Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4 - Wikidata - thesis-toulmin - TriplyDB

Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4

Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4

http://www.wikidata.org/entity/Q24644339

about

Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining A human XRCC4-XLF complex bridges DNA XRCC4's interaction with XLF is required for coding (but not signal) end joining BRCT domains: easy as one, two, three The structural basis for partitioning of the XRCC1/DNA ligase III- BRCT-mediated dimer complexes XRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break Repair Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions Structural Basis of DNA Ligase IV-Artemis Interaction in Nonhomologous End-Joining Structural Insights into the Role of Domain Flexibility in Human DNA Ligase IV Role of non-homologous end joining in V(D)J recombination A noncatalytic function of the ligation complex during nonhomologous end joining.Nonhomologous end joining: a good solution for bad ends Non-homologous end joining: emerging themes and unanswered questions.Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a time Structural dynamics in DNA damage signaling and repair Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.DNA Ligase IV regulates XRCC4 nuclear localization.XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair.Dual modes of interaction between XRCC4 and polynucleotide kinase/phosphatase: implications for nonhomologous end joining.DNA ligases as therapeutic targets XLF regulates filament architecture of the XRCC4·ligase IV complex.Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.Genetic polymorphisms of DNA double-strand break repair pathway genes and glioma susceptibility.Recognition and repair of chemically heterogeneous structures at DNA ends Yeast DNA ligase IV mutations reveal a nonhomologous end joining function of BRCT1 distinct from XRCC4/Lif1 binding.Associations of LIG4 and HSPB1 genetic polymorphisms with risk of radiation-induced lung injury in lung cancer patients treated with radiotherapy Yeast two-hybrid junk sequences contain selected linear motifs Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex.Genome-wide screens for sensitivity to ionizing radiation identify the fission yeast nonhomologous end joining factor Xrc4.The α2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection.Zinc-finger nuclease-mediated targeted insertion of reporter genes for quantitative imaging of gene expression in sea urchin embryos.PCR artifact in testing for homologous recombination in genomic editing in zebrafish.Structure-Based Virtual Ligand Screening on the XRCC4/DNA Ligase IV Interface.Lif1 SUMOylation and its role in non-homologous end-joining.DNA double strand break repair via non-homologous end-joining.The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response.DNA repair gene XRCC4 codon 247 polymorphism modified diffusely infiltrating astrocytoma risk and prognosis.An Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.DNA repair pathways in trypanosomatids: from DNA repair to drug resistance.Detection and repair of ionizing radiation-induced DNA double strand breaks: new developments in nonhomologous end joining.

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Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4

http://www.wikidata.org/entity/Q24644339

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and Functional Inte ...... oteins DNA Ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Molecular and Cellular Biology

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Structural and functional inte ...... oteins DNA ligase IV and XRCC4

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Bernard Salles

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Peï-Yu Wu

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

Philippe Frit

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

Sara N Andres

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

SriLakshmi Meesala

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Stéphanie Dauvillier

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Ying Huang

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P2860

DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes

The role of double-strand break repair — insights from human genetics

Crystal structure of an Xrcc4-DNA ligase IV complex

In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex

The BRCT domain is a phospho-protein binding domain

Cernunnos, a novel nonhomologous end-joining factor, is mutated in human immunodeficiency with microcephaly

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining

Ku recruits XLF to DNA double-strand breaks

Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells

Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV

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3163-3172

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scholarly article

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10.1128/MCB.01895-08

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11

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29

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JoAnn M. Sekiguchi

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2009-03-30T00:00:00Z

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19332554

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2682001

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