53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions. - Test2 - elhamkhani - TriplyDB

53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions.

53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions.

http://www.wikidata.org/entity/Q28000132

about

Writers, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break Repair Interplay between Ubiquitin, SUMO, and Poly(ADP-Ribose) in the Cellular Response to Genotoxic Stress Homologous Recombination Deficiency: Exploiting the Fundamental Vulnerability of Ovarian Cancer 53BP1: pro choice in DNA repair MicroRNAs down-regulate homologous recombination in the G1 phase of cycling cells to maintain genomic stability BRCA1 and CtIP Are Both Required to Recruit Dna2 at Double-Strand Breaks in Homologous Recombination Rif1 maintains telomere length homeostasis of ESCs by mediating heterochromatin silencing A PTIP-PA1 subcomplex promotes transcription for IgH class switching independently from the associated MLL3/MLL4 methyltransferase complex TIRR regulates 53BP1 by masking its histone methyl-lysine binding function RAD51 Is a Selective DNA Repair Target to Radiosensitize Glioma Stem Cells.Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks.53BP1 and the LINC Complex Promote Microtubule-Dependent DSB Mobility and DNA Repair The p53-binding protein 1-Tudor-interacting repair regulator complex participates in the DNA damage response.Generation and repair of AID-initiated DNA lesions in B lymphocytes.A fine-scale dissection of the DNA double-strand break repair machinery and its implications for breast cancer therapy.CtIP-mediated resection is essential for viability and can operate independently of BRCA1.Mechanisms controlling the smooth muscle cell death in progeria via down-regulation of poly(ADP-ribose) polymerase 1.Conditional genetic interactions of RTT107, SLX4, and HRQ1 reveal dynamic networks upon DNA damage in S. cerevisiae.PRL-3 promotes telomere deprotection and chromosomal instability.Heterochromatin controls γH2A localization in Neurospora crassa.The 9-1-1 checkpoint clamp stimulates DNA resection by Dna2-Sgs1 and Exo1.A new Riff: Rif1 eats its cake and has it too.DNA double-strand break repair: a tale of pathway choices.AMPKα1 deficiency promotes cellular proliferation and DNA damage via p21 reduction in mouse embryonic fibroblasts.PTIP associates with Artemis to dictate DNA repair pathway choice.UbcH7 regulates 53BP1 stability and DSB repair Use of the γ-H2AX assay to investigate DNA repair dynamics following multiple radiation exposures.Regulators of homologous recombination repair as novel targets for cancer treatment.KAP1 Deacetylation by SIRT1 Promotes Non-Homologous End-Joining Repair Ectopic expression of RNF168 and 53BP1 increases mutagenic but not physiological non-homologous end joining.Critical Function of γH2A in S-Phase EEPD1 Rescues Stressed Replication Forks and Maintains Genome Stability by Promoting End Resection and Homologous Recombination Repair.Biochemical mechanism of DSB end resection and its regulation.Low-dose ionizing irradiation triggers a 53BP1 response to DNA double strand breaks in mouse spermatogonial stem cells.An H2A Histone Isotype, H2ac, Associates with Telomere and Maintains Telomere Integrity.Replication fork stability confers chemoresistance in BRCA-deficient cells Impaired 53BP1/RIF1 DSB mediated end-protection stimulates CtIP-dependent end resection and switches the repair to PARP1-dependent end joining in G1.Chemical proteomics reveals a γH2AX-53BP1 interaction in the DNA damage response SCAI promotes DNA double-strand break repair in distinct chromosomal contexts USP7 deubiquitinase promotes ubiquitin-dependent DNA damage signaling by stabilizing RNF168.

