The evolution of function within the Nudix homology clan. - Test2 - elhamkhani - TriplyDB

The evolution of function within the Nudix homology clan.

The evolution of function within the Nudix homology clan.

http://www.wikidata.org/entity/Q33559060

about

Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H Pyrophosphohydrolase Activity.Extreme Deviations from Expected Evolutionary Rates in Archaeal Protein Families.Vive la radiorésistance!: converging research in radiobiology and biogerontology to enhance human radioresistance for deep space exploration and colonization.Structural and biochemical characterization of Siw14: a protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates.

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P2860

The evolution of function within the Nudix homology clan.

http://www.wikidata.org/entity/Q33559060

description

2016 nî lūn-bûn

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2016 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

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2016年論文

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2016年论文

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name

The evolution of function within the Nudix homology clan.

@ast

The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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type

label

The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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prefLabel

The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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The evolution of function within the Nudix homology clan.

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Annsea Park

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Anting Xu

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Jack F Kirsch

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John R Srouji

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P2860

The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein

Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif

Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates

Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family

Gene ontology: tool for the unification of biology

Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP

Cloning, characterisation and crystallisation of a diadenosine 5',5"'-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans

The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms

The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A resolution reveals its catalytic mechanism in isoprenoid biosynthesis

Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases

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5

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Steven E. Brenner

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