The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability. - sprookjes - yvandenbroek - TriplyDB

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

http://www.wikidata.org/entity/Q36144884

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The role of RecQ helicases in non-homologous end-joining RECQL4 in genomic instability and aging The Tumor-Associated Variant RAD51 G151D Induces a Hyper-Recombination Phenotype RECQ helicase RECQL4 participates in non-homologous end joining and interacts with the Ku complex The intrinsically disordered amino-terminal region of human RecQL4: multiple DNA-binding domains confer annealing, strand exchange and G4 DNA binding.RECQL4 Promotes DNA End Resection in Repair of DNA Double-Strand Breaks.RECQL5 has unique strand annealing properties relative to the other human RecQ helicase proteins.Human RecQ helicases in DNA repair, recombination, and replication.Neisseria gonorrhoeae RecQ helicase HRDC domains are essential for efficient binding and unwinding of the pilE guanine quartet structure required for pilin antigenic variation The RECQL4 protein, deficient in Rothmund-Thomson syndrome is active on telomeric D-loops containing DNA metabolism blocking lesions Altered RECQ Helicase Expression in Sporadic Primary Colorectal Cancers.Hrq1, a homolog of the human RecQ4 helicase, acts catalytically and structurally to promote genome integrity.Yeast Hrq1 shares structural and functional homology with the disease-linked human RecQ4 helicase.RecQ helicase BLM regulates prostate cancer cell proliferation and apoptosis.Overexpression of RECQL4 is associated with poor prognosis in patients with gastric cancer

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The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

http://www.wikidata.org/entity/Q36144884

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@ast

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@en

type

label

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@ast

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@en

prefLabel

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@ast

The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@en

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Nucleic Acids Research

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The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.

@en

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Avik K Ghosh

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

Deborah L Croteau

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

Dharmendra Kumar Singh

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

Igor Shevelev

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

Mahesh Ramamoorthy

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

Marie L Rossi

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

Pavel Janscak

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

Tomasz Kulikowicz

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

Venkateswarlu Popuri

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

Vilhelm A Bohr

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

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Characterization of the human and mouse WRN 3'-->5' exonuclease

The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases

Colocalization, physical, and functional interaction between Werner and Bloom syndrome proteins

RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell cycle progression

Rif1 provides a new DNA-binding interface for the Bloom syndrome complex to maintain normal replication

Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases

The Bloom's syndrome gene product is a 3'-5' DNA helicase

Dual DNA unwinding activities of the Rothmund-Thomson syndrome protein, RECQ4

Interaction between the helicases genetically linked to Fanconi anemia group J and Bloom's syndrome

Recql5 and Blm RecQ DNA helicases have nonredundant roles in suppressing crossovers.

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6632-6648

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scholarly article

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10.1093/NAR/GKS349

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14

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40

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2012-04-28T00:00:00Z

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224868338

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22544709

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3413146

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