Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair - Wikidata - awgldk - TriplyDB

Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair

Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair

http://www.wikidata.org/entity/Q27652502

about

Human single-stranded DNA binding proteins are essential for maintaining genomic stability The metagenomic telescope DNA repair. Mechanism of DNA interstrand cross-link processing by repair nuclease FAN1 RAD50 and NBS1 form a stable complex functional in DNA binding and tethering SOSS complexes participate in the maintenance of genomic stability Rad17 recruits the MRE11-RAD50-NBS1 complex to regulate the cellular response to DNA double-strand breaks Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications DNA damage induces nucleoid compaction via the Mre11-Rad50 complex in the archaeon Haloferax volcanii DNA end resection: many nucleases make light work DNA Damage Signalling and Repair Inhibitors: The Long-Sought-After Achilles' Heel of Cancer Radio-resistant mesenchymal stem cells: mechanisms of resistance and potential implications for the clinic Double strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamily Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases The Mre11/Rad50/Nbs1 complex: recent insights into catalytic activities and ATP-driven conformational changes Recruitment and activation of the ATM kinase in the absence of DNA-damage sensors.Emerging critical roles of Fe-S clusters in DNA replication and repair.Crystal Structure of the First Eubacterial Mre11 Nuclease Reveals Novel Features that May Discriminate Substrates During DNA Repair Flipping of alkylated DNA damage bridges base and nucleotide excision repair A Mycobacterial Cyclic AMP Phosphodiesterase That Moonlights as a Modifier of Cell Wall Permeability Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.The Mre11:Rad50 Structure Shows an ATP-Dependent Molecular Clamp in DNA Double-Strand Break Repair ATP driven structural changes of the bacterial Mre11:Rad50 catalytic head complex Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair Conserved Structural Chemistry for Incision Activity in Structurally Non-homologous Apurinic/Apyrimidinic Endonuclease APE1 and Endonuclease IV DNA Repair Enzymes The molecular basis of ATM-dependent dimerization of the Mdc1 DNA damage checkpoint mediator The YmdB Phosphodiesterase Is a Global Regulator of Late Adaptive Responses in Bacillus subtilis DNA Double-Strand Break Repair Pathway Choice Is Directed by Distinct MRE11 Nuclease Activities Structure of Mre11–Nbs1 complex yields insights into ataxia-telangiectasia–like disease mutations and DNA damage signaling ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling Structural basis for DNA recognition and nuclease processing by the Mre11 homologue SbcD in double-strand breaks repair End-resection at DNA double-strand breaks in the three domains of life Bidirectional resection of DNA double-strand breaks by Mre11 and Exo1 DNA end recognition by the Mre11 nuclease dimer: insights into resection and repair of damaged DNA.Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repair MRE11-deficiency associated with improved long-term disease free survival and overall survival in a subset of stage III colon cancer patients in randomized CALGB 89803 trial The response to and repair of RAG-mediated DNA double-strand breaks Crystal structure of a Fanconi anemia-associated nuclease homolog bound to 5' flap DNA: basis of interstrand cross-link repair by FAN1.RECQL5 and BLM exhibit divergent functions in cells defective for the Fanconi anemia pathway Tel1 and Rif2 Regulate MRX Functions in End-Tethering and Repair of DNA Double-Strand Breaks

P2860

Q21263027-65E91772-E8B5-4E6A-A2EE-D9250D6FF43F Q21558488-B89C4074-4278-465D-8C48-2CB108691484 Q24307525-5631E4D3-FB35-460B-8312-5F40AF9565CE Q24317537-9B749E48-5B1A-4361-9BB7-EFC5D0376961 Q24329163-D0C88981-0E7F-45BF-A089-B47A8559865D Q24337442-19569975-CCAA-4246-820E-0E699FF31CEA Q24608343-4B058CD9-4683-40F7-8E16-5C1D2A3FB38B Q24626250-BC7A2CC5-7046-4EAF-BB69-DBDB97AC0639 Q24654725-2C93DAD0-3168-4F41-87BF-8670519172B6 Q26776513-33725379-9EAB-4EAD-B063-3ECCC43FB642 Q26800196-FA2545E0-1757-464B-981D-C44E979A9D1D Q26850039-3929E3CF-1943-4908-88BE-205D93D0DDDD Q27005670-FDB98C69-7E5F-470C-8B0D-4FEC510CEE6F Q27010421-FE27FAEB-9829-4AA0-83C1-42E917D09415 Q27310232-9CF29589-EC9B-40C6-86B1-A6993FCF6FCA Q27332013-9A3F1CFC-6F3F-41AD-9541-A80E6CE3E2D7 Q27644430-25189316-871C-4DC0-AA1D-B90A7E9727DF Q27655873-E3B42B06-7104-49DC-AF01-E7AEB4BA69CA Q27657658-5A2D159A-D4E9-4BB9-B4F8-091CC3B209C4 Q27657670-E13E8DA2-458A-4A5B-9320-5D9313145D3B Q27667335-01220236-1FCA-40CA-9D2D-F7343FE2A55D Q27667404-19AC3E47-49FE-4641-909B-A9CED8F83716 Q27674381-F9B9BE5C-D18E-4C01-BA04-2C8D4D85FEAF Q27674627-83668E15-0D84-492B-9A17-A6989EC0435D Q27676022-FD1EBA3A-3CF6-4873-81BD-AF01D0DA6463 Q27676681-0C2900E4-4130-46E9-9AD8-07EDC184F52F Q27680466-1299F58C-6FEE-4022-A99A-E8F90D122986 Q27680811-4D5F1360-DA05-407C-A1B4-AB5FD6C3F2CD Q27681202-9C2AF730-6F0C-413F-898D-13C6F5B3CA34 Q27681577-2241A537-888E-424C-8DCE-81DB60FCD1B5 Q27689081-634ACD98-9DB6-4E57-838E-571234645668 Q27694756-9245C272-83C9-4517-BC86-D495ABF5752C Q27930407-5DFB1675-57DE-4EE9-A101-78AA326A1656 Q27937081-5D2775FD-8166-41B4-B94D-791614E0C1A2 Q28085622-FDE4681E-7885-431D-BC8A-F508E0D720BB Q28249648-C24930CF-46C1-4116-8F63-C86629EC9482 Q28256889-DE52CB41-92E6-4FEB-94C0-374230787291 Q28492645-0D2EE6A1-CE1C-45E9-B263-EC4681D5A00F Q28512695-087C3713-E910-406A-9895-C9A865E5EE3D Q28550291-E4845C4D-4ACE-4486-AE2C-BA7E6E9B10AE

