Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
about
Functional significance of the interaction with Ku in DNA double-strand break recognition of XLFStructural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joiningA human XRCC4-XLF complex bridges DNAXRCC4's interaction with XLF is required for coding (but not signal) end joiningDNA-PK: a dynamic enzyme in a versatile DSB repair pathwayXRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break RepairNon-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactionsNonhomologous end joining: a good solution for bad endsA fine-scale dissection of the DNA double-strand break repair machinery and its implications for breast cancer therapy.Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joiningThe C-terminus of Nej1 is critical for nuclear localization and non-homologous end-joining.XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair.Cooperative assembly of a protein-DNA filament for nonhomologous end joiningXLF regulates filament architecture of the XRCC4·ligase IV complex.Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex.XRCC4/XLF Interaction Is Variably Required for DNA Repair and Is Not Required for Ligase IV StimulationDNA double strand break repair via non-homologous end-joining.A role for XLF in DNA repair and recombination in human somatic cells.Detection and repair of ionizing radiation-induced DNA double strand breaks: new developments in nonhomologous end joining.The spatial organization of non-homologous end joining: from bridging to end joining.Functional overlaps between XLF and the ATM-dependent DNA double strand break response.Loss of NHEJ1 Protein Due to a Novel Splice Site Mutation in a Family Presenting with Combined Immunodeficiency, Microcephaly, and Growth Retardation and Literature Review.Mechanisms of DNA damage, repair, and mutagenesis.TDP1 promotes assembly of non-homologous end joining protein complexes on DNA.Spatial and temporal organization of multi-protein assemblies: achieving sensitive control in information-rich cell-regulatory systems.Achieving selectivity in space and time with DNA double-strand-break response and repair: molecular stages and scaffolds come with strings attached
P2860
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P2860
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@ast
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@en
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@nl
type
label
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@ast
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@en
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@nl
prefLabel
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@ast
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@en
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.
@nl
P2093
P2860
P50
P356
P1476
Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF
@en
P2093
Isabelle Callebaut
Jean-Paul Mornon
Marcela Nunez
Pascal Drevet
Raphael Guerois
Simona Miron
P2860
P304
26475-26483
P356
10.1074/JBC.M110.138156
P407
P50
P577
2010-06-17T00:00:00Z