Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase - Wikidata - awgldk - TriplyDB

Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

http://www.wikidata.org/entity/Q27729722

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Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif Functional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteins The hDcp2 protein is a mammalian mRNA decapping enzyme Functional characterization of the mammalian mRNA decapping enzyme hDcp2 Structure of a Coenzyme A Pyrophosphatase from Deinococcus radiodurans: a Member of the Nudix Family Functional and Structural Characterization of DR_0079 from Deinococcus radiodurans , a Novel Nudix Hydrolase with a Preference for Cytosine (Deoxy)ribonucleoside 5′-Di- and Triphosphates †Structural and Dynamic Features of the MutT Protein in the Recognition of Nucleotides with the Mutagenic 8-Oxoguanine Base Structure of a Nudix hydrolase (MutT) in the Mg 2+ -bound state from Bartonella henselae , the bacterium responsible for cat scratch fever Divalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli Multiple Nudix family proteins possess mRNA decapping activity Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance.Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases.Cloning and characterization of a new member of the Nudix hydrolases from human and mouse Characterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifolius Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.Role of the essential yeast protein PSU1 in p6anscriptional enhancement by the ligand-dependent activation function AF-2 of nuclear receptors.Structure and substrate-binding mechanism of human Ap4A hydrolase.The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.Trypanosoma cruzi Needs a Signal Provided by Reactive Oxygen Species to Infect Macrophages The ytkD (mutTA) gene of Bacillus subtilis encodes a functional antimutator 8-Oxo-(dGTP/GTP)ase and is under dual control of sigma A and sigma F RNA polymerases 4-Oxalocrotonate tautomerase, a 41-kDa homohexamer: backbone and side-chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy.Significance of the conserved amino acid sequence for human MTH1 protein with antimutator activity.Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein.A comprehensive bioinformatics analysis of the Nudix superfamily in Arabidopsis thaliana.Cloning and expression of diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L.Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme.Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase.The Nudix hydrolases of Deinococcus radiodurans.Orf186 Represents a New Member of the Nudix Hydrolases, Active on Adenosine(5′)triphospho(5′)adenosine, ADP-ribose, and NADH

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P2860

Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

http://www.wikidata.org/entity/Q27729722

description

1995 nî lūn-bûn

@nan

1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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type

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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prefLabel

Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase

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A F Miller

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A G Gittis

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A S Mildvan

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C Abeygunawardana

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D J Weber

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J Lin

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M J Bessman

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14997-15005

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scholarly article

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10.1021/BI00046A006

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34

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1995-11-01T00:00:00Z

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7578113

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