DNA Damage-Induced Cell Cycle Checkpoint Control Requires CtIP, a Phosphorylation-Dependent Binding Partner of BRCA1 C-Terminal Domains

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The BRCT Domain Is a Phospho-Protein Binding Domain

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BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

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The C-terminal (BRCT) Domains of BRCA1 Interact in Vivo with CtIP, a Protein Implicated in the CtBP Pathway of Transcriptional Repression

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Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response

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BRCA1 Supports XIST RNA Concentration on the Inactive X Chromosome

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A subset of ATM‐ and ATR‐dependent phosphorylation events requires the BRCA1 protein

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Binding of CtIP to the BRCT Repeats of BRCA1 Involved in the Transcription Regulation of p21 Is Disrupted Upon DNA Damage

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The human decatenation checkpoint

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Interaction between a Cellular Protein That Binds to the C-terminal Region of Adenovirus E1A (CtBP) and a Novel Cellular Protein Is Disrupted by E1A through a Conserved PLDLS Motif

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Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide

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Characterization of a carboxy-terminal BRCA1 interacting protein

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Nuclear Localization and Cell Cycle-specific Expression of CtIP, a Protein That Associates with the BRCA1 Tumor Suppressor

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Structural Basis of BACH1 Phosphopeptide Recognition by BRCA1 Tandem BRCT Domains

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Ataxia telangiectasia-related protein is involved in the phosphorylation of BRCA1 following deoxyribonucleic acid damage.

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Effect of DNA damage on a BRCA1 complex

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Human CtIP promotes DNA end resection

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Homologous Recombination and Human Health: The Roles of BRCA1, BRCA2, and Associated Proteins

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Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response

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CtIP Links DNA Double-Strand Break Sensing to Resection

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CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response

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Chapter 16 Chk1 and Chk2 as Checkpoint Targets

Zhang, H., Xiao, Z., & Sowin, T. (2009)

Chk1 and Chk2 as Checkpoint Targets

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