Eldin, S., Forget, A.L., Lindenmuth, D. M., Logan, K. M. and Knight, K.L. (2000).
Mutations in the N-terminal region of RecA that disrupt the stability of free protein oligomers but not RecA-DNA complexes.
J. Mol. Biol. 299, 91-101.

DeZutter, J.A.K., Forget, A.L., Logan, K.M. and Knight, K.L. (2001).
Phe217 regulates allosteric information transfer across the subunit interface of the RecA protein filament.
Structure 9, 47-55.

Ranatunga, W., Jackson, D., Lloyd, J.A., Forget, A.L., Flowers II, R.A., Knight, K.L. and Borgstahl, G.E.O. (2001).
The human Rad52 protein has two modes of self-association.
J. Biol. Chem. 276, 15876-15880.

Logan, K.M., Forget, A.L., Verderese, J.P. and Knight, K.L. (2001).
ATP-mediated changes in cross-subunit interactions in the RecA protein.
Biochemistry 40, 11382-11389.

Lloyd, J.A., Forget, A.L. and Knight, K.L. (2002).
Correlation of oligomeric properties with the oligomeric state of human Rad52 protein.
J. Biol. Chem. 277, 46172-46178.

Forget, A.L., Bennett, B.T. and Knight, K.L. (2004).
Xrcc3 is recruited to DNA double strand breaks early and independent of Rad51. 
J Cell. Biochem. 93, 429-436.

Forget, A.L., Banfill, M., McGrew, D.A., Calmann, M., Schiffer, C. and Knight, K.L. (2006)
RecA dimers serve as a functional unit for assembly of active nucleoprotein filaments.
Biochemistry 45(45), 13537-13542.

Forget, A.L., Loftus, M.S., McGrew, D.A., Bennett, B.T. and Knight, K.L. (2007)
The Human Rad51 K133A Mutant is Functional for DNA Double-Strand Break Repair in Human Cells.
Biochemistry 46(11), 3566-3575.

Forget. A.L. and Kowalczykowski, S.C. (2010)
Single-molecule imaging brings Rad51 nucleoprotein filaments into focus.
Trends in Cell Biology, 20, 269-276 (published online March 17, 2010, as doi:10.1016/j.tcb.2010.02.004). PMID: 20299221; PMCID: PMC2862779 [Abstract] [Full Text] [PDF]
(see Trends in Cell Biology - Most Read Articles [PDF])

Forget, A.L. and Kowalczykowski, S.C. (2012)
Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search.
Nature, 482, 423–427 (published online February 8, 2012, doi:10.1038/nature10782). PMID: 22318518; PMCID: PMC3288143 [Abstract] [Full Text] [PDF] [Supplementary Information] [Supplementary Movie 1] [Supplementary Movie 2] [Supplementary Movie 3]
(see Biocompare, Life Sciences Articles, News: How DNA finds its match [PDF])
(see biotic-blog: How DNA finds its match [PDF])
(see California Aggie: Protein plays DNA matchmaker role [PDF])
(see Cancer-z blogspot: How DNA finds its match [PDF])
(see Cell.com News: UC Davis study shows how DNA finds its match [PDF])
(see Crop Biotech Update: How DNA finds its match [PDF])
(see Current Biology Dispatch: Homologous Recombination: How RecA Finds the Perfect Partner [PDF])
(see EurekAlert: How DNA finds its match [PDF])
(see InvestigaMedicina.com: El proceso de recombinación ha sido una incógnita desde el descubrimiento del ADN [PDF])
(see National Cancer Institute News: UC Davis study shows how DNA finds its match [PDF])
(see Nikon Instruments Research Papers: New insights into DNA repair  [PDF])
(see Phys.Org News: Study shows how DNA finds its match [PDF])
(see ScienceDaily: How DNA finds it match [PDF])
(see UC Davis News and Information: How DNA finds its match [PDF])
(see YouTube video: Scientists show DNA matchup [Video])

Forget, A.L., Dombrowski, C.C., Amitani, I., and Kowalczykowski, S.C. (2013)
Exploring protein-DNA interactions in 3D using in situ construction, manipulation, and visualization of individual DNA dumbbells with optical traps, microfluidics, and fluorescence microscopy.
Nature Protocols, 8, 525-538. PMID: 23411634; PMCID: PMC4329291. [Abstract] [Full Text] [PDF] [Supplementary Figure 1]

Rad, B., Forget, A.L., Baskin, R.J., and Kowalczykowski, S.C. (2015)
Single-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding.
Proc. Natl. Acad. Sci. USA 112, E6852-6861 (published online November 4, 2015 as doi: 10.1073/pnas.1518028112). PMID: 26540728; PMCID: PMC4687592. [Abstract] [Full Text] [PDF] [Supporting Information]