Protein Ubiquitination
Mostrando 13-24 de 431 artigos, teses e dissertações.
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13. Expression of USP2a and study of its interaction with clathrin in human oral squamous carcinoma and prostate cancer cells / Estudo da expressão da enzima desubiquitinante USP2a e de sua interação com a proteina clatrina em celulas derivadas de carcinomas espinocelulares bucais e de prostata humanos
The ubiquitin (Ub)-proteasome pathway controls cellular protein turnover by degrading targeted intracellular proteins tagged with poly-Ub chains. Ubiquitination is a reversible process and the deubiquitinating enzymes (DUBs) are proteases that specifically cleave off Ub from Ub-protein conjugates. They can act in a preproteasomal level removing the poly-Ub t
Publicado em: 2007
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14. Expressão da acido graxo sintase, ErbB-2, p27 E Skp2 na carinogenese bucal induzida por 1-oxido 4-nitroquinolina em camundongos e efeito antitumoral do Orlistat / Fatty Acid Sintase, ErbB-2, p27 E Skp2 expression in oral carcinogenesis induced by 4-nitroquinoline 1-oxide and antitumoral Orlistat effects
Squamous cell carcinoma of the oral cavity is one of the most common malignant epithelial neoplasms, and a better understanding of its molecular pathways could help the development of new treatment or preventive agents. Several proteins such as Fatty Acid Synthase (FAS), ErbB-2, p27 and Skp2 are involved in the tumorigenesis process. FAS has an enzyme with m
Publicado em: 2007
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15. RNF5, a RING Finger Protein That Regulates Cell Motility by Targeting Paxillin Ubiquitination and Altered Localization
RNF5 is a RING finger protein found to be important in the growth and development of Caenorhabditis elegans. The search for RNF5-associated proteins via a yeast two-hybrid screen identified a LIM-containing protein in C. elegans which shows homology with human paxillin. Here we demonstrate that the human homologue of RNF5 associates with the amino-terminal d
American Society for Microbiology.
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16. Rapid Ca2+-dependent decrease of protein ubiquitination at synapses
Protein ubiquitination has been implicated in the regulation of axonal growth and synaptic plasticity as well as in the pathogenesis of neurodegenerative diseases. Here we show that depolarization-dependent Ca2+ influx into synaptosomes produces a global, rapid (range of seconds), and reversible decrease of the ubiquitinated state of proteins, which correlat
National Academy of Sciences.
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17. Critical Contribution of the MDM2 Acidic Domain to p53 Ubiquitination
MDM2 is an E3 ubiquitin ligase that targets p53 for proteasomal degradation. Recent studies have shown, however, that the ring-finger domain (RFD) of MDM2, where the ubiquitin E3 ligase activity resides, is necessary but not sufficient for p53 ubiquitination, suggesting that an additional activity of MDM2 might be required. To test this possibility, we gener
American Society for Microbiology.
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18. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
A RING finger-containing protein (AO7) that binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination was identified. Mutations of cation-coordinating residues within AO7’s RING finger abolished ubiquitination, as did chelation of zinc. Several otherwise-unrelated RING finger proteins, including BRCA1, Siah-1, TRC8, NF-X1
The National Academy of Sciences.
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19. Ubiquitination Regulates Proteolytic Processing of G Protein-coupled Receptors after Their Sorting to Lysosomes*
Ubiquitination is essential for the endocytic sorting of various G protein-coupled receptors to lysosomes. Here we identify a distinct function of this covalent modification in controlling the later proteolytic processing of receptors. Mutation of all cytoplasmic lysine residues in the murine δ-opioid receptor blocked receptor ubiquitination without prevent
American Society for Biochemistry and Molecular Biology.
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20. Altered ubiquitination and stability of aquaporin-1 in hypertonic stress
Aquaporin-1 (AQP1) water channel protein expression is increased by hypertonic stress. The contribution of changes in protein stability to hypertonic induction of AQP1 have not been described. Incubation of BALB/c fibroblasts spontaneously expressing AQP1 with proteasome inhibitors increased AQP1 expression, suggesting basal proteasome-dependent degrada
The National Academy of Sciences.
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21. Alternate exon insertion controls selective ubiquitination and degradation of different AUF1 protein isoforms
The A+U-rich element (ARE) in the 3′ non-coding region (3′ NCR) of short-lived cytokine mRNAs binds several regulatory proteins, including hnRNP D/AUF1, which comprises four isoforms of 37, 40, 42 and 45 kDa. ARE-mRNA degradation involves ubiquitin–proteasome activity, and one or more AUF1 proteins are thought to be ubiquitinated. Here we have characte
Oxford University Press.
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22. Ubiquitin-mediated Targeting of a Mutant Plasma Membrane ATPase, Pma1-7, to the Endosomal/Vacuolar System in Yeast
Pma1-7 is a mutant plasma membrane ATPase that is impaired in targeting to the cell surface at 37°C and is delivered instead to the endosomal/vacuolar pathway for degradation. We have proposed that Pma1-7 is a substrate for a Golgibased quality control mechanism. By contrast with wild-type Pma1, Pma1-7 is ubiquitinated. Ubiquitination and endosomal targetin
The American Society for Cell Biology.
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23. A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination
Temporal control of p27Kip1 (p27) degradation imposes periodicity in its activity during cell cycle progression and its accumulation during cell cycle exit. Degradation of p27 is initiated by phosphorylation of p27 at Thr-187, which marks the protein for ubiquitination by SCFSkp2 and subsequent proteolysis by the 26S proteasome. Here we show that the p27 ubi
The National Academy of Sciences.
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24. Hypoxia-inducible factor 1α protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations
Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that mediates cellular and systemic homeostatic responses to reduced O2 availability in mammals, including angiogenesis, erythropoiesis, and glycolysis. HIF-1 activity is controlled by the O2-regulated expression of the HIF-1α subunit. Under nonhypoxic conditions, HIF-1α protein is subject to ubi
The National Academy of Sciences.