Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain (2000)
- Authors:
- USP affiliated authors: FERRO, EMER SUAVINHO - ICB ; FERNANDES, BEATRIZ LIEBLICH - ICB ; REBOUCAS, NANCY AMARAL - ICB ; CAMARGO, ANTONIO CARLOS MARTINS DE - ICB
- Unidade: ICB
- Assunto: FISIOLOGIA
- Language: Inglês
-
ABNT
HAYASHI, Mirian A F et al. Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain. 2000Tradução . . Acesso em: 19 abr. 2024. -
APA
Hayashi, M. A. F., Portaro, F. C. V., tambourgi, D. V., Sucupira, M., Fernandes, B. L., Ferro, E. S., et al. (2000). Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain. -
NLM
Hayashi MAF, Portaro FCV, tambourgi DV, Sucupira M, Fernandes BL, Ferro ES, Rebouças NA, Camargo ACM, Ferro ES. Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain. 2000 ;[citado 2024 abr. 19 ] -
Vancouver
Hayashi MAF, Portaro FCV, tambourgi DV, Sucupira M, Fernandes BL, Ferro ES, Rebouças NA, Camargo ACM, Ferro ES. Molecular and immunological evidences demonstrate that endooligopeptidase A is the predominat cytosolic oligopeptidase of rabbit brain. 2000 ;[citado 2024 abr. 19 ] - Species specificity of thimet oligopeptidase (ec3.4.24.15)
- Stability of the MHC class I epitopes in the cytosol and the role of the thimet-oligopeptidase EC 3.4.24.151,2
- Caracterizacao de dois clones de cdna selecionados de um banco de cerebro de coelho utilizando o anticorpo anti-endooligopeptidase a
- Specific peptides of casein pancreatic digestion enhances the production of tetanus toxin
- 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)
- 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
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