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The EMBO Journal|February 16, 2018
Regulation of Hed1 and Rad54 binding during maturation of the meiosis-specific presynaptic complexJ Brooks Crickard, Kyle Kaniecki, YoungHo Kwon, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 12, 2012
Single-molecule imaging of DNA curtains reveals mechanisms of KOPS sequence targeting by the DNA translocase FtsKJa Yil Lee, Ilya J Finkelstein, Estelle Crozat, et al.
Nucleic Acids Research|March 28, 2019
The RecQ helicase Sgs1 drives ATP-dependent disruption of Rad51 filamentsJ Brooks Crickard, Chaoyou Xue, Weibin Wang, et al.
Astrobiology|October 2, 2023
Solid-State Single-Molecule Sensing with the Electronic Life-Detection Instrument for Enceladus/Europa (ELIE)Christopher E Carr, José L Ramírez-Colón, Daniel Duzdevich, et al.
Cell Reports|October 19, 2017
Yeast Srs2 Helicase Promotes Redistribution of Single-Stranded DNA-Bound RPA and Rad52 in Homologous Recombination RegulationLuisina De Tullio, Kyle Kaniecki, Youngho Kwon, et al.
The Journal of Biological Chemistry|May 7, 2017
Sequence imperfections and base triplet recognition by the Rad51/RecA family of recombinasesJa Yil Lee, Justin B Steinfeld, Zhi Qi, et al.
Molecular Cell|January 9, 2021
The Rad51 paralog complex Rad55-Rad57 acts as a molecular chaperone during homologous recombinationUpasana Roy, Youngho Kwon, Lea Marie, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 20, 2019
Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resectionNing Jia, Mihaela C Unciuleac, Chaoyou Xue, et al.
Cell Reports|January 5, 2017
Telomere Recognition and Assembly Mechanism of Mammalian ShelterinFabian Erdel, Katja Kratz, Smaranda Willcox, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 10, 2021
Clutch mechanism of chemomechanical coupling in a DNA resecting motor nucleaseMihaela-Carmen Unciuleac, Aviv Meir, Chaoyou Xue, et al.
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