Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation. - Wikidata - wikimedia - TriplyDB

Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.

Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.

http://www.wikidata.org/entity/Q37084017

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Structure and function of the telomeric CST complex PP2A and Aurora differentially modify Cdc13 to promote telomerase release from telomeres at G2/M phase.Quantitative proteomic discovery of dynamic epigenome changes that control human cytomegalovirus (HCMV) infection High resolution is not a strict requirement for characterization and quantification of histone post-translational modifications.Identification of nuclear hormone receptor pathways causing insulin resistance by transcriptional and epigenomic analysis.Novel connections between DNA replication, telomere homeostasis, and the DNA damage response revealed by a genome-wide screen for TEL1/ATM interactions in Saccharomyces cerevisiae.Quantitative dynamics of the link between cellular metabolism and histone acetylation.DNA repair at telomeres: keeping the ends intact.A quantitative atlas of histone modification signatures from human cancer cells Cdc13 at a crossroads of telomerase action Regulation of telomere metabolism by the RNA processing protein Xrn1.Multiple Levels of Control Determine How E4bp4/Nfil3 Regulates NK Cell Development.The mechanisms of K. lactis Cdc13 in telomere DNA-binding and telomerase regulation.

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Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.

http://www.wikidata.org/entity/Q37084017

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 13 December 2012

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Novel phosphorylation sites in ...... or telomere length regulation.

@en

Novel phosphorylation sites in ...... or telomere length regulation.

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type

label

Novel phosphorylation sites in ...... or telomere length regulation.

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Novel phosphorylation sites in ...... or telomere length regulation.

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prefLabel

Novel phosphorylation sites in ...... or telomere length regulation.

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Novel phosphorylation sites in ...... or telomere length regulation.

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Journal of Proteome Research

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Novel phosphorylation sites in ...... for telomere length regulation

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Benjamin A Garcia

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David H Perlman

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

Virginia A Zakian

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

Yun Wu

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

P2860

Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.

Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

Cdc13 N-Terminal Dimerization, DNA Binding, and Telomere Length Regulation

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α

Specific association of human telomerase activity with immortal cells and cancer

Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance.

A mutant with a defect in telomere elongation leads to senescence in yeast.

The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein

Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional EST genes.

Sir proteins, Rif proteins, and Cdc13p bind Saccharomyces telomeres in vivo.

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316-327

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scholarly article

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10.1021/PR300408V

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1

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12

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Peter A. DiMaggio

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2012-12-13T00:00:00Z

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233771367

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23181431

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phosphorylation

telomere length

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3739059

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