Catalytic and structural role of the metal ion in dUTP pyrophosphatase
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Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPasesFlexible segments modulate co-folding of dUTPase and nucleocapsid proteinsThe Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase Is Essential for CatalysisDirect contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPasesThe Crystal Structure of the Leishmania major Deoxyuridine Triphosphate Nucleotidohydrolase in Complex with Nucleotide Analogues, dUMP, and DeoxyuridineOn the catalytic mechanism of dimeric dUTPasesDeinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTPNLS copy-number variation governs efficiency of nuclear import--case study on dUTPasesThe dUTPase enzyme is essential in Mycobacterium smegmatisCalpain-catalyzed proteolysis of human dUTPase specifically removes the nuclear localization signal peptide.Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.Preventive DNA repair by sanitizing the cellular (deoxy)nucleoside triphosphate pool.Dynamics of re-constitution of the human nuclear proteome after cell division is regulated by NLS-adjacent phosphorylation.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.Genome sequence of Perigonia lusca single nucleopolyhedrovirus: insights into the evolution of a nucleotide metabolism enzyme in the family Baculoviridae.Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control.Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme.Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.dUTPase expression correlates with cell division potential in Drosophila melanogaster.Potential steps in the evolution of a fused trimeric all-β dUTPase involve a catalytically competent fused dimeric intermediate.
P2860
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P2860
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@ast
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@en
type
label
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@ast
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@en
prefLabel
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@ast
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@en
P2093
P2860
P356
P1476
Catalytic and structural role of the metal ion in dUTP pyrophosphatase
@en
P2093
Angela Bekesi
Beata G Vertessy
Devkumar Mustafi
Marvin W Makinen
P2860
P304
P356
10.1073/PNAS.1031504100
P407
P577
2003-04-29T00:00:00Z