P2860

Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair

http://www.wikidata.org/entity/Q27652502

description

2008 nî lūn-bûn

@nan

2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@ast

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@en

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@nl

type

label

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@ast

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@en

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@nl

prefLabel

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@ast

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@en

Mre11 Dimers Coordinate DNA En ...... in Double-Strand-Break Repair

@nl

P1433

Q27652502-7C47AC78-4BBA-4B10-BC9E-D453CE955E7B

P1476

Q27652502-6842C286-CA87-4610-8D24-4A4D005C6AF9

P2093

Q27652502-19D8DB88-E75C-4C47-89F0-49891E0E5C7B

Q27652502-269D9C1E-49C5-404A-8583-BE88B69A65B6

Q27652502-417CCB7C-50EE-4580-A60C-D07F8C368497

Q27652502-4698A5DE-263D-4F12-8610-47BF32E1A26D

Q27652502-88C42E75-4E94-40A5-B4EA-6CA8FDEA56C2

Q27652502-B000F062-D7CD-4B01-A559-98FB97EF0907

Q27652502-B1048B08-9C25-45E2-ABD3-2870A604C06A

Q27652502-B395A8C3-B5AE-44F7-9DC0-0F90FF78B0FD

Q27652502-C957BB69-3DC9-46FA-A855-8DA824FF73CA

Q27652502-DCD6F789-651D-45B7-BCE8-4181B55BB7F2

P2860

Q27652502-01B0704C-F489-44A1-BA87-2D02607F1203

Q27652502-037C34D2-3D62-4C5E-988B-27A484B21216

Q27652502-03CAD53B-B0A4-4D77-A9FF-D8A1F9FA3069

Q27652502-04933BEF-884E-41EB-81F9-D350FC6B8BEA

Q27652502-09AD738A-46A8-47A9-B68E-85BA33F9D4B0

Q27652502-0F3785FD-7604-4640-9EA6-C75235596AA4

Q27652502-13DDF161-E8AC-4574-81C1-EF14837575E1

Q27652502-15963AE5-614A-441F-A34E-FA497E74A27D

Q27652502-18988CCB-754A-47A5-B471-ED7315C43A07

Q27652502-2621C277-0463-4838-A71A-75DD061E46EF

P304

Q27652502-88C02B8E-0E5B-4907-92C3-2072AFB6752F

P31

Q27652502-208714B6-D84D-4A90-953D-E92805B6EA07

P3181

Q27652502-EECB63B7-AD7B-4C2B-9D77-E7606749F055

P356

Q27652502-647A25C5-224C-4E46-A11B-3604F3BB53E7

P407

Q27652502-01DA20C4-E738-47E6-8267-AE10E6336602

P433

Q27652502-FA3B650A-BC07-4224-A107-DFC49A58A987

P478

Q27652502-CA7B4A41-34FE-47CD-9A63-A6629ADE76A8

P50

Q27652502-21C9584A-B3F3-4502-A6FA-3165FC586D52

Q27652502-5ED70C02-F10B-4C72-9C53-61FA7A687C0F

Q27652502-F6952923-F175-473E-B1B0-27883EAE0D2C

P577

Q27652502-A0147F21-F76B-4B9F-9F87-9119E88ABBCD

P5875

Q27652502-3288DA31-ACBB-48D4-9E0A-2368DD941F03

P698

Q27652502-F6570067-AF36-4B71-909C-CFBEA2E60493

P932

Q27652502-51090DB8-2449-4BB8-A9C6-A1F659850DAE

P3181

P356

J.CELL.2008.08.017

P1433

P1476

Mre11 dimers coordinate DNA en ...... in double-strand-break repair

@en

P2093

Chiharu Hitomi

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

Dana Cahill

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

David S Shin

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

Davide Moiani

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

Grant Guenther

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

James P Carney

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

Jessica S Williams

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

Lynda M Groocock

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

Paul Russell

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

R Scott Williams

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

P2860

ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex

The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair

The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks

The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response

Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95

XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations

Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex

Human CtIP promotes DNA end resection

Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase

Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair

P304

97-109

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

P31

scholarly article

P3181

2284217

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

P356

10.1016/J.CELL.2008.08.017

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

P407

P433

1

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

P478

135

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

P50

Gabriel Moncalian

P577

2008-10-01T00:00:00Z

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

P5875

23316772

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

P698

18854158

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

P932

2681233

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