P2860

Q26742134-1B63ADE2-C7AE-48D2-ACAF-D6E000982208 Q26752447-8A61DE82-22EF-404B-94B0-3970EA90B1AB Q26783551-829E3FF7-4368-48B5-9A3C-1E0DE33667C4 Q26828847-F43D3DE1-4847-456C-8EFC-1F4A4067CABA Q28240422-D9562FFA-2105-4938-8D88-89FCBBE568B0 Q28261099-5F590F5D-1263-40DD-AC27-FCAEABD0C1F4 Q28591651-014DEAA2-6F8B-4E7F-8F84-015867A70D67 Q28591850-3EA7AAB9-2B5E-4A35-81D5-5470299E15F9 Q29465810-CCD3E738-F92F-4FB1-A278-BB0DACEE3A63 Q30365298-C58DDE6C-5B7B-407E-961B-32BF362F93DE Q30578616-4B90C66E-8A1B-4579-B4E2-BB0FCCC46840 Q30673640-9A706037-E582-4DCA-9153-9AA460123E47 Q33586561-DFF6C494-A146-4F85-8746-45F3E5DF5A8F Q33690522-EED9A96A-7077-4965-941D-1263C810B60A Q33698648-489926E7-92DE-403D-99E3-34B2A7290EB8 Q33703015-D3B67FFB-CF9A-4531-B890-49DAE6AF971E Q33730599-BD3D68E7-EBDE-41C5-8C85-AA2FFCED76EF Q33784933-A9390E53-A4B9-4C5A-9FBF-4B7C9DD9AD4A Q33878962-523D75D0-1B46-4985-90B5-EB98058377C0 Q34057278-B890F8E7-D9B5-4D4F-B91E-82C3526F7989 Q34249598-131FD94D-8E92-4B64-8931-215DE3D4A13C Q34342524-9D8713D9-13BB-4380-9ABE-768A7C5B4EA9 Q34528005-E28CB732-4425-4F40-8AB5-72438B16992C Q34614152-EF2D0DF6-BF7F-4779-87CE-217FCAA49FBE Q34697707-4866DFFE-549A-4339-9A84-AD430F27EBC5 Q34709157-18D092AB-1AC2-4B08-A7D0-0B62C9CBF457 Q35060189-1B1E98F1-4AF9-45F3-863E-7F855EB59BB3 Q35200273-2526BF0F-DABC-4CC1-855A-3D9015F96D8A Q35532757-F0D5F9A9-B718-4843-BD23-B3A873E7BBB1 Q35656738-47CCF38A-D76E-4187-944E-0A680333D3E0 Q35774171-8D0CBA7D-0BD3-494B-958C-DA2F4879B938 Q35873250-57F84E15-41CA-45CC-B1E2-E34156E46EE9 Q35908828-4E024CF1-22CC-4E77-9CDE-E28F2C133423 Q35917737-575D5B4D-5422-4648-B2BE-A1F3E0EDD85E Q36030762-6028F577-F8DA-4D01-A55A-1496F6D7B5F4 Q36083474-87058F49-54C5-4CEE-95EA-41A54832380B Q36096169-27D91C71-4AA9-4FB2-AF13-63357342A598 Q36108201-84D15C07-6C00-406F-B349-5A8B47095A35 Q36184268-4E0F171A-D97C-4DE9-AF30-8026FEA35099 Q36184372-D1D7FCDA-ADF1-4CDC-B984-A35877A94151

P2860

53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions.

http://www.wikidata.org/entity/Q28000132

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年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

53BP1 mediates productive and ...... t phosphoprotein interactions.

@ast

53BP1 mediates productive and ...... t phosphoprotein interactions.

@en

53BP1 mediates productive and ...... t phosphoprotein interactions.

@nl

type

label

53BP1 mediates productive and ...... t phosphoprotein interactions.

@ast

53BP1 mediates productive and ...... t phosphoprotein interactions.

@en

53BP1 mediates productive and ...... t phosphoprotein interactions.

@nl

altLabel

53BP1 mediates productive and ...... ct phosphoprotein interactions

@en

prefLabel

53BP1 mediates productive and ...... t phosphoprotein interactions.

@ast

53BP1 mediates productive and ...... t phosphoprotein interactions.

@en

53BP1 mediates productive and ...... t phosphoprotein interactions.

