Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance - Wikidata - awgldk - TriplyDB

Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance

Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance

http://www.wikidata.org/entity/Q30373537

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Human HLTF mediates postreplication repair by its HIRAN domain-dependent replication fork remodelling.Identification of a Substrate Recognition Domain in the Replication Stress Response Protein Zinc Finger Ran-binding Domain-containing Protein 3 (ZRANB3).HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.SMARCAL1 maintains telomere integrity during DNA replication.HIV-1 Vpr degrades the HLTF DNA translocase in T cells and macrophages.Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins.The helicase-like transcription factor (HLTF) in cancer: loss of function or oncomorphic conversion of a tumor suppressor?Replication fork regression and its regulation.SMARCAL1 and telomeres: Replicating the troublesome ends Differential expression profile analysis of DNA damage repair genes in CD133+/CD133- colorectal cancer cells.The Tyrosyl-DNA Phosphodiesterase 1β (Tdp1β) Gene Discloses an Early Response to Abiotic Stresses.Replication Fork Reversal: Players and Guardians.Mechanisms of bacterial DNA replication restart.HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase.Restoration of Replication Fork Stability in BRCA1- and BRCA2-Deficient Cells by Inactivation of SNF2-Family Fork Remodelers.Functions of SMARCAL1, ZRANB3, and HLTF in maintaining genome stability.Structural basis for the molecular interactions in DNA damage tolerances.AtRAD5A is a DNA translocase harboring a HIRAN domain which confers binding to branched DNA structures and is required for DNA repair in vivo.Rad5, HLTF, and SHPRH: A Fresh View of an Old Story The HIRAN domain of helicase-like transcription factor positions the DNA translocase motor to drive efficient DNA fork regression Ubiquitylation at the Fork: Making and Breaking Chains to Complete DNA Replication

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Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance

http://www.wikidata.org/entity/Q30373537

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2015 nî lūn-bûn

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2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Structure of a Novel DNA-bindi ...... cation in DNA Damage Tolerance

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Structure of a Novel DNA-bindi ...... cation in DNA Damage Tolerance

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Structure of a Novel DNA-bindi ...... cation in DNA Damage Tolerance

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JBC.M115.643643

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Journal of Biological Chemistry

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Structure of a Novel DNA-bindi ...... cation in DNA Damage Tolerance

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Asami Hishiki

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Mamoru Sato

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Toshiyuki Shimizu

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

Yuzu Ikegaya

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

P2860

Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen

Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic integrity after replication stress

The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and participates in cellular response to replication stress

ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response

Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks

Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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10.1074/JBC.M115.643643

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Hiroshi Hashimoto

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2015-04-09T00:00:00Z

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25858588

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