Ku must load directly onto the chromosome end in order to mediate its telomeric functions. - Test2 - elhamkhani - TriplyDB

Ku must load directly onto the chromosome end in order to mediate its telomeric functions.

Ku must load directly onto the chromosome end in order to mediate its telomeric functions.

http://www.wikidata.org/entity/Q33996667

about

Finding the end: recruitment of telomerase to telomeres TRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeres Human LIGIV is synthetically lethal with the loss of Rad54B-dependent recombination and is required for certain chromosome fusion events induced by telomere dysfunction Competition between Heterochromatic Loci Allows the Abundance of the Silencing Protein, Sir4, to Regulate de novo Assembly of Heterochromatin.Mutually exclusive binding of telomerase RNA and DNA by Ku alters telomerase recruitment model.Regulation of Ku-DNA association by Yku70 C-terminal tail and SUMO modification The principal role of Ku in telomere length maintenance is promotion of Est1 association with telomeres Interplay between Ku and Replication Protein A in the Restriction of Exo1-mediated DNA Break End Resection Chromosome end protection by blunt-ended telomeres Functional characterisation of long intergenic non-coding RNAs through genetic interaction profiling in Saccharomyces cerevisiae.Ku Binding on Telomeres Occurs at Sites Distal from the Physical Chromosome Ends Cdc13 at a crossroads of telomerase action Biology of telomeres: lessons from budding yeast.Consider the workhorse: Nonhomologous end-joining in budding yeast.Acute exercise activates p38 MAPK and increases the expression of telomere-protective genes in cardiac muscle.Genome-wide studies of telomere biology in budding yeast Blunt-ended telomeres: an alternative ending to the replication and end protection stories.The Ku heterodimer and the metabolism of single-ended DNA double-strand breaks.Structural Insights into Yeast Telomerase Recruitment to Telomeres.ATF7 mediates TNF-α-induced telomere shortening.Ku DNA End-Binding Activity Promotes Repair Fidelity and Influences End-Processing During Nonhomologous End-Joining in Saccharomyces cerevisiae.Sgs1 and Sae2 promote telomere replication by limiting accumulation of ssDNA.

P2860

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P2860

Ku must load directly onto the chromosome end in order to mediate its telomeric functions.

http://www.wikidata.org/entity/Q33996667

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

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

Ku must load directly onto the ...... diate its telomeric functions.

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Ku must load directly onto the ...... diate its telomeric functions.

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Ku must load directly onto the ...... diate its telomeric functions.

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Ku must load directly onto the ...... diate its telomeric functions.

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P356

JOURNAL.PGEN.1002233

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Ku must load directly onto the ...... diate its telomeric functions.

@en

P2093

Albert Ribes-Zamora

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

Alison A Bertuch

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

Christopher L Williams

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

Christopher R Lopez

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

Sandra M Indiviglio

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

Svasti Haricharan

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

P2860

Shelterin-like proteins and Yku inhibit nucleolytic processing of Saccharomyces cerevisiae telomeres

Mammalian telomeres end in a large duplex loop

Interaction of human Ku70 with TRF2

PTOP interacts with POT1 and regulates its localization to telomeres

How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures

The human Rap1 protein complex and modulation of telomere length

Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing.

Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair

Conserved structure for single-stranded telomeric DNA recognition

The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA

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e1002233

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scholarly article

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10.1371/JOURNAL.PGEN.1002233

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8

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21852961

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3154960

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