Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer - Test2 - elhamkhani - TriplyDB

Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer

Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer

http://www.wikidata.org/entity/Q28260830

about

Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation The BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine 4 methyltransferase complex DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains CCDC98 targets BRCA1 to DNA damage sites Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex STRUCTURE-FUNCTION OF THE TUMOR SUPPRESSOR BRCA1 Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains BRCT domains: easy as one, two, three Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1 A guide for functional analysis of BRCA1 variants of uncertain significance Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif A microchip platform for structural oncology applications.Solution Structure of Polymerase μ's BRCT Domain Reveals an Element Essential for Its Role in Nonhomologous End Joining †Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach Structure of a Second BRCT Domain Identified in the Nijmegen Breakage Syndrome Protein Nbs1 and its Function in an MDC1-Dependent Localization of Nbs1 to DNA Damage Sites The Structure of Fcp1, an Essential RNA Polymerase II CTD Phosphatase Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair A Pocket on the Surface of the N-Terminal BRCT Domain of Mcph1 Is Required to Prevent Abnormal Chromosome Condensation Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIÎ² binding protein 1 Structure of the DNA-bound BRCA1 C-terminal Region from Human Replication Factor C p140 and Model of the Protein-DNA Complex Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1 Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control Impact of BRCA1 BRCT Domain Missense Substitutions on Phosphopeptide Recognition Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1 Molecular Basis for the Association of Microcephalin (MCPH1) Protein with the Cell Division Cycle Protein 27 (Cdc27) Subunit of the Anaphase-promoting Complex Structural Insights into Recognition of MDC1 by TopBP1 in DNA Replication Checkpoint Control Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes.Beyond DNA: An Integrated and Functional Approach for Classifying Germline Variants in Breast Cancer Genes Tumor suppressor BRCA1 epigenetically controls oncogenic microRNA-155 Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics BRCT domains: A little more than kin, and less than kind Plasma Membrane Association but Not Midzone Recruitment of RhoGEF ECT2 Is Essential for Cytokinesis How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers High occurrence of BRCA1 intragenic rearrangements in hereditary breast and ovarian cancer syndrome in the Czech Republic.Rtt107/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs.FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein.Dual-fluorophore quantitative high-throughput screen for inhibitors of BRCT-phosphoprotein interaction

P2860

Q24293084-E0AD9D29-6193-4E11-BC28-B5F327A19959 Q24296996-CB308F46-A854-4D6A-978C-359D92D0119D Q24306945-35D2D939-4ED8-4264-8455-0BC509AEDA35 Q24321418-68E9B281-9FDF-46DF-A7D4-D721678E528F Q24337134-43DDFA52-EFB0-47D7-8621-35D992E3EC80 Q24339507-1992C4D6-3F6A-442C-BC91-16B1E8182E3B Q24600363-5AC73FAF-D070-4C99-B05B-48DF8CF18665 Q24628641-DA9CE8AC-5490-4947-96B0-F19C2192EACB Q24635835-F41D9217-5D02-444C-8A7C-F56F27C5A232 Q24651980-81C28637-70E7-4126-AC77-48E0BF0DA883 Q26829268-DFBB3CE0-9965-4117-9BEB-571487336AD7 Q26999072-16DD8161-2546-4A26-9F2A-767259020CAC Q27311331-1BAEF067-4FD0-42BE-B934-450F69D572E6 Q27648712-7E5F9A16-20AB-4849-9454-A3D6F56C76AF Q27649882-77A724FE-EFBD-4004-9CA1-E34DD772FF6C Q27650955-61567DAE-D9C6-4C68-AA3D-ABCB32200D54 Q27652973-12496842-DCBC-4674-B071-4C2A04883BF5 Q27657670-6BD1197B-7E44-4F17-BF8B-970F7E63340A Q27658266-58D093D3-35A6-46C9-9EA3-B6E193ACD6D3 Q27658324-BBDAD996-705B-43DD-A97B-0B40209552E3 Q27659008-C0D817AB-6E01-4FB4-BEB0-BAB0E54E5578 Q27664093-65A0E5F3-21E1-4733-8103-60246CE325F6 Q27666163-6EA8D085-0612-4833-9FAF-6EE50A33F0AD Q27667456-A2AA5FAD-3EC9-41C4-B32D-27A5C9C8556E Q27671621-F90372CA-2FB2-4A9C-A85D-9EE2C8134F4C Q27675971-CACFFA69-A0DA-46E5-A8F5-F905A0099712 Q27679213-865CF985-774B-410F-B15C-E7DBB804689C Q27930239-2BEDAADD-5FCF-4983-B1A5-2F3E2CF5B5B0 Q28072478-5EBBAE1D-F4C0-4BFD-8F68-7FCFF3836E8A Q28249114-0B7F562B-D6F3-4843-940E-528211B9B9F3 Q28274000-38C32AF5-23AE-4B23-BA6F-816F5289D59D Q28297156-E4711E40-CB1C-4D9C-9AC8-BAEC1BB75963 Q28390760-86016AAB-34CC-41C8-8FAD-A9531343FCC8 Q28728558-60EC8E03-37C3-4F93-B894-8F84A6C33211 Q28818796-6E4CD663-E52C-4474-9867-0C90E30E5420 Q29547350-3422EBB7-69EC-4D3E-9A2B-20C9A3BABF42 Q30832030-AEFA7A55-CCF1-446C-A3D3-D6ED7B625E38 Q33263145-B1575CE3-3D73-4A15-A1AA-CB6817DDF221 Q33289084-B7CDB4DA-88B8-4A14-9BCB-CE0B9B9FD2FC Q33312344-552A750D-1266-4449-82C3-42BE2EF1A1D9

