E 3 Ubiquitin Ligase
Mostrando 1-12 de 285 artigos, teses e dissertações.
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1. E3 ubiquitin ligase Cbl-b potentiates the apoptotic action of arsenic trioxide by inhibiting the PI3K/Akt pathway
Arsenic trioxide (ATO) is a strong inducer of apoptosis in malignant hematological cells. Inducible phosphatidyl inositol 3 kinase (PI3K)-Akt activation promotes resistance to ATO. In the present study, we evaluated whether E3 ubiquitin ligase Cbl-b, a negative regulator of PI3K activation, is involved in the action of ATO. The effect of ATO on cell viabilit
Brazilian Journal of Medical and Biological Research. Publicado em: 2011-02
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2. Associação entre o proteassoma e o inibidor de protease BTCI : caracterização fisico-química e efeitos moleculares em células de câncer de mama (MCF-7)
Dietas ricas em leguminosas têm sido associadas à baixa incidência de câncer em populações humanas, sendo essas plantas, ricas em inibidores de proteases. O BTCI (black-eyed pea trypsin/chymotrypsin inhibitor) é um inibidor de protease da família Bowman-Birk, isolado de sementes da leguminosa Vigna unguiculata (feijão-de-corda), que inibe a tripsina
Publicado em: 2010
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3. Study of Arkadia expression, ubiquitination E-3 protein, in thyroid tumors and its relation to the TGF-beta signaling pathway. / Estudo da expressão de Arkadia, proteína E3 de ubiquitinação, em tumores de tiróide e sua relação com a via de sinalização de TGF-Beta.
Arkadia participa do processo de amplificação da sinalização de TGF-b mediada por Smads, via degradação do I-Smad. O objetivo desse estudo foi caracterizar e investigar a influência de Arkadia em linhagens celulares de cânceres de tiróide. A expressão gênica de Arkadia em linhagens celulares de carcinomas papílifero (NPA), folicular (WRO) e anapl
Publicado em: 2009
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4. Caracterização da participação do sistema de ubiquitinação e degradação proteassômica no bloqueio do ciclo celular mediado pela proteína Vpr do HIV-1
HIV-1 Vpr is a viral accessory protein that activates ATR through the induction of DNA replication stress. ATR activation results in cell cycle arrest in G2 and induction of apoptosis. In the present study, we investigate the role of the ubiquitin/proteasome system (UPS) in the above activity of Vpr. We report that the general function of the UPS is required
Publicado em: 2008
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5. In silico analysis identifies a C3HC4-RING finger domain of a putative E3 ubiquitin-protein ligase located at the C-terminus of a polyglutamine-containing protein
Almost identical polyglutamine-containing proteins with unknown structures have been found in human, mouse and rat genomes (GenBank AJ277365, AF525300, AY879229). We infer that an identical new gene (RING) finger domain of real interest is located in each C-terminal segment. A three-dimensional (3-D) model was generated by remote homology modeling and the fu
Brazilian Journal of Medical and Biological Research. Publicado em: 18/02/2007
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6. Estudos funcionais e estruturais da proteína recombinante humana UBE2G2 (Ubiquitin-conjugating enzyme E2G2).
The ubiquitin system represents a selective mechanism for intracellular proteolysis in eukaryotic cells that involves the sequential activity of three enzymes, E1 (Ubiquitin activating enzyme), E2 (Ubiquitin-conjugating enzyme), and E3 (Ubiquitin-protein ligase). The identification of these proteins and their targets as well as structural data is essential t
Publicado em: 2005
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7. Identificação, caracterização e estudo da expressão dos genes hsc70 e hsp83 em Rhynchosciara americana / Identification, characterization and study of expression of the genes hsc70 and hsp83 in Rhynchosciara americana
With the idea of identify some of these proteins involved in the folding process of the proteins synthesized on the Rhynchosciara salivary gland, this project started adopting the shotgun cDNA sequencing strategy. This cDNA library was constructed utilizing salivary glands of Rhynchosciara americana at a developmental period where the cocoon construction beg
Publicado em: 2005
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8. A Label-free Quantitative Proteomics Strategy to Identify E3 Ubiquitin Ligase Substrates Targeted to Proteasome Degradation*
The ubiquitin-proteasome system is a central mechanism for controlled proteolysis that regulates numerous cellular processes in eukaryotes. As such, defects in this system can contribute to disease pathogenesis. In this pathway, E3 ubiquitin ligases provide platforms for binding specific substrates, thereby coordinating their ubiquitylation and subsequent de
The American Society for Biochemistry and Molecular Biology.
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9. Identification of the von Hippel–Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
Mutations of von Hippel–Lindau disease (VHL) tumor-suppressor gene product (pVHL) are found in patients with dominant inherited VHL syndrome and in the vast majority of sporadic clear cell renal carcinomas. The function of the pVHL protein has not been clarified. pVHL has been shown to form a complex with elongin B and elongin C (VBC) and with cullin (CUL)
The National Academy of Sciences.
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10. LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation
LNX is a RING finger and PDZ domain containing protein that interacts with the cell fate determinant Numb. To investigate the function of LNX, we tested its RING finger domain for ubiquitin ligase activity. The isolated RING finger domain was able to function as an E2-dependent, E3 ubiquitin ligase in vitro and mutation of a conserved cysteine residue within
Oxford University Press.
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11. Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes
Infected cell protein 0 (ICP0) of herpes simplex virus 1, a multifunctional ring finger protein, enhances the expression of genes introduced into cells by infection or transfection, interacts with numerous cellular and viral proteins, and is associated with the degradation of several cellular proteins. Sequences encoded by exon 2 of ICP0 (residues 20–241)
The National Academy of Sciences.
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12. E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)
Protein ubiquitinylation plays a key role in many important cellular processes. Ubiquitinylation requires the E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and, frequently, a substrate-specific E3 ubiquitin-protein ligase. In one class of E3 ubiquitin ligases, the catalytic domain contains a zinc-binding RING finger motif. ARD1 (ADP-rib
National Academy of Sciences.