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Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells.

Liu N, Schild D, Thelen MP, Thompson LH.

Nucleic Acids Res. 2002 Feb 15;30(4):1009-15.


Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells.

Wiese C, Collins DW, Albala JS, Thompson LH, Kronenberg A, Schild D.

Nucleic Acids Res. 2002 Feb 15;30(4):1001-8.


Evidence for simultaneous protein interactions between human Rad51 paralogs.

Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ.

J Biol Chem. 2000 Jun 2;275(22):16443-9.


RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51.

Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS.

J Biol Chem. 2002 Mar 8;277(10):8406-11. Epub 2001 Dec 13.


Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro.

Lio YC, Mazin AV, Kowalczykowski SC, Chen DJ.

J Biol Chem. 2003 Jan 24;278(4):2469-78. Epub 2002 Nov 8.


Role of RAD51C and XRCC3 in genetic recombination and DNA repair.

Liu Y, Tarsounas M, O'regan P, West SC.

J Biol Chem. 2007 Jan 19;282(3):1973-9. Epub 2006 Nov 17.


Domain mapping of the Rad51 paralog protein complexes.

Miller KA, Sawicka D, Barsky D, Albala JS.

Nucleic Acids Res. 2004 Jan 2;32(1):169-78. Print 2004.


Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination.

Wiese C, Hinz JM, Tebbs RS, Nham PB, Urbin SS, Collins DW, Thompson LH, Schild D.

Nucleic Acids Res. 2006 May 22;34(9):2833-43. Print 2006.


Interplay between human DNA repair proteins at a unique double-strand break in vivo.

Rodrigue A, Lafrance M, Gauthier MC, McDonald D, Hendzel M, West SC, Jasin M, Masson JY.

EMBO J. 2006 Jan 11;25(1):222-31. Epub 2006 Jan 5.


Complex formation by the human RAD51C and XRCC3 recombination repair proteins.

Masson JY, Stasiak AZ, Stasiak A, Benson FE, West SC.

Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8440-6.


Functional characterization and identification of mouse Rad51d splice variants.

Gruver AM, Yard BD, McInnes C, Rajesh C, Pittman DL.

BMC Mol Biol. 2009 Mar 27;10:27. doi: 10.1186/1471-2199-10-27.


The Arabidopsis RAD51 paralogs RAD51B, RAD51D and XRCC2 play partially redundant roles in somatic DNA repair and gene regulation.

Wang Y, Xiao R, Wang H, Cheng Z, Li W, Zhu G, Wang Y, Ma H.

New Phytol. 2014 Jan;201(1):292-304. doi: 10.1111/nph.12498. Epub 2013 Sep 18.


Identification and purification of two distinct complexes containing the five RAD51 paralogs.

Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC.

Genes Dev. 2001 Dec 15;15(24):3296-307.


Human Rad51C deficiency destabilizes XRCC3, impairs recombination, and radiosensitizes S/G2-phase cells.

Lio YC, Schild D, Brenneman MA, Redpath JL, Chen DJ.

J Biol Chem. 2004 Oct 1;279(40):42313-20. Epub 2004 Jul 29.


Xrcc3 is recruited to DNA double strand breaks early and independent of Rad51.

Forget AL, Bennett BT, Knight KL.

J Cell Biochem. 2004 Oct 15;93(3):429-36.


XRCC3 ATPase activity is required for normal XRCC3-Rad51C complex dynamics and homologous recombination.

Yamada NA, Hinz JM, Kopf VL, Segalle KD, Thompson LH.

J Biol Chem. 2004 May 28;279(22):23250-4. Epub 2004 Mar 22.


Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex.

Kurumizaka H, Ikawa S, Nakada M, Enomoto R, Kagawa W, Kinebuchi T, Yamazoe M, Yokoyama S, Shibata T.

J Biol Chem. 2002 Apr 19;277(16):14315-20. Epub 2002 Feb 7.


A hot spot for RAD51C interactions revealed by a peptide that sensitizes cells to cisplatin.

Connell PP, Siddiqui N, Hoffman S, Kuang A, Khatipov EA, Weichselbaum RR, Bishop DK.

Cancer Res. 2004 May 1;64(9):3002-5.


Differential and collaborative actions of Rad51 paralog proteins in cellular response to DNA damage.

Yonetani Y, Hochegger H, Sonoda E, Shinya S, Yoshikawa H, Takeda S, Yamazoe M.

Nucleic Acids Res. 2005 Aug 10;33(14):4544-52. Print 2005.


RAD51, XRCC3, and XRCC2 mutation screening in Finnish breast cancer families.

Pelttari LM, Kiiski JI, Ranta S, Vilske S, Blomqvist C, Aittomäki K, Nevanlinna H.

Springerplus. 2015 Feb 24;4:92. doi: 10.1186/s40064-015-0880-3. eCollection 2015.

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