Insights into DNA recombination from the structure of a RAD51–BRCA2 complex

By L. Pellegrini, David S. Yu, Thomas Lo, Shubha Anand, Miyoung Lee, Tom L. Blundell, A. Venkitaraman. Nature, 2002

730 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/193d3db2ab24e6a43b43d9c6bc6dd9f9d724e53b

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

In Molecular Biology

Citations in the corpus

BRCA1 and BRCA2: different roles in a common pathway of genome protection (2011, background): “The BRC repeats have subtle differences in sequence and bind RAD51 with varying affinity by mimicking the structure of RAD51 monomer”
The role of double-strand break repair — insights from human genetics (2006, background): “RAD51, a central player in HR, is loaded onto ssDNA and promotes strand invasion, with BRCA2 having a role in delivering RAD51 to the DN”
Current approaches for the fitting and refinement of atomic models into cryo-EM maps using CCP-EM (2018, methodology): “External restraints were generated by ProSMART using a homologous structural model derived using MX (PDB entry 1n0w; Pellegrini et al. , 2002) as a reference.”
Molecular views of recombination proteins and their control (2003, background): “A partial structure has also been gained by crystallographic analysis of a segment of RAD51 (Ref”
The roles of BRCA1 and BRCA2 and associated proteins in the maintenance of genomic stability (2006, background): “How this was mediated at the molecular level was clarified in a paper describing the crystallographic structure of a RAD51-BRC4 complex (Pellegrini et al., 2002).”
Homologous recombination and human health: the roles of BRCA1, BRCA2 and associated proteins (2015, background): “Point mutations in BRC repeats that impair RAD51 interaction are found in breast cancer patients (Pellegrini et al. 2002), although functional studies 10 Cite this article as Cold Spring Harb Perspect Biol 2015;7:a016600 are required to determine the effects of these mutations in full-length BRCA2.”
RAD51 and Breast Cancer Susceptibility: No Evidence for Rare Variant Association in the Breast Cancer Family Registry Study (2012, background): “Pellegrini et al (2002) reported the structure of the complex between the BRC repeat and the RecA-homology domain of RAD51 and concluded that the BRC repeat mimics a motif in RAD51 enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strandpairing reacti”
Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis (2010, neutral): “Structure determinations of one repeat, BRC4, have identified two distinct modules within a 33-amino acid peptide that contribute to RAD51 bindin”