J
Jessica P. Lao
Researcher at University of California, Davis
Publications - 13
Citations - 987
Jessica P. Lao is an academic researcher from University of California, Davis. The author has contributed to research in topics: Homologous recombination & Congenital disorder of glycosylation. The author has an hindex of 9, co-authored 13 publications receiving 890 citations. Previous affiliations of Jessica P. Lao include Howard Hughes Medical Institute & University of California.
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Journal ArticleDOI
BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules.
TL;DR: It is proposed that differential activity of Sgs1 and procrossover factors at the two DSB ends effects productive formation of dHJs and crossovers and prevents multichromatid JMs and counterproductive crossing-over.
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RecQ Helicase, Sgs1, and XPF Family Endonuclease, Mus81-Mms4, Resolve Aberrant Joint Molecules during Meiotic Recombination
TL;DR: It is concluded that Sgs1 and Mus81-Mms4 collaborate to eliminate aberrant JMs, whereas as-yet-unidentified enzymes process normal JMs.
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Meiotic crossover control by concerted action of Rad51-Dmc1 in homolog template bias and robust homeostatic regulation.
Jessica P. Lao,Veronica Cloud,Chu Chun Huang,Jennifer Grubb,Drew Thacker,Chih Ying Lee,Michael E. Dresser,Neil Hunter,Douglas K. Bishop +8 more
TL;DR: In this paper, the authors show that Rad51-mediated meiotic recombination is not subject to regulatory processes associated with high-fidelity chromosome segregation, such as homolog bias, a process that directs strand exchange between homologs rather than sister chromatids.
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Rad52 Promotes Postinvasion Steps of Meiotic Double-Strand-Break Repair
TL;DR: It is revealed that Rad52 promotes postinvasion steps of both crossover and noncrossover pathways of meiotic recombination in Saccharomyces cerevisiae and suggests a general annealing mechanism for reuniting DSB ends during recombination.
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A new protein complex promoting the assembly of Rad51 filaments
Hiroyuki Sasanuma,Maki S. Tawaramoto,Jessica P. Lao,Harumi Hosaka,Eri Sanda,Mamoru Suzuki,Eiki Yamashita,Neil Hunter,Miki Shinohara,Atsushi Nakagawa,Akira Shinohara +10 more
TL;DR: A novel molecular mechanism for this class of Rad51-mediators, which includes the human Rad51 paralogues, is revealed, which is inferred by the high-resolution crystal structure, which reveals Psy3-Csm2 to be a structural mimic of the Rad 51-dimer, a fundamental unit of theRad51-filament.