Biophysical Research Communications
- Volume/Número/Paginação/Ano: v. 255, p. 596-601, 1999
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ABNT
PORTARO, Fernanda C V et al. Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol. Biochemical and Biophysical Research Communications, v. 255, p. 596-601, 1999Tradução . . Acesso em: 19 fev. 2026. -
APA
Portaro, F. C. V., Gomes, M. D., Cabrera, A., Fernandes, B. L., Silva, C. L., Ferro, E. S., et al. (1999). Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol. Biochemical and Biophysical Research Communications, 255, 596-601. -
NLM
Portaro FCV, Gomes MD, Cabrera A, Fernandes BL, Silva CL, Ferro ES, Juliano L, Camargo ACM de. Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol. Biochemical and Biophysical Research Communications. 1999 ; 255 596-601.[citado 2026 fev. 19 ] -
Vancouver
Portaro FCV, Gomes MD, Cabrera A, Fernandes BL, Silva CL, Ferro ES, Juliano L, Camargo ACM de. Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol. Biochemical and Biophysical Research Communications. 1999 ; 255 596-601.[citado 2026 fev. 19 ] - Thimet oligopeptidase and the stability of MHC class I epitopes in macrophages cytosol
- 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
- Stability of the MHC class I epitopes in the cytosol and the role of the thimet-oligopeptidase EC 3.4.24.151,2
- A new protein onthe route of MHC-I associated antigen presentation: thimet-oligopeptidase 24.15 (EC 3.4.24.15)
- Plasmidio rp4 produz instabilidade genetica em proteus mirabilis
- Expressao do gene da alfa-amilase de bacillus subtilis sob o controle do promotor 010 do bacteriofago t7
- Development of an operational substrate for ZapA, a metalloprotease secreted by the bacterium Proteus mirabilis
- High efficiency of transformation of Proteus mirabilis with a pUC19 derivative vector directs the expression and secretion of the Bacillus subtilis alfa-amylase gene
- ZapA, a possible virulence factor from Proteus mirabilis exhibits broas protease substrate specificity
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