Mohamad A. Abbani, Ph.D.

molecular basis of bacterial pathogenesis

Robert T. Clubb	grad student	2006	UCLA
(Structural basis for directionality control of tyrosine recombinase-mediated DNA rearrangements.)
Parag Kumar Mallick	post-doc	2007-2009	UCLA

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Abbani MA, Papagiannis CV, Sam MD, et al. (2007) Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly. Proceedings of the National Academy of Sciences of the United States of America. 104: 2109-14
Papagiannis CV, Sam MD, Abbani MA, et al. (2007) Fis targets assembly of the Xis nucleoprotein filament to promote excisive recombination by phage lambda. Journal of Molecular Biology. 367: 328-43
Sam MD, Abbani MA, Cascio D, et al. (2006) Crystallization, dehydration and preliminary X-ray analysis of excisionase (Xis) proteins cooperatively bound to DNA. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 825-8
Abbani M, Iwahara M, Clubb RT. (2005) The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases. Journal of Molecular Biology. 347: 11-25
Warren D, Sam MD, Manley K, et al. (2003) Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. Proceedings of the National Academy of Sciences of the United States of America. 100: 8176-81