53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
about
PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitryThe histone demethylase LSD1/KDM1A promotes the DNA damage responseUbc13: the Lys63 ubiquitin chain building machineWriters, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break RepairChoreographing the Double Strand Break Response: Ubiquitin and SUMO Control of Nuclear ArchitectureInterplay between Ubiquitin, SUMO, and Poly(ADP-Ribose) in the Cellular Response to Genotoxic StressRole of Deubiquitinating Enzymes in DNA RepairA Novel Aspect of Tumorigenesis-BMI1 Functions in Regulating DNA Damage ResponseFine-tuning the ubiquitin code at DNA double-strand breaks: deubiquitinating enzymes at workEpigenetic Codes Programing Class Switch RecombinationRPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response53BP1: pro choice in DNA repairMetabolic modulation of chromatin: implications for DNA repair and genomic integrityDNA DSB repair pathway choice: an orchestrated handover mechanismDouble-strand break repair-adox: Restoration of suppressed double-strand break repair during mitosis induces genomic instabilityCrosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repairFemtosecond near-infrared laser microirradiation reveals a crucial role for PARP signaling on factor assemblies at DNA damage sites.Acetylation Reader Proteins: Linking Acetylation Signaling to Genome Maintenance and CancerHistone ubiquitylation and its roles in transcription and DNA damage responseUbiquitylation, neddylation and the DNA damage responseUSP51 deubiquitylates H2AK13,15ub and regulates DNA damage responseDouble strand break repair functions of histone H2AXTIRR regulates 53BP1 by masking its histone methyl-lysine binding functionQuantitative proteomic analysis of histone modificationsDephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks.RFWD3-Dependent Ubiquitination of RPA Regulates Repair at Stalled Replication Forks.The p53-binding protein 1-Tudor-interacting repair regulator complex participates in the DNA damage response.USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism.Chromatin modifications during repair of environmental exposure-induced DNA damage: a potential mechanism for stable epigenetic alterations.A fine-scale dissection of the DNA double-strand break repair machinery and its implications for breast cancer therapy.USP13 regulates the RAP80-BRCA1 complex dependent DNA damage response.The anaphase promoting complex impacts repair choice by protecting ubiquitin signalling at DNA damage sitesDNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin.An RNF168 fragment defective for focal accumulation at DNA damage is proficient for inhibition of homologous recombination in BRCA1 deficient cells.Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells.The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.SIRT7 promotes genome integrity and modulates non-homologous end joining DNA repair.The histone H2A deubiquitinase USP16 interacts with HERC2 and fine-tunes cellular response to DNA damage.AMPKα1 deficiency promotes cellular proliferation and DNA damage via p21 reduction in mouse embryonic fibroblasts.Structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) promotes non-homologous end joining and inhibits homologous recombination repair upon DNA damage
P2860
Q24312535-2F39B5BC-0633-476E-B4D5-7CBA88F0FEFBQ24339556-A2227F7B-9C49-443E-BB2A-D85906EF62A5Q26739716-A344E53D-47B3-4E75-B7F6-375CDFB64258Q26742134-C0432C07-5892-4B3C-8923-4E49695BBC27Q26744843-F9EA9056-3A3B-4960-8A79-9613E4EDE410Q26752447-FB0DED7A-DDEF-4F2C-BB09-8AAFBEB0535AQ26773800-C4CBEAF9-5A61-412D-A1A1-D6C6667FFFDFQ26774980-5425FA28-388B-44AF-923F-4C21D31A6A36Q26781153-063340B6-7BE5-4BAC-84F5-1EDB0A27557BQ26781345-04D85DAD-13CB-41E6-9A5E-2961D955C8E1Q26827954-2C843646-7B3E-4912-935F-6301919F13F7Q26828847-0805AACB-02E2-438E-90F1-831931F6106DQ26861294-0F438B93-C3DB-4DDC-B803-9E187A4062D7Q26861805-7F255436-4C26-4EE5-8F41-AF6280D9DE0AQ26991670-221D8082-0231-470D-8664-E01B9505238FQ27023465-6AE81DA1-1983-4B29-A1A8-BC70DC1CCBE0Q27324256-985A6C56-068D-432A-9EAD-8F282639842EQ28076086-744EF8A7-A416-4A22-82D4-EA76711B2DB0Q28081194-DA2CEB1C-864B-449B-9F56-0570F410C538Q28087342-3AF8B742-615D-4F1C-BAB4-EBBD3AD36D88Q28596573-6AD51FEA-945A-4773-B4A8-ABB06A8E090EQ28661754-528C44E7-7A9F-460F-861F-EEF913F53F65Q29465810-0AA64E2C-DB62-4EC5-8DB0-381F648A64D1Q30375585-7CE518A4-5875-4E5A-A11B-033495335645Q30578616-290063BA-1D31-4F32-84BC-A1BDE3F57B90Q32884525-34D2F017-7772-472D-9B01-4CB6A4FA9D58Q33586561-D8B9EDB5-32B4-4DE4-9D5E-C216C0588D1DQ33602611-60B602DF-A043-4C97-8A76-B5BB6137E8D7Q33606592-5495B910-C362-4220-AB71-8ABA71ABCFF6Q33698648-476BA0CC-7F87-47FF-9E9D-802FFE89058EQ33770883-9CDA0BB9-1E2E-4AE9-AD73-63B3A32098F5Q33804824-4F0EEB72-683A-4188-A1F2-4668F5CFCCD2Q33834990-EFB2146D-320B-4F86-BD11-0997898E1894Q33843055-DDA0E933-37BD-4F02-A503-C44E4EFB4097Q34089181-DDE1C631-0A4A-4865-A320-69AF444CE035Q34525512-65410762-263A-4E4A-8258-71C9036884C9Q34528261-8FEDDB60-593E-4265-A16A-17FD70F4005FQ34552755-A4CBE0B4-9212-4F6F-A0F5-F640F15AEAEDQ34614152-999C6B30-046B-49F5-9C87-04DCB3EDC221Q34634191-08094E9E-3EDC-468D-A7F5-3A5015C97FC6
P2860
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
name
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@ast
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@en
type
label
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@ast
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@en
prefLabel
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@ast
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@en
P2093
P2860
P921
P3181
P356
P1433
P1476
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
@en
P2093
Alexandre Orthwein
Charles C Y Leung
Cristina Escribano-Díaz
Daniel Durocher
Frank Sicheri
Julianne Kitevski-LeBlanc
Marella D Canny
Marie-Claude Landry
P2860
P2888
P3181
P356
10.1038/NATURE12318
P407
P577
2013-06-12T00:00:00Z
P5875
P6179
1000270527