Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. - Wikidata - awgldk - TriplyDB

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

http://www.wikidata.org/entity/Q35973264

about

Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species Human single-stranded DNA binding proteins are essential for maintaining genomic stability Functional wiring of the yeast kinome revealed by global analysis of genetic network motifs DNA end resection: many nucleases make light work The RNA Splicing Response to DNA Damage The Sum1/Ndt80 transcriptional switch and commitment to meiosis in Saccharomyces cerevisiae Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor IIIC Dissecting phosphorylation networks: lessons learned from yeast At short telomeres Tel1 directs early replication and phosphorylates Rif1.SPO24 is a transcriptionally dynamic, small ORF-encoding locus required for efficient sporulation in Saccharomyces cerevisiae.The histone H3K36 demethylase Rph1/KDM4 regulates the expression of the photoreactivation gene PHR1 Rad53-Mediated Regulation of Rrm3 and Pif1 DNA Helicases Contributes to Prevention of Aberrant Fork Transitions under Replication Stress.Separate roles for the DNA damage checkpoint protein kinases in stabilizing DNA replication forks.Phosphorylation of Yeast Pah1 Phosphatidate Phosphatase by Casein Kinase II Regulates Its Function in Lipid Metabolism Pseudosubstrate inhibition of the anaphase-promoting complex by Acm1: regulation by proteolysis and Cdc28 phosphorylation.Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes.Coupling of septins to the axial landmark by Bud4 in budding yeast Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p.The protein factor-arrest 11 (Far11) is essential for the toxicity of human caspase-10 in yeast and participates in the regulation of autophagy and the DNA damage signaling.Cdk phosphorylation of a nucleoporin controls localization of active genes through the cell cycle.Regulation of clathrin-mediated endocytosis by dynamic ubiquitination and deubiquitination.Septin-Associated Protein Kinases in the Yeast Saccharomyces cerevisiae SUMO-mediated regulation of DNA damage repair and responses PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae Assembly of Slx4 signaling complexes behind DNA replication forks Mechanisms and Consequences of Double-Strand DNA Break Formation in Chromatin ATR: an essential regulator of genome integrity Cordon Bleu serves as a platform at the basal region of microvilli, where it regulates microvillar length through its WH2 domains.Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site.Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum--a representative of the third domain of life.Predicting protein post-translational modifications using meta-analysis of proteome scale data sets.A truncated DNA-damage-signaling response is activated after DSB formation in the G1 phase of Saccharomyces cerevisiae.A proteome-wide analysis of kinase-substrate network in the DNA damage response.Cdk1-dependent regulation of the Mre11 complex couples DNA repair pathways to cell cycle progression Systematic analysis of essential genes reveals important regulators of G protein signaling.Elucidating the CXCL12/CXCR4 signaling network in chronic lymphocytic leukemia through phosphoproteomics analysis Preserving Yeast Genetic Heritage through DNA Damage Checkpoint Regulation and Telomere Maintenance.A strategy for interaction site prediction between phospho-binding modules and their partners identified from proteomic data

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P2860

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

http://www.wikidata.org/entity/Q35973264

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@ast

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@en

type

label

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@ast

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@en

prefLabel

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@ast

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@en

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PNAS.0701622104

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.

@en

P2093

Claudio P Albuquerque

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Huilin Zhou

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Marcus B Smolka

http://www.w3.org/2001/XMLSchema#string

Sheng-hong Chen

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P2860

Large-scale characterization of HeLa cell nuclear phosphoproteins

Global analysis of protein expression in yeast

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

A role for Saccharomyces cerevisiae histone H2A in DNA repair.

Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage.

Control of ribonucleotide reductase localization through an anchoring mechanism involving Wtm1.

The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1.

Proteomic analysis of nucleoporin interacting proteins.

Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways

Genetic network interactions among replication, repair and nuclear pore deficiencies in yeast.

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