Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
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The metagenomic telescopeKeeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPasesdUTPase: the frequently overlooked enzyme encoded by many retrovirusesThe Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase Is Essential for CatalysisStructure and enzymatic mechanism of a moonlighting dUTPasePhosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insightsDeinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTPKinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzymeNLS copy-number variation governs efficiency of nuclear import--case study on dUTPasesIdentification of diverse full-length endogenous betaretroviruses in megabats and microbatsX-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solutionCatalytic mechanism of α-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.Evolution of the Kdo2-lipid A biosynthesis in bacteriaDifferential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination.In Vitro Analysis of Predicted DNA-Binding Sites for the Stl Repressor of the Staphylococcus aureus SaPIBov1 Pathogenicity Island.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.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.A Hidden Active Site in the Potential Drug Target Mycobacterium tuberculosis dUTPase Is Accessible through Small Amplitude Protein Conformational Changes.Drosophila proteins involved in metabolism of uracil-DNA possess different types of nuclear localization signals.Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control.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.dUTPase expression correlates with cell division potential in Drosophila melanogaster.The Stl repressor from Staphylococcus aureus is an efficient inhibitor of the eukaryotic fruitfly dUTPase.
P2860
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P2860
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
description
2007 nî lūn-bûn
@nan
2007 թուականին հրատարակուած գիտական յօդուած
@hyw
2007 թվականին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@ast
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@en
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@nl
type
label
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@ast
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@en
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@nl
prefLabel
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@ast
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@en
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@nl
P2093
P2860
P50
P3181
P356
P1476
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins
@en
P2093
Beáta G Vértessy
Emese Kónya
Eva Klement
Helena Zábranská
Iva Pichová
Katalin F Medzihradszky
Michalea Rumlová
Mónika Fuxreiter
Veronika Németh-Pongrácz
P2860
P304
P3181
P356
10.1093/NAR/GKL1074
P407
P577
2006-12-14T00:00:00Z