Ubiquitin Conjugating Enzyme
Mostrando 1-12 de 169 artigos, teses e dissertações.
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1. O gene UBE2A (Ubiquitin conjugating enzyme 2 A) e a deficiência mental: triagem de mutações e estudos funcionais / UBE2A (Ubiquitin conjugating enzyme 2 A) gene and mental retardation: search for mutations and functional studies
Em trabalho anterior, identificamos a mutação c.382C8594;T no gene UBE2A, localizado em Xq24 e codificador de enzima conjugadora de ubiquitina, como causa de nova síndrome de deficiência mental (DM) de herança ligada ao cromossomo X. Foi a primeira descrição de mutação nesse gene e a primeira associação de mutação em gene que codifica conjugase
Publicado em: 2010
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2. 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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3. 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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4. 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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5. Characterization of constitutive and putative differentially expressed mRNAs by means of expressed sequence tags, differential display reverse transcriptase-PCR and randomly amplified polymorphic DNA-PCR from the sand fly vector Lutzomyia longipalpis
Molecular studies of insect disease vectors are of paramount importance for understanding parasite-vector relationship. Advances in this area have led to important findings regarding changes in vectors' physiology upon blood feeding and parasite infection. Mechanisms for interfering with the vectorial capacity of insects responsible for the transmission of d
Memórias do Instituto Oswaldo Cruz. Publicado em: 2001-01
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6. A ubiquitin conjugating enzyme encoded by African swine fever virus.
The post-translational modification of proteins by covalent attachment of ubiquitin occurs in all eukaryotes by a multi-step process. A family of E2 or ubiquitin conjugating (UBC) enzymes catalyse one step of this process and these have been implicated in several diverse regulatory functions. We report here the sequence of a gene encoded by African swine fev
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7. Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP).
The E6 protein of the high-risk human papillomaviruses inactivates the tumor suppressor protein p53 by stimulating its ubiquitinylation and subsequent degradation. Ubiquitinylation is a multistep process involving a ubiquitin-activating enzyme, one of many distinct ubiquitin-conjugating enzymes, and in certain cases, a ubiquitin ligase. In human papillomavir
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8. Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IκBα
The NF-κB/Rel proteins are sequestered in the cytoplasm in association with IκBα. In response to external signals, IκBα is phosphorylated, multi-ubiquitinated, and degraded by proteasomes, thereby releasing NF-κB/Rel proteins to migrate to the nucleus. We have cloned a mouse ubiquitin-conjugating enzyme (mE2), which associates with IκBα. mE2 is homol
The National Academy of Sciences of the USA.
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9. Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme.
The RAD6 gene of Saccharomyces cerevisiae encodes a 20 kd ubiquitin conjugating (E2) enzyme that is required for DNA repair, DNA damage-induced mutagenesis, and sporulation. Here, we demonstrate a novel activity of RAD6 protein--its ability to mediate protein degradation dependent on the N-end-recognizing ubiquitin protein ligase (E3). In reaction mixtures c
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10. Identification of a Gene Product Induced by Hard-Surface Contact of Colletotrichum gloeosporioides Conidia as a Ubiquitin-Conjugating Enzyme by Yeast Complementation
The germinating conidia of many phytopathogenic fungi on hosts must differentiate into an infection structure called the appressorium in order to penetrate their hosts. Chemical signals, such as the host’s surface wax or fruit ripening hormone, ethylene, trigger germination and appressorium formation of the avocado pathogen Colletotrichum gloeosporioides o
American Society for Microbiology.
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11. Two Ubiquitin-Conjugating Enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, Have Distinct Functions for Ubiquitination of Mitotic Cyclin
Cell cycle events are regulated by sequential activation and inactivation of Cdk kinases. Mitotic exit is accomplished by the inactivation of mitotic Cdk kinase, which is mainly achieved by degradation of cyclins. The ubiquitin-proteasome system is involved in this process, requiring APC/C (anaphase-promoting complex/cyclosome) as a ubiquitin ligase. In Xeno
American Society for Microbiology.
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12. Characterization of novel yeast RAD6 (UBC2) ubiquitin-conjugating enzyme mutants constructed by charge-to-alanine scanning mutagenesis.
Ubiquitination of intracellular proteins by the yeast RAD6 (UBC2) ubiquitin-conjugating (E2) enzyme is required for cellular processes as diverse as DNA repair, selective proteolysis, and normal growth. For most RAD6-dependent functions, the relevant in vivo targets, as well as the mechanisms and cofactors that govern RAD6 substrate selectivity, are unknown.