P2860

Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer

http://www.wikidata.org/entity/Q28260830

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Structure and mechanism of BRC ...... 1 with implications for cancer

@ast

Structure and mechanism of BRC ...... 1 with implications for cancer

@en

Structure and mechanism of BRC ...... 1 with implications for cancer

@nl

type

label

Structure and mechanism of BRC ...... 1 with implications for cancer

@ast

Structure and mechanism of BRC ...... 1 with implications for cancer

@en

Structure and mechanism of BRC ...... 1 with implications for cancer

@nl

prefLabel

Structure and mechanism of BRC ...... 1 with implications for cancer

@ast

Structure and mechanism of BRC ...... 1 with implications for cancer

@en

Structure and mechanism of BRC ...... 1 with implications for cancer

@nl

P1433

Q28260830-3D858DFF-C98C-458D-BD55-CDFBDB0B6F28

P1476

Q28260830-F5425E9D-9FAF-4FE5-974B-015FB93EADDB

P2093

Q28260830-32F4A3A1-B55D-4A7F-957E-5A43CF08B0C8

Q28260830-67125A7F-75BC-4EF0-AD23-4ADDB746A23B

Q28260830-949CECB3-E681-4E04-8130-775B2992E545

Q28260830-9526CDD0-D9E3-428E-8442-AA688A9346A8

Q28260830-BC1E7C49-1854-4371-A3D3-044E6FAD0B96

Q28260830-C181D998-9289-4BC8-AAD6-B64E3DD1E5D6

P2860

Q28260830-0E729311-690A-4F43-8279-C7C74B687139

Q28260830-254E0EF3-A66C-44CA-A1C6-76ED8AD49244

Q28260830-259187B1-7DBD-485F-87A1-270150FDE36B

Q28260830-28218537-43C2-48FE-B945-64727B56708F

Q28260830-2D5D1E53-213A-486E-B85E-0F7871D22CC8

Q28260830-2E944195-2619-44DD-9778-F5FE4A0DC3B0

Q28260830-35EC87F4-12F8-4325-87D4-EA9C816AB5C4

Q28260830-3651DBF5-8F6A-402F-A14D-6691EE4CF9FB

Q28260830-3BCCC485-D011-4E22-A4CB-B2CA5C09672F

Q28260830-3E510DB8-93FF-4060-AA72-37631E423E63

P2888

Q28260830-23ABD68A-2F67-4A19-9589-13EC18CE068A

P304

Q28260830-86BDE966-0342-4F17-A70A-6B069DFE4E19

P31

Q28260830-A9D93242-D965-48FA-B94B-FC3C4A77A6A7

P3181

Q28260830-57EFC9D4-6FED-4E1D-A2F4-3E9356170CB1

P356

Q28260830-790A964B-EAD5-4A4D-BAB7-4614BFB1B779

P407

Q28260830-7276827B-11EB-45B1-9573-88CF14634243

P433

Q28260830-14F20735-B15A-4218-B7BA-53481385C257

P478

Q28260830-91FF244A-7811-4E59-81D1-51806F63393E

P50

Q28260830-0C539170-10B3-4A26-A531-5CA1C4613E67

P577

Q28260830-E827C488-C873-4D62-8570-07875FF9E3C5

P698

Q28260830-D0696A2E-2A64-4E5E-9588-AB33E037E79D

P921

Q28260830-A9F3BC01-19FA-4440-A0D4-2803DF88D4F3

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

Structure and mechanism of BRC ...... 1 with implications for cancer

@en

P2093

Drew M Lowery

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

Isaac A Manke

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

Julie A Clapperton

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

Lesley F Haire

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

Michael B Yaffe

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

Timmy Ho

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

P2860

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure

The BRCT domain is a phospho-protein binding domain

Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor.

The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations

The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1

Structural consequences of a cancer-causing BRCA1-BRCT missense mutation

The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain

P2888

P304

512-8

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

P31

scholarly article

P3181

2963137

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

P356

10.1038/NSMB775

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

P407

P433

6

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

P478

11

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

P50

Stephen J Smerdon

P577

2004-06-01T00:00:00Z

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

P698

15133502

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

P921

phosphorylation