Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
about
Evolution and horizontal transfer of dUTPase-encoding genes in viruses and their hostsKeeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPasesStructure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.Flexible segments modulate co-folding of dUTPase and nucleocapsid proteinsStructure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPasesStructure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase fromArabidopsis thalianaThe Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase Is Essential for CatalysisMolecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomersCrystallization and crystal-packing studies ofChlorellavirus deoxyuridine triphosphataseDirect contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPasesAromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPaseCrystallization ofChlorelladeoxyuridine triphosphataseTying down the arm in Bacillus dUTPase: structure and mechanismStructure and enzymatic mechanism of a moonlighting dUTPasePhosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insightsThe human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial speciesKinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzymeRegulation of human dUTPase gene expression and p53-mediated transcriptional repression in response to oxaliplatin-induced DNA damageKinetic properties and inhibition of the dimeric dUTPase-dUDPase from Leishmania majorNLS copy-number variation governs efficiency of nuclear import--case study on dUTPasesCrystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.Insights into the gene expression profile of uncultivable hemotrophic Mycoplasma suis during acute infection, obtained using proteome analysis.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.The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase.HERV-K(OLD): ancestor sequences of the human endogenous retrovirus family HERV-K(HML-2).Chlorella virus-encoded deoxyuridine triphosphatases exhibit different temperature optima.Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.AutoMatch: target-binding protein design and enzyme design by automatic pinpointing potential active sites in available protein scaffolds.Human herpesviruses-encoded dUTPases: a family of proteins that modulate dendritic cell function and innate immunityIncorporation of dUTP does not mediate mutation of A:T base pairs in Ig genes in vivoCalcium inhibition of ribonuclease H1 two-metal ion catalysisCatalytic and structural role of the metal ion in dUTP pyrophosphataseNucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination.A new crucial protein interaction element that targets the adenovirus E4-ORF1 oncoprotein to membrane vesiclesStructural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.Functionally distinct monomers and trimers produced by a viral oncoprotein.Cell polarity proteins: common targets for tumorigenic human viruses.Principles of macromolecular X-ray crystallography.Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria.
P2860
Q24517483-54165A1F-59CA-4E59-8A3D-91D93D20C6BDQ24646369-956E127A-5223-47B5-A1B4-435EBB85A92FQ27334123-BC5EC2A7-62F6-4564-BC13-62EA41CEDBBEQ27640764-EA246483-6DF2-4B60-A9AF-5725D0BCD3FAQ27641295-203F2C5A-FE17-44C2-B8D9-C32A33567193Q27644214-A7A761F9-084B-4EBA-A6B2-D7915717B7C7Q27645680-62E6C1CB-96DF-464A-9E9A-BA7C60FA7E34Q27646514-544775DC-BCA3-485B-A315-1534914C09E3Q27654224-21B248F8-2F87-49A1-99DA-117C1D485EC5Q27657942-AD2D0926-338B-4DB1-8F8B-79280FA7B075Q27661770-951C5CD2-9BAE-484E-A363-4E9B5E3EDE5EQ27663080-8027196B-B27C-4E36-BE10-1B5A277DA065Q27675961-5436D2A4-47A9-4875-8B3A-40B7169033A7Q27685288-F3C9214A-E9C4-4F3E-855E-E7D5398BF984Q27687839-13BC77C4-04D2-482B-B147-4A344C94F8E0Q27687877-2947DD42-FE03-42A4-9645-3AD87201F2BAQ28244129-45BAD214-814B-4A44-8065-4A23BE645D5FQ28248221-B67BDF68-C70F-46E4-A49E-CF7E36A094C5Q28301157-3EB5C464-0960-4A4D-967B-17385C00E174Q28367425-0D7BAE55-814F-42DF-ABB0-855AEC6941A4Q28587984-BE401C13-FCB7-4F67-84FB-F92F8530ECC3Q30176729-FAA1FA81-EB17-400E-8D71-ACC06B733859Q30506460-A90C5470-4303-43A8-B5B5-C90516BFD634Q30569983-428D0610-4AD1-4773-8E18-914819518A26Q30882604-CBF418D2-E2AF-4638-A7BD-A44E47090206Q33844963-91B37A0E-9FB0-4F91-AD2C-EEF9E18CE23AQ33908710-436AFB18-2089-4A62-BC14-CD73B35878B0Q33921147-115B5FC8-ED6D-4ECD-9CB8-D4E971ABD569Q34121578-C29FBE32-70E0-4361-9A83-86698808E0D2Q34248754-218F3DD7-8268-4EFD-BA26-4C7763DA8DA2Q34401362-FC22DF83-5A6E-4B19-BDBB-5F226E07D710Q34402463-05AAFA52-84C6-4514-9981-DDDED3807929Q35021854-10CB6DA1-F0CB-472D-9962-DFE462D6969BQ35197919-6509D2A0-7A4E-4B4F-B456-798EFD5226D9Q35857357-C5A12BAB-B36B-417B-8BC7-4DBD6E74C220Q35868354-1C356772-4739-418E-AAEA-374F1B2C10D2Q36318620-541647B8-D955-4DAE-8FEA-0C17C52520B8Q36409895-DBBA1A46-9627-49F0-A063-FF4B313EF95BQ37144775-B8594A2C-BEEC-46FB-AAFA-21C6DA2E5D64Q37148803-0E7CB800-3417-4C46-8C84-5B23D7FD6768
P2860
Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@ast
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@en
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@nl
type
label
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@ast
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@en
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@nl
prefLabel
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@ast
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@en
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@nl
P3181
P1433
P1476
Human dUTP pyrophosphatase: ur ...... med by three separate subunits
@en
P2093
P304
P3181
P356
10.1016/S0969-2126(96)00114-1
P407
P577
1996-09-01T00:00:00Z