Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV - Wikidata - wikimedia - TriplyDB

Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV

Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV

http://www.wikidata.org/entity/Q24563248

about

CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks ATM-mediated phosphorylation of polynucleotide kinase/phosphatase is required for effective DNA double-strand break repair Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK Eukaryotic DNA ligases: structural and functional insights Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2 FHA domain Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4 Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4 DNA-PK: a dynamic enzyme in a versatile DSB repair pathway Diseases associated with defective responses to DNA damage Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions Structural basis for the phosphatase activity of polynucleotide kinase/phosphatase on single- and double-stranded DNA substrates Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4.Processing of damaged DNA ends for double-strand break repair in mammalian cells The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis XRCC1 stimulates polynucleotide kinase by enhancing its damage discrimination and displacement from DNA repair intermediates DNA joint dependence of pol X family polymerase action in nonhomologous end joining Non-homologous end-joining, a sticky affair Role of non-homologous end joining in V(D)J recombination Role of polynucleotide kinase/phosphatase in mitochondrial DNA repair Mechanism of action of an imidopiperidine inhibitor of human polynucleotide kinase/phosphatase.Nonhomologous end joining: a good solution for bad ends A strategy for interaction site prediction between phospho-binding modules and their partners identified from proteomic data Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joining Assessing Candidate Gene nsSNPs for Phenotypic Differences in Double-Strand Break Repair Using Radiation-Induced gammaH2A.X Foci 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 Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response.DNA Ligase IV regulates XRCC4 nuclear localization.Polynucleotide kinase as a potential target for enhancing cytotoxicity by ionizing radiation and topoisomerase I inhibitors 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.XLF regulates filament architecture of the XRCC4·ligase IV complex.Neurological disorders associated with DNA strand-break processing enzymes.Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation DNA repair mechanisms in dividing and non-dividing cells.

P2860

Q22001526-70CD722A-319F-4C06-A989-B5A2F4E8C42C Q22065419-2D5C0CED-FCA2-4CE5-B1AD-F8BAF7AFC145 Q24299831-DEC9C75A-C207-4F4A-8AF2-CB5C8987ADB7 Q24305338-81748411-E4B8-4357-B302-609B7F9F3360 Q24318721-CF7721D2-9B47-4711-B033-A1E58CCEA8E8 Q24617266-B923C92B-40B9-4449-A805-8C285396FEB1 Q24646357-64FD60AC-50C6-483D-A619-9740CE70708D Q24675041-9AD220CF-C519-4E49-AF1A-8B87C4816DA6 Q24682173-2921FD1C-7D93-4050-8F42-22351FF5E753 Q26866928-B609C0B0-4F4B-43D3-A3D3-FBBE5038BC27 Q26997852-F7EB3E82-96A7-4E8D-8410-E821CC72B262 Q27657670-A0FBC0D9-0BE8-40E0-A4C4-9DF7C9EAC97C Q27674365-2F39CC76-A361-4F7E-9AE0-F668F327D253 Q27676221-2DD29D09-4EE4-4A03-8733-0164DD182927 Q27931428-9E853661-C0C4-41D5-9ED7-9DA970D8DF2B Q28000148-26672735-EF80-4A8B-9385-D791F2A1012F Q28081821-F78242D1-9971-40CF-A993-843E0E802D54 Q28237523-08E331A0-DA00-4F86-A706-A4A14B3B6A90 Q28257407-2A0BDFA4-704A-4362-9488-62DA421BCA9D Q28260337-180AAE46-EFC5-443F-96A3-41012BC243D1 Q28266265-10B6E41F-6FF9-49AD-9A05-598376D5B66C Q28570918-75D1D2D8-588F-49B3-B401-7EE8CE4C50DC Q33593867-2C7147B0-B4E2-45CB-A130-E2AE17090DC2 Q33625010-AD61D84F-10ED-4157-82AE-C745C5CD28F4 Q33669971-1DD7650E-0206-490D-99B0-CAD69A6F6203 Q33741181-6E55DAC7-FDEA-4085-90A1-7C6126C5F846 Q33788936-AF51E3F0-15C6-4F47-AEEA-0CFCC5BA8C90 Q33807557-AFDF4B46-D74D-4BFF-8932-B1B83C31E8AC Q33854272-1CCBA6C7-16C5-4580-8CCF-1A2E1BE2B65F Q33914715-34A982F0-CC94-442D-82FD-9690CF95FDB1 Q33927202-BD3CD97B-3115-4801-BE5B-2285DFB20C03 Q34118213-15938994-FBD3-4729-AF5B-69B7BFBCB55C Q34231660-A86E35D9-3C2D-47FE-B927-7DB2C3788919 Q34329896-328570FD-C30B-4812-990A-2B53018B910F Q34333731-7D30446F-F231-4D66-B741-662DD57ED79F Q34433470-8562BF94-E124-45B5-B83C-0F96CAC3C71D Q34535722-20D25FE2-C6F9-484C-9C12-59E187719CDC Q34550224-E1109AE1-1606-4D48-A91A-838C6A3FAC86 Q34610477-A4B3C84E-4FD1-4434-B4A4-55B39D18DD62 Q34727858-4DA21202-D25E-4715-8DAD-EBBD195FD66E

