Human telomeric proteins occupy selective interstitial sites. - Test2 - elhamkhani - TriplyDB

Human telomeric proteins occupy selective interstitial sites.

Human telomeric proteins occupy selective interstitial sites.

http://www.wikidata.org/entity/Q33851199

about

TRF2 controls telomeric nucleosome organization in a cell cycle phase-dependent manner Telomere- and Telomerase-Associated Proteins and Their Functions in the Plant Cell Telomeres-structure, function, and regulation TRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeres TRF2 and lamin A/C interact to facilitate the functional organization of chromosome ends Malaria parasites possess a telomere repeat-binding protein that shares ancestry with transcription factor IIIA ZBTB48 is both a vertebrate telomere-binding protein and a transcriptional activator TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres.Complementary Activities of TELOMERE REPEAT BINDING Proteins and Polycomb Group Complexes in Transcriptional Regulation of Target Genes.SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage.Subtelomeric CTCF and cohesin binding site organization using improved subtelomere assemblies and a novel annotation pipeline.PRL-3 promotes telomere deprotection and chromosomal instability.Nontelomeric role for Rap1 in regulating metabolism and protecting against obesity.Mitochondrial localization of telomeric protein TIN2 links telomere regulation to metabolic control TRF2 inhibits a cell-extrinsic pathway through which natural killer cells eliminate cancer cells.Nucleolar organization, ribosomal DNA array stability, and acrocentric chromosome integrity are linked to telomere function.ERK1/2/MAPK pathway-dependent regulation of the telomeric factor TRF2.Unraveling secrets of telomeres: one molecule at a time.TeloPIN: a database of telomeric proteins interaction network in mammalian cells The human TTAGGG repeat factors 1 and 2 bind to a subset of interstitial telomeric sequences and satellite repeats.The OB-fold domain 1 of human POT1 recognizes both telomeric and non-telomeric DNA motifs Maintaining the end: roles of telomere proteins in end-protection, telomere replication and length regulation Subtelomere-binding protein Tbf1 and telomere-binding protein Rap1 collaborate to inhibit localization of the Mre11 complex to DNA ends in budding yeast.Rap1 is indispensable for TRF2 function in etoposide-induced DNA damage response in gastric cancer cell line.The Daxx/Atrx Complex Protects Tandem Repetitive Elements during DNA Hypomethylation by Promoting H3K9 Trimethylation.Genome-wide analysis of in vivo TRF1 binding to chromatin restricts its location exclusively to telomeric repeats.Human Rap1 interacts directly with telomeric DNA and regulates TRF2 localization at the telomere The trithorax group protein Ash2l is essential for pluripotency and maintaining open chromatin in embryonic stem cells.A higher-order entity formed by the flexible assembly of RAP1 with TRF2.A TRF1-controlled common fragile site containing interstitial telomeric sequences.TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions.Rap1 relocalization contributes to the chromatin-mediated gene expression profile and pace of cell senescence Acacetin and chrysin, two polyphenolic compounds, alleviate telomeric position effect in human cells.Silencing subtelomeric VSGs by Trypanosoma brucei RAP1 at the insect stage involves chromatin structure changes The molecular genetics of the telomere biology disorders.A genetic interaction between RAP1 and telomerase reveals an unanticipated role for RAP1 in telomere maintenance.Telomeric impact of conventional chemotherapy.Transcriptional outcome of telomere signalling.TRF2-mediated stabilization of hREST4 is critical for the differentiation and maintenance of neural progenitors.Structural and functional association of androgen receptor with telomeres in prostate cancer cells.

P2860

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P2860

Human telomeric proteins occupy selective interstitial sites.

http://www.wikidata.org/entity/Q33851199

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Human telomeric proteins occupy selective interstitial sites.

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Human telomeric proteins occupy selective interstitial sites.

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type

label

Human telomeric proteins occupy selective interstitial sites.

@ast

Human telomeric proteins occupy selective interstitial sites.

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prefLabel

Human telomeric proteins occupy selective interstitial sites.

@ast

Human telomeric proteins occupy selective interstitial sites.

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Human telomeric proteins occupy selective interstitial sites.

@en

P2093

Dong Yang

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

Hyeung Kim

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

Quanyuan He

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

Rui Chen

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

Yuanyan Xiong

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

Yumei Li

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

Zhou Songyang

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

P2860

TIN2, a new regulator of telomere length in human cells

Identification of human Rap1: implications for telomere evolution

TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase

The POT1-TPP1 telomere complex is a telomerase processivity factor

A mammalian factor that binds telomeric TTAGGG repeats in vitro

PTOP interacts with POT1 and regulates its localization to telomeres

Rap1 affects the length and heterogeneity of human telomeres

POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex

A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly

A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2

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1013-1027

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scholarly article

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10.1038/CR.2011.39

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7

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21

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21423278

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3193500

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