Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. - Test2 - elhamkhani - TriplyDB

Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

http://www.wikidata.org/entity/Q40557832

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Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4 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 STRUCTURE-FUNCTION OF THE TUMOR SUPPRESSOR BRCA1 Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains Functional Evolution of BRCT Domains from Binding DNA to Protein 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 The role of poly(ADP-ribosyl)ation in DNA damage response and cancer chemotherapy The dynamic organization of fungal acetyl-CoA carboxylase.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 Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair 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 γH2A binds Brc1 to maintain genome integrity during S-phase 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 Structural studies of the PARP-1 BRCT domain Molecular Basis for the Association of Microcephalin (MCPH1) Protein with the Cell Division Cycle Protein 27 (Cdc27) Subunit of the Anaphase-promoting Complex Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair Structural Insights into Recognition of MDC1 by TopBP1 in DNA Replication Checkpoint Control Phosphorylation-Dependent Assembly and Coordination of the DNA Damage Checkpoint Apparatus by Rad4TopBP1 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 Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics Functional impact of missense variants in BRCA1 predicted by supervised learning Characterization of Promiscuous Binding of Phosphor Ligands to Breast-Cancer-Gene 1 (BRCA1) C-Terminal (BRCT): Molecular Dynamics, Free Energy, Entropy and Inhibitor Design BRCT domains: A little more than kin, and less than kind Homologs of breast cancer genes in plants Assessment of human Nter and Cter BRCA1 mutations using growth and localization assays in yeast.

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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

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2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年论文

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2004年论文

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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

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Nature Structural & Molecular Biology

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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.

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P2093

D Duong Hau

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

J N Mark Glover

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Megan S Lee

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R Scott Williams

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P2860

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

Crystal structure of an Xrcc4-DNA ligase IV complex

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

Structure of an XRCC1 BRCT domain: a new protein-protein interaction module

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

BRCA1 interacts with components of the histone deacetylase 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

Solution structure and backbone dynamics of the human DNA ligase IIIalpha BRCT domain

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519-525

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10.1038/NSMB776

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6

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11

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2004-05-09T00:00:00Z

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8571377

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15133503

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