BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting
By Isaac A. Manke, Drew M. Lowery, Anhco Nguyen, Michael B. Yaffe. Science, 2003
700 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/bd7ba46a8f56390b6e0da94df64a9d187041eb12
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In Genetics
In Molecular Biology
- Vladimir N Uversky
- A. Keith Dunker
- Christopher J. Oldfield
- Stephen P. Jackson
- J. Bartek
- S. Polo
- Lukasz Kurgan
- T. Stracker
Citations in the corpus
- Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005, background): “encodes two tandem copies of a BRCA1 C-terminal (BRCT) domain (Manke et al., 2003).”
- The MRE11 complex: starting from the ends (2011, background): “FHA and tandem BRCT domains generally function as 'stand-alone' phosphopeptide-binding domain”
- RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. (2007, background): “Thus, it appears that the pThr-binding FHA domain of RNF8 has evolved to bind to similar motifs as those recognized by the BRCT domains of the foci-forming proteins BRCA1 and MDC1.”
- Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. (2011, background): “Indeed, PTIP focus formation is BRCT-dependent (Manke et al. 2003), suggesting a requirement for phosphorylation, while, as described further below, 53BP1 recruitment depends on its ability to bind methylated histone residues (Huyen et al.”
- Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1 (2021, background): “Close examination of the data in these papers suggests some recruitment for a construct without the C-terminal pair, but all four being required for a robust recruitment or interaction, placing Ser-25 of 53BP1 as a candidate for interaction with BRCT4 of PTIP.”
- Cell-cycle checkpoints and cancer (2004, background): “Interestingly, the BRCT domains have recently been shown to serve as protein-phosphoprotein-binding module”