Liliana M. Sampaleanu, Ph.D.

Affiliations: 
2003 University of Toronto, Toronto, ON, Canada 
Area:
Biochemistry
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"Liliana Sampaleanu"
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Parents

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P. Lynne Howell grad student 2003 University of Toronto
 (Using duck delta1 and delta2 crystallin to investigate the enzymatic mechanism of argininosuccinate lyase.)
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Publications

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Leighton TL, Dayalani N, Sampaleanu LM, et al. (2015) Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex Mutations. Journal of Bacteriology. 197: 2229-38
Tammam S, Sampaleanu LM, Koo J, et al. (2013) PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA. Journal of Bacteriology. 195: 2126-35
Tammam S, Sampaleanu LM, Koo J, et al. (2011) Characterization of the PilN, PilO and PilP type IVa pilus subcomplex. Molecular Microbiology. 82: 1496-514
Sampaleanu LM, Bonanno JB, Ayers M, et al. (2009) Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex. Journal of Molecular Biology. 394: 143-59
Ayers M, Sampaleanu LM, Tammam S, et al. (2009) PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin. Journal of Molecular Biology. 394: 128-42
Koo J, Tammam S, Ku SY, et al. (2008) PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin. Journal of Bacteriology. 190: 6961-9
Chiang P, Sampaleanu LM, Ayers M, et al. (2008) Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU. Microbiology (Reading, England). 154: 114-26
Tsai M, Sampaleanu LM, Greene C, et al. (2004) A duck delta1 crystallin double loop mutant provides insight into residues important for argininosuccinate lyase activity. Biochemistry. 43: 11672-82
Sampaleanu LM, Codding PW, Lobsanov YD, et al. (2004) Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis. The Biochemical Journal. 384: 437-47
Sampaleanu LM, Yu B, Howell PL. (2002) Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase. The Journal of Biological Chemistry. 277: 4166-75
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