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The University of Alabama at Birmingham
 
 
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Publications

1.            Li, T., C.L. Weaver, J. Lin, E.C. Duran, J.M. Miller, and A.L. Lucius, E. coli ClpB is a Non-Processive Polypeptide Translocase. 2015.
2.            Li, T., J. Lin, and A.L. Lucius, Examination of polypeptide substrate specificity for Escherichia coli ClpB. Proteins, 2015. 83(1): p. 117-34.
3.            Miller, J.M. and A.L. Lucius, ATP-gamma-S Competes with ATP for Binding at Domain 1 but not Domain 2 during ClpA Catalyzed Polypeptide Translocation. Biophys Chem, 2014. 185: p. 58-69.
4.            Fancy, R.M., L. Wang, T. Napier, J. Lin, G. Jing, A.L. Lucius, J.M. McDonald, T. Zhou, and Y. Song, Characterization of calmodulin-Fas death domain interaction: an integrated experimental and computational study. Biochemistry, 2014. 53(16): p. 2680-8.
5.            Miller, J.M., J. Lin, T. Li, and A.L. Lucius, E. coli ClpA Catalyzed Polypeptide Translocation is Allosterically Controlled by the Protease ClpP. Journal of Molecular Biology, 2013. 425(15): p. 2795-2812.
6.            Li, T. and A.L. Lucius, Examination of Polypeptide Substrate Specificity for E. coli ClpA. Biochemistry, 2013. 52: p. 4941-4954.
7.            Lucius, A.L., P.K. Veronese, and R.P. Stafford, Dynamic light scattering to study allosteric regulation. Methods in molecular biology, 2012. 796: p. 175-86.
8.            Veronese, P.K., B. Rajendar, and A.L. Lucius, Activity of Escherichia coli ClpA Bound by Nucleoside Di- and Triphosphates. Journal of molecular biology, 2011. 409(3): p. 333-47.
9.            Sheff, J.T., A.L. Lucius, S.B. Owens, and G.M. Gray, Generally Applicable NMR Titration Methods for the Determination of Equilibrium Constants for Coordination Complexes: Syntheses and Characterizations of Metallacrown Ethers with α,ω-Bis(phosphite)-polyether Ligands and Determination of Equilibrium Binding Constants to Li+. Organometallics, 2011. 30(21): p. 5695-5709.
10.          Lucius, A.L., J.M. Miller, and B. Rajendar, Application of the Sequential n-Step Kinetic Mechanism to Polypeptide Translocases. Methods Enzymol, 2011. 488: p. 239-64.
11.          Veronese, P.K. and A.L. Lucius, Effect of Temperature on the Self-Assembly of the Escherichia coli ClpA Molecular Chaperone. Biochemistry, 2010. 49(45): p. 9820-9.
12.          Rajendar, B. and A.L. Lucius, Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase. J Mol