Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase - Wikidata - awgldk - TriplyDB

Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase

Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase

http://www.wikidata.org/entity/Q27648296

about

The metagenomic telescope Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases The Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase Is Essential for Catalysis Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase Tying down the arm in Bacillus dUTPase: structure and mechanism Structure and enzymatic mechanism of a moonlighting dUTPase Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insights Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme Regulation of human dUTPase gene expression and p53-mediated transcriptional repression in response to oxaliplatin-induced DNA damage NLS copy-number variation governs efficiency of nuclear import--case study on dUTPases The dUTPase enzyme is essential in Mycobacterium smegmatis Catalytic mechanism of α-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.Calpain-catalyzed proteolysis of human dUTPase specifically removes the nuclear localization signal peptide.Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination.Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria.Preventive DNA repair by sanitizing the cellular (deoxy)nucleoside triphosphate pool.Association of RNA with the uracil-DNA-degrading factor has major conformational effects and is potentially involved in protein folding.Crystallization and preliminary crystallographic analysis of dUTPase from the φ11 helper phage of Staphylococcus aureus.Cellular response to efficient dUTPase RNAi silencing in stable HeLa cell lines perturbs expression levels of genes involved in thymidylate metabolism.Drosophila proteins involved in metabolism of uracil-DNA possess different types of nuclear localization signals.Trading in cooperativity for specificity to maintain uracil-free DNA.Physiological truncation and domain organization of a novel uracil-DNA-degrading factor.The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner.The Stl repressor from Staphylococcus aureus is an efficient inhibitor of the eukaryotic fruitfly dUTPase.Evolutionary and mechanistic insights into substrate and product accommodation of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum.Potential steps in the evolution of a fused trimeric all-β dUTPase involve a catalytically competent fused dimeric intermediate.Structural model of human dUTPase in complex with a novel proteinaceous inhibitor.Cysteine residues contribute to the dimerization and enzymatic activity of human nuclear dUTP nucleotidohydrolase (nDut)

P2860

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P2860

Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase

http://www.wikidata.org/entity/Q27648296

description

2007 nî lūn-bûn

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2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年论文

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Balázs Varga

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Beáta G Vértessy

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Eva Hunyadi-Gulyás

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Eva Klement

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Ferenc Tölgyesi

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4783-8

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scholarly article

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2392534

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