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Items: 1 to 20 of 103


Using a fragment-based approach to target protein-protein interactions.

Scott DE, Ehebauer MT, Pukala T, Marsh M, Blundell TL, Venkitaraman AR, Abell C, Hyvönen M.

Chembiochem. 2013 Feb 11;14(3):332-42. doi: 10.1002/cbic.201200521. Epub 2013 Jan 23.


Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases.

Scott DE, Coyne AG, Venkitaraman A, Blundell TL, Abell C, Hyvönen M.

ChemMedChem. 2015 Feb;10(2):296-303. doi: 10.1002/cmdc.201402428. Epub 2014 Dec 2.


Engineering Archeal Surrogate Systems for the Development of Protein-Protein Interaction Inhibitors against Human RAD51.

Moschetti T, Sharpe T, Fischer G, Marsh ME, Ng HK, Morgan M, Scott DE, Blundell TL, R Venkitaraman A, Skidmore J, Abell C, Hyvönen M.

J Mol Biol. 2016 Nov 20;428(23):4589-4607. doi: 10.1016/j.jmb.2016.10.009. Epub 2016 Oct 8.


Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2.

Shin DS, Pellegrini L, Daniels DS, Yelent B, Craig L, Bates D, Yu DS, Shivji MK, Hitomi C, Arvai AS, Volkmann N, Tsuruta H, Blundell TL, Venkitaraman AR, Tainer JA.

EMBO J. 2003 Sep 1;22(17):4566-76.


Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction.

Scott DE, Marsh M, Blundell TL, Abell C, Hyvönen M.

FEBS Lett. 2016 Apr;590(8):1094-102. doi: 10.1002/1873-3468.12139. Epub 2016 Apr 6.


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

Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR.

Nature. 2002 Nov 21;420(6913):287-93. Epub 2002 Nov 10.


Integrated biophysical approach to fragment screening and validation for fragment-based lead discovery.

Silvestre HL, Blundell TL, Abell C, Ciulli A.

Proc Natl Acad Sci U S A. 2013 Aug 6;110(32):12984-9. doi: 10.1073/pnas.1304045110. Epub 2013 Jul 19.


Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity.

Chang YW, Ko TP, Lee CD, Chang YC, Lin KA, Chang CS, Wang AH, Wang TF.

PLoS One. 2009;4(3):e4890. doi: 10.1371/journal.pone.0004890. Epub 2009 Mar 19.


New insights into the biological function of BRCA2 from its structural interactions.

Waterworth A.

Breast Cancer Res. 2003;5(2):107-8. Epub 2003 Feb 4. No abstract available.


Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and Dss1.

Dray E, Siaud N, Dubois E, Doutriaux MP.

Plant Physiol. 2006 Mar;140(3):1059-69. Epub 2006 Jan 13.


Interrogation of the protein-protein interactions between human BRCA2 BRC repeats and RAD51 reveals atomistic determinants of affinity.

Cole DJ, Rajendra E, Roberts-Thomson M, Hardwick B, McKenzie GJ, Payne MC, Venkitaraman AR, Skylaris CK.

PLoS Comput Biol. 2011 Jul;7(7):e1002096. doi: 10.1371/journal.pcbi.1002096. Epub 2011 Jul 14.


Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair.

Park JY, Singh TR, Nassar N, Zhang F, Freund M, Hanenberg H, Meetei AR, Andreassen PR.

Oncogene. 2014 Oct 2;33(40):4803-12. doi: 10.1038/onc.2013.421. Epub 2013 Oct 21.


A variant of the breast cancer type 2 susceptibility protein (BRC) repeat is essential for the RECQL5 helicase to interact with RAD51 recombinase for genome stabilization.

Islam MN, Paquet N, Fox D 3rd, Dray E, Zheng XF, Klein H, Sung P, Wang W.

J Biol Chem. 2012 Jul 6;287(28):23808-18. doi: 10.1074/jbc.M112.375014. Epub 2012 May 29.


Two modules in the BRC repeats of BRCA2 mediate structural and functional interactions with the RAD51 recombinase.

Rajendra E, Venkitaraman AR.

Nucleic Acids Res. 2010 Jan;38(1):82-96. doi: 10.1093/nar/gkp873. Epub 2009 Oct 29.


Molecular mimicry connects BRCA2 to Rad51 and recombinational DNA repair.

Kowalczykowski SC.

Nat Struct Biol. 2002 Dec;9(12):897-9. No abstract available.


RAD51-associated protein 1 (RAD51AP1) interacts with the meiotic recombinase DMC1 through a conserved motif.

Dunlop MH, Dray E, Zhao W, Tsai MS, Wiese C, Schild D, Sung P.

J Biol Chem. 2011 Oct 28;286(43):37328-34. doi: 10.1074/jbc.M111.290015. Epub 2011 Sep 8.


An integrated in silico approach to analyze the involvement of single amino acid polymorphisms in FANCD1/BRCA2-PALB2 and FANCD1/BRCA2-RAD51 complex.

Doss CG, Nagasundaram N.

Cell Biochem Biophys. 2014 Nov;70(2):939-56. doi: 10.1007/s12013-014-0002-9.


RecA family proteins in archaea: RadA and its cousins.

Haldenby S, White MF, Allers T.

Biochem Soc Trans. 2009 Feb;37(Pt 1):102-7. doi: 10.1042/BST0370102.


The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity.

Galkin VE, Wu Y, Zhang XP, Qian X, He Y, Yu X, Heyer WD, Luo Y, Egelman EH.

Structure. 2006 Jun;14(6):983-92.


Biophysical screening for the discovery of small-molecule ligands.

Ciulli A.

Methods Mol Biol. 2013;1008:357-88. doi: 10.1007/978-1-62703-398-5_13.

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