A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae
about
Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolitesStructural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domainsCrystal Structures of Two Coronavirus ADP-Ribose-1''-Monophosphatases and Their Complexes with ADP-Ribose: a Systematic Structural Analysis of the Viral ADRP DomainCrystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved propertyThe SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-QuadruplexesHydrolase regulates NAD+ metabolites and modulates cellular redox.Genomics-guided analysis of NAD recycling yields functional elucidation of COG1058 as a new family of pyrophosphatases.Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domainsMolecular Insights into Poly(ADP-ribose) Recognition and Processing.The nsp3 macrodomain promotes virulence in mice with coronavirus-induced encephalitisRNA damage in biological conflicts and the diversity of responding RNA repair systemsExpression, purification and crystallization of the SARS-CoV macro domain.Proteome-scale analysis of biochemical activity.Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.Viral Macro Domains Reverse Protein ADP-Ribosylation.ADP-ribose-1"-monophosphatase: a conserved coronavirus enzyme that is dispensable for viral replication in tissue culture.A genetic screen for high copy number suppressors of the synthetic lethality between elg1Δ and srs2Δ in yeast.Web-Beagle: a web server for the alignment of RNA secondary structures.Nudix hydrolases degrade protein-conjugated ADP-ribose.We are writing to express our concerns regarding the recently published article by Kumaran et al.Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis.Specificity of reversible ADP-ribosylation and regulation of cellular processes.Preparation of potential cell-permeant nucleoside-2',3'-cyclic phosphate precursors.Evolution of Eukaryotic Chromatin Proteins and Transcription Factors
P2860
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P2860
A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae
description
2005 nî lūn-bûn
@nan
2005 թուականին հրատարակուած գիտական յօդուած
@hyw
2005 թվականին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@ast
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@en
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@nl
type
label
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@ast
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@en
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@nl
prefLabel
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@ast
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@en
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@nl
P2093
P2860
P3181
P356
P1476
A highly specific phosphatase ...... ng in Saccharomyces cerevisiae
@en
P2093
Eric M Phizicky
Neil P Shull
Sherry L Spinelli
P2860
P304
P3181
P356
10.1093/NAR/GKI211
P407
P577
2005-01-01T00:00:00Z