FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner. - Test2 - elhamkhani - TriplyDB

FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.

FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.

http://www.wikidata.org/entity/Q30863349

about

Structural and mechanistic insight into DNA unwinding by Deinococcus radiodurans UvrD The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway Structural Mechanisms of Hexameric Helicase Loading, Assembly, and Unwinding Close encounters for the first time: Helicase interactions with DNA damage Mechanistic and biological aspects of helicase action on damaged DNA.Distinct roles of RECQ1 in the maintenance of genomic stability.Interactive Roles of DNA Helicases and Translocases with the Single-Stranded DNA Binding Protein RPA in Nucleic Acid Metabolism.Modulation of UvrD helicase activity by covalent DNA-protein cross-links.Fanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes.Molecular and cellular functions of the FANCJ DNA helicase defective in cancer and in Fanconi anemia Impact of age-associated cyclopurine lesions on DNA repair helicases.Bone marrow cell transcripts from Fanconi anaemia patients reveal in vivo alterations in mitochondrial, redox and DNA repair pathways.High-affinity DNA-binding domains of replication protein A (RPA) direct SMARCAL1-dependent replication fork remodeling RECQ1 interacts with FEN-1 and promotes binding of FEN-1 to telomeric chromatin.DNA helicases involved in DNA repair and their roles in cancer DNA repair and replication fork helicases are differentially affected by alkyl phosphotriester lesion.DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster.DNA secondary structure of the released strand stimulates WRN helicase action on forked duplexes without coordinate action of WRN exonuclease The human RecQ helicases BLM and RECQL4 cooperate to preserve genome stability.RECQ1 plays a distinct role in cellular response to oxidative DNA damage.Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB.Translocation and stability of replicative DNA helicases upon encountering DNA-protein cross-links.FANCJ at the FORK.The RECQL4 protein, deficient in Rothmund-Thomson syndrome is active on telomeric D-loops containing DNA metabolism blocking lesions Biochemical Characterization of the Human Mitochondrial Replicative Twinkle Helicase: SUBSTRATE SPECIFICITY, DNA BRANCH MIGRATION, AND ABILITY TO OVERCOME BLOCKADES TO DNA UNWINDING.Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions Probing Genome Maintenance Functions of human RECQ1.FANCJ protein is important for the stability of FANCD2/FANCI proteins and protects them from proteasome and caspase-3 dependent degradation.Fanconi anemia (FA) and crosslinker sensitivity: Re-appraising the origins of FA definition.Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase RecQ and Fe-S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions.Long-range resection of DNA DSBs by EXO1 or DNA2

P2860

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P2860

FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.

http://www.wikidata.org/entity/Q30863349

description

2009 nî lūn-bûn

@nan

2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մայիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年学术文章

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2009年学术文章

@zh-cn

2009年学术文章

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2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

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name

FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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type

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FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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prefLabel

FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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FANCJ helicase uniquely senses ...... e in a strand-specific manner.

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P1433

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P356

JBC.M109.012229

P1433

Journal of Biological Chemistry

P1476

FANCJ helicase uniquely senses ...... e in a strand-specific manner.

@en

P2093

Aaron C Mason

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

Avvaru N Suhasini

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

Joshua A Sommers

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

Marc S Wold

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

Oleg N Voloshin

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

R Daniel Camerini-Otero

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

Robert M Brosh

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

P2860

Functional and physical interaction between WRN helicase and human replication protein A

Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork

Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer

Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints

Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A

The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations

The DNA repair helicases XPD and FancJ have essential iron-sulfur domains.

Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism

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18458-18470

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scholarly article

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10.1074/JBC.M109.012229

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P407

P433

27

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P478

284

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2009-05-05T00:00:00Z

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19419957

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2709400

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