XLF regulates filament architecture of the XRCC4·ligase IV complex.
about
XLS (c9orf142) is a new component of mammalian DNA double-stranded break repairStructural 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 joiningA practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteinsDouble strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamilyDNA-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 interactionsStructural Basis of DNA Ligase IV-Artemis Interaction in Nonhomologous End-JoiningStructural Insights into the Role of Domain Flexibility in Human DNA Ligase IVThe DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosisRole of non-homologous end joining in V(D)J recombinationDeveloping advanced X-ray scattering methods combined with crystallography and computationImplementation and performance of SIBYLS: a dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the Advanced Light Source.Nonhomologous end joining: a good solution for bad endsStructural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complexHigh-throughput SAXS for the characterization of biomolecules in solution: a practical approachStructural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a timeDNA Ligase IV regulates XRCC4 nuclear localization.Cernunnos influences human immunoglobulin class switch recombination and may be associated with B cell lymphomagenesisXPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase.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 joiningNon-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.Saccharomyces cerevisiae DNA ligase IV supports imprecise end joining independently of its catalytic activity.Recognition and repair of chemically heterogeneous structures at DNA endsYeast DNA ligase IV mutations reveal a nonhomologous end joining function of BRCT1 distinct from XRCC4/Lif1 binding.A recessive variant of XRCC4 predisposes to non- BRCA1/2 breast cancer in chinese women and impairs the DNA damage response via dysregulated nuclear localizationAkt-mediated phosphorylation of XLF impairs non-homologous end-joining DNA repair.Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex.Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repairValidation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS).Ionizing radiation-induced DNA injury and damage detection in patients with breast cancerStructure-Based Virtual Ligand Screening on the XRCC4/DNA Ligase IV Interface.Restoration of ATM Expression in DNA-PKcs-Deficient Cells Inhibits Signal End Joining.Accurate SAXS profile computation and its assessment by contrast variation experimentsDNA double strand break repair via non-homologous end-joining.Role of the yeast DNA repair protein Nej1 in end processing during the repair of DNA double strand breaks by non-homologous end joiningAn Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.
P2860
Q24337357-242E317B-52E4-4519-99F7-DE842165685FQ24622950-864D41AF-D086-4B22-9034-7E11AA643EA3Q24630031-B96DA0C0-A943-4906-9809-70C99374E8BCQ24630098-6CC21361-AA6D-4455-912C-0BEC6E6B96C9Q26796304-33367043-B1A0-4961-BD87-BE473C619FF4Q26850039-63BF0BC5-D11A-40A4-8998-5FC89CFEF7BDQ26866928-8DDB832D-51FE-4A8F-9BA5-AF961CB901B3Q27670908-F9CECED2-6C09-4920-953D-184A9C4AA14DQ27674365-C0360D5A-8CED-4D20-A716-A322DD996C45Q27675393-88B94F2E-6CB6-4BCD-A041-965A52510B6FQ27679426-CC47298B-C761-4AFF-A25C-31EBCCA2FE46Q28081821-93726731-D400-4806-B504-0912EA23F0A3Q28266265-195D83DF-E962-4C80-A39E-A9FBFF7420E0Q28681355-13198E37-C0AE-4324-AA9F-B8F67300F223Q30532509-01A7C609-792E-4FC9-AC70-ED7E1088F17AQ33625010-C5BBD9AD-6376-4D9A-8FA8-19886878C8FFQ33741181-9AB90AFE-8453-4C84-BDA2-DA2674CD33F4Q33753946-0675FF44-E367-4961-AAC2-72B4FF4C1391Q33914715-A01AA63D-272A-4555-B92B-7286CD1BE033Q34118213-84AD182E-9384-4EBB-B60A-905D1CD8ED18Q34152519-E498D1DA-E801-4007-A2A2-2206C672E5F7Q34184951-6F293A6B-6E6E-4533-80A3-B804ABB388EEQ34329896-CAAFE745-FE14-4B6F-9C71-DD8FCEB8413AQ34341430-10F4984E-4C13-4BCF-909D-2FBD08F778E6Q34550224-B5E246E7-1310-4C2D-A8E3-635E06ADD787Q34795549-AF02CEB3-8B80-4E97-9C61-F9B1C3940C6CQ35002075-633C5739-CE12-472F-ACDA-509DCF6E6BC8Q35007981-A57DD7CE-A470-4F2B-9BF4-ADCCB4D46C19Q35067965-E1EC4935-A171-4E11-89A8-A3B56E5F2B8EQ35108163-E94EA1C1-15D4-4591-93AE-678671C036CAQ35539378-D2166A39-8244-4113-83DE-11F4FA3BD55DQ35644654-8552DC8A-C638-4682-9CEB-2DF8C18F68E2Q36293440-EF7AC5B7-4903-4122-9A22-CCDC691FC352Q36606214-A13A96E9-B68F-4000-A79E-2A1F1525F82DQ36674946-F19C4F3F-B2D9-4D86-A821-C74C359756E2Q36706287-C234DDD0-C010-4360-82F7-BA18B84D129AQ37117438-4AA5A690-B967-43B7-84EF-23974BA53E8CQ37135926-9393D25B-3382-4FAC-B06C-1CF5ECF528D1Q37289660-822839F0-E4C5-404A-B6AC-10F5DCEB8ED2Q37551399-CD0FE747-FD57-4AE3-ACCE-0EFE11C950BB
P2860
XLF regulates filament architecture of the XRCC4·ligase IV complex.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@ast
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@en
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@nl
type
label
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@ast
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@en
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@nl
prefLabel
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@ast
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@en
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@nl
P2093
P2860
P1433
P1476
XLF regulates filament architecture of the XRCC4·ligase IV complex.
@en
P2093
John A Tainer
Michal Hammel
Shujuan Fang
Susan P Lees-Miller
P2860
P304
P356
10.1016/J.STR.2010.09.009
P577
2010-11-01T00:00:00Z