Species specificity of thimet oligopeptidase (ec3.4.24.15) (1996)
- Authors:
- USP affiliated authors: CAMARGO, ANTONIO CARLOS MARTINS DE - ICB ; FERNANDES, BEATRIZ LIEBLICH - ICB ; REBOUCAS, NANCY AMARAL - ICB ; FERRO, EMER SUAVINHO - ICB
- School: ICB
- Subjects: BIOFÍSICA; FISIOLOGIA; FARMACOLOGIA; MICROBIOLOGIA
- Language: Inglês
- Source:
- Título do periódico: Biological Chemistry Hoppe-Seyler
- Volume/Número/Paginação/Ano: v.377, p.283-91, 1996
-
ABNT
HAYASHI, M A F; GOMES, M D; REBOUÇAS, Nancy Amaral; et al. Species specificity of thimet oligopeptidase (ec3.4.24.15). Biological Chemistry Hoppe-Seyler[S.l.], v. 377, p. 283-91, 1996. -
APA
Hayashi, M. A. F., Gomes, M. D., Rebouças, N. A., Fernandes, B. L., Ferro, E. S., & Camargo, A. C. M. de. (1996). Species specificity of thimet oligopeptidase (ec3.4.24.15). Biological Chemistry Hoppe-Seyler, 377, 283-91. -
NLM
Hayashi MAF, Gomes MD, Rebouças NA, Fernandes BL, Ferro ES, Camargo ACM de. Species specificity of thimet oligopeptidase (ec3.4.24.15). Biological Chemistry Hoppe-Seyler. 1996 ;377 283-91. -
Vancouver
Hayashi MAF, Gomes MD, Rebouças NA, Fernandes BL, Ferro ES, Camargo ACM de. Species specificity of thimet oligopeptidase (ec3.4.24.15). Biological Chemistry Hoppe-Seyler. 1996 ;377 283-91. - Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain
- Stability of the MHC class I epitopes in the cytosol and the role of the thimet-oligopeptidase EC 3.4.24.151,2
- Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide
- Specific peptides of casein pancreatic digestion enhances the production of tetanus toxin
- Caracterizacao de dois clones de cdna selecionados de um banco de cerebro de coelho utilizando o anticorpo anti-endooligopeptidase a
- Thimet oligopeptidase and the stability of MHC class I epitopes in macrophages cytosol
- 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)
- Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC3.4.24.16) comparison with thimet oligopeptidase (EC3.4.24.15) and neprilysin (EC3.4.24.11)
- Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15)
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