@nl

P1433

Q28000132-44FB9233-BC42-4D61-94AA-13F5BA262DE8

P1476

Q28000132-99C63865-9AC4-4FA9-8A3A-EB4E904D468F

P2093

Q28000132-1C43EB59-A65D-4EE5-B4FF-945159801B7D

Q28000132-1D57F465-6F6E-43DA-AEB9-A7E34C1AFDAD

Q28000132-3B2BECA7-36AF-4FA2-AC36-8624D3C13E55

Q28000132-3EEB7F14-DF25-4428-A27D-2C5A4139429B

Q28000132-4432FB04-502E-4439-A86B-4BB3702FC4D2

Q28000132-4C4603B2-D371-455F-9C3C-4900DAFE27C9

Q28000132-61B31EBA-E9F0-427E-A328-E5B44EB95267

Q28000132-9CADC76F-BD97-432D-BC62-693815A4B300

Q28000132-BBF8A02D-7CD3-4118-A9CC-B6721DE2A859

Q28000132-D04AE688-FF1B-40FC-9AEB-36B3B3B5E329

P2860

Q28000132-1C240027-74FC-48E8-96D8-AC3BF2679DA7

Q28000132-205E37DA-E54C-499A-AB09-B5BFCF9F7CBB

Q28000132-208F3ED0-D8DE-4B76-97AA-C7464DD20DD2

Q28000132-353FC6C7-AB1A-4DDE-8082-636F86339158

Q28000132-38A02CF9-352A-42D5-9B4A-4DE75B154EA2

Q28000132-3AB9EFB5-E0A7-447A-A558-EB8095BE8A1C

Q28000132-3D66D8A9-6B18-4250-9FF3-A724D4FDD5AE

Q28000132-42E20001-61AD-4CBE-A216-3BD807433774

Q28000132-47A29690-69C7-453F-B9C3-5A9B0B412786

Q28000132-4925D7B5-3331-4222-892A-95CF739B6B95

P304

Q28000132-0842E5CA-1256-4110-9357-FDFA28F631D3

P31

Q28000132-BBA82219-61B3-4A70-B874-2530F8BA5357

P3181

Q28000132-508AB1BA-4BBD-45A3-B233-3B9A87A71DBB

P356

Q28000132-7314EB0E-AE03-45DA-BED5-8B285B0E1172

P407

Q28000132-A25A437E-165A-4A8E-9E5E-71ED9E059D71

P433

Q28000132-025E2CA2-35FF-4607-A2A2-E7F5B83C8106

P478

Q28000132-82008DF5-FCB1-449A-A3D4-EBEC829393A2

P50

Q28000132-4685FDC5-2165-4F6F-86C7-9F4EB9C294F4

Q28000132-6AC92398-75A4-4983-8460-10A985B1C71B

Q28000132-93AF9E2B-152E-4EB1-A057-E4FDAF531EB1

Q28000132-B23BE379-4211-42E0-ADB5-06573B2D12C9

Q28000132-C4E1A078-B36C-43BB-A1F3-2EAF37CCEDBE

Q28000132-D201C1D8-5ACC-4D85-BF0C-05245D210B18

Q28000132-EA4B10B7-6880-4582-B02B-8DD05DAFEEF1

Q28000132-F633728B-F581-40D4-9B39-5F051C30937C

P577

Q28000132-432D2F2D-8F52-4F38-9521-20791EBD9C17

P5875

Q28000132-38E118AF-EC1E-4E24-A249-257E74DA9B10

P698

Q28000132-1A91CBA5-D902-4F2E-B64A-4A097DD9F19C

P932

Q28000132-AECFE0E0-0617-41AD-8199-26760E71F88B

P3181

P356

J.CELL.2013.05.023

P1433

P1476

53BP1 mediates productive and ...... ct phosphoprotein interactions

@en

P2093

André Nussenzweig

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

Barry P Sleckman

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

Duane R Wesemann

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

Elsa Callen

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

Federica Polato

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

Frederick W Alt

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

Hua-Tang Chen

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

Linda M Starnes

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

Margarida Santos

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

Michael J Kruhlak

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

P2860

Bioconductor: open software development for computational biology and bioinformatics

The BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine 4 methyltransferase complex

The BRCT domain is a phospho-protein binding domain

PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex

Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation

Accumulation of Pax2 transactivation domain interaction protein (PTIP) at sites of DNA breaks via RNF8-dependent pathway is required for cell survival after DNA damage

Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage

Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint

53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers

Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy

P304

1266-1280

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

P31

scholarly article

P3181

1267640

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

P356

10.1016/J.CELL.2013.05.023

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

P407

P433

6

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

P478

153

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

P50

Jeremy A Daniel

Oscar Fernandez-Capetillo

Anthony T Tubbs

Michela Di Virgilio

Maria Nieto-Soler

P577

2013-05-30T00:00:00Z

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

P5875

237003300

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

P698

23727112

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

P932

3713552

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