Proteolysis and peptidases (2004)
- Autor:
- Autor USP: FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Assunto: HISTOLOGIA
- Idioma: Inglês
- Resumo: Extralysosomal proteolysis by multicatalytic complexes such as the 26S proteasome produces large amounts of peptides in the cytosol, mitochondria and nuclei of eukaryotic cells, and there is increasing evidence that the resulting free intracellular peptides can modulate specific protein interactions. The demonstration that free peptides added to the intracellular milieu can regulate cellular functions mediated by protein interactions suggests new putative roles for these molecules in gene regulation, metabolism, cell signaling and protein targeting. Such interactions frequently involve specific consensus amino acid sequences that can be predicted based on similarities in domain composition. We have recently developed a new strategy for identifying novel natural peptides, the sequences of which correspond to fragments of intracellular proteins and contain putative post-translational modification sites. In this presentation, we show evidences that intracellular peptides released by proteasomes may be involved in regulating protein interactions. In particular, the cell biology of endopeptidase 24.15 (thimet oligopeptidase; EC 3.4.24.15) will be discussed in detail since this enzyme has been implicated in both extracellular and intracellular peptide metabolism
- Imprenta:
- Fonte:
- Título do periódico: Abstracts
- Nome do evento: Congress of the Brazilian Society for Cell Biology
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ABNT
FERRO, Emer Suavinho. Proteolysis and peptidases. 2004, Anais.. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo, 2004. . Acesso em: 19 abr. 2024. -
APA
Ferro, E. S. (2004). Proteolysis and peptidases. In Abstracts. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo. -
NLM
Ferro ES. Proteolysis and peptidases. Abstracts. 2004 ;[citado 2024 abr. 19 ] -
Vancouver
Ferro ES. Proteolysis and peptidases. Abstracts. 2004 ;[citado 2024 abr. 19 ] - Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)
- Peptidase activities and expression in spontaneously hypertensive rats
- Activation of the protease thimet-oligopeptidase E.C.3.4.24.15 by cytochrome C
- Desenvolvimento de plataforma para análise molecular de novos farmacos
- Ativação constitutiva e internalização do receptor AT1 da angiotensina II: papel da ponte dissulfeto CYS18-CYS274 e da terceira alça extracelular
- Além da conquista de Rocha e Silva. [Entrevista] por Daniela Pinto Senador
- Análise funcional da endopeptidases 24.15 (EC 3.4.24.15) e de seus mutantes com capacidade reduzida de interação à membrana plasmática
- Análise molecular da endopeptidase 24.25 (EC 3.4.24.15) nuclear
- Requisitos estruturais para a dimerização do receptor AT1 da angiotensina II
- Endopeptidase 24.15 (EC 3.4.24.15) detection in the imune system
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