CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance. - Wikidata - wikimedia - TriplyDB

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

http://www.wikidata.org/entity/Q33636085

about

Structural and functional analysis of an OB-fold in human Ctc1 implicated in telomere maintenance and bone marrow syndromes.Dynamic DNA binding, junction recognition and G4 melting activity underlie the telomeric and genome-wide roles of human CST.STN1-POLA2 interaction provides a basis for primase-pol α stimulation by human STN1.Telomeres: Implications for Cancer Development.In medio stat virtus: unanticipated consequences of telomere dysequilibrium.The CST Complex Mediates End Protection at Double-Strand Breaks and Promotes PARP Inhibitor Sensitivity in BRCA1-Deficient Cells.53BP1-RIF1-shieldin counteracts DSB resection through CST- and Polα-dependent fill-in

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P2860

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

http://www.wikidata.org/entity/Q33636085

description

2017 nî lūn-bûn

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2017 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի փետրվարին հրատարակված գիտական հոդված

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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name

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@ast

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@en

type

label

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@ast

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@en

prefLabel

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@ast

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@en

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Nucleic Acids Research

P1476

CTC1-mediated C-strand fill-in is an essential step in telomere length maintenance.

@en

P2093

Carolyn M Price

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

Christopher Kasbek

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

Mary Chaiken

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

Shih-Jui Hsu

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

Xuyang Feng

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

P2860

PTOP interacts with POT1 and regulates its localization to telomeres

POT1 as a terminal transducer of TRF1 telomere length control

Human POT1 facilitates telomere elongation by telomerase

PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replication

RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway

Conserved telomere maintenance component 1 interacts with STN1 and maintains chromosome ends in higher eukaryotes

OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation

The human CST complex is a terminator of telomerase activity

Structure and conformational change of a replication protein A heterotrimer bound to ssDNA

Structure of the Human Telomeric Stn1-Ten1 Capping Complex

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4281-4293

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10.1093/NAR/GKX125

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8

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45

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2017-02-23T00:00:00Z

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28334750

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telomere length

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5416890

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