P2860

Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV

http://www.wikidata.org/entity/Q24563248

description

2004 nî lūn-bûn

@nan

2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

name

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@ast

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@en

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@nl

type

label

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@ast

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@en

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@nl

prefLabel

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@ast

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@en

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@nl

P1433

Q24563248-B3569029-61AE-48C2-844F-25972F4E04FE

P1476

Q24563248-0B18922A-CEE0-4094-815C-4081C02BC97B

P2093

Q24563248-19A7FBBE-281B-4883-8B4B-817B86502EB9

Q24563248-2AADC357-4F93-46FC-9378-D652E81EFF85

Q24563248-39F25125-C81E-4D46-8736-67AF19108DCA

Q24563248-5BCD8D7F-ACB6-4285-81C0-46C702735C20

Q24563248-5C66A9FC-A949-4C1F-9DF6-C54EAF865D62

P2860

Q24563248-00DDA559-0067-4ABC-9310-DD4304B688CA

Q24563248-05D821DB-93BF-49BF-853D-1195277E46B0

Q24563248-0DCA9F31-06B2-47AD-8143-2329ED0D00F8

Q24563248-11F9D0EC-A093-40AD-8C9B-C1AC3A0053CA

Q24563248-1928908C-FE54-4476-BB86-62910263429E

Q24563248-301EE3CE-63D3-4DC6-B162-11BC206366C0

Q24563248-41FEFD8E-BDDA-431B-BD37-5FAA53192186

Q24563248-5241DACA-13C4-414C-AAA6-8BE3AA467ADA

Q24563248-53CB84DE-2FBF-4F29-8EDA-3D665321A9AA

Q24563248-60137AE7-127B-4748-A244-25B3762C4DBA

P304

Q24563248-24632C01-1EE8-4D0E-918F-3598B358F47C

P31

Q24563248-6262B1DD-8546-4E44-892C-91C27C2D83FB

P356

Q24563248-349B45AF-D148-4DCA-ACD2-0D77E90666A3

P407

Q24563248-D6D9C827-DCCF-40CD-879B-C914A6FFE1B8

P433

Q24563248-E374E3D7-999C-444C-98F6-64F01041B19A

P478

Q24563248-943F6173-20C1-4E5A-9E92-D3E2784645F0

P50

Q24563248-3043255E-40DD-4058-B353-FC7FC40BAD13

Q24563248-4D3371A8-D892-44D6-8B93-A1EAC0909A49

Q24563248-E07AE91D-5D4E-4A0C-BF15-CC5320FB73C5

P577

Q24563248-8EC22875-3BAB-4C78-B515-161244E3BBA0

P5875

Q24563248-DEB701EF-41CD-4BF9-B1F5-D29A2B73E95F

P698

Q24563248-562C9BE5-C79F-4078-BFD3-7855D934A5F4

P932

Q24563248-7AEC4565-C7F1-44E2-88BA-465F99D2C35D

P356

SJ.EMBOJ.7600375

P1433

The EMBO Journal

P1476

Xrcc4 physically links DNA end ...... DNA ligation by DNA ligase IV

@en

P2093

Christine Anne Koch

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

Michael Weinfeld

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

Paul O'Donnell

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

Roger Agyei

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

Sarah Galicia

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

P2860

Molecular characterization of a human DNA kinase

Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination

Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1

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

DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity

Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining

Crystal structure of the Xrcc4 DNA repair protein and implications for end joining

Lif1p targets the DNA ligase Lig4p to sites of DNA double-strand breaks.

Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase

P304

3874-85

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

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7600375

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

P407

P433

19

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

P478

23

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

P50

Daniel Durocher

Pavel Metalnikov

Andrei Starostine

P577

2004-10-01T00:00:00Z

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

P5875

8328962

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

P698

15385968

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

P932

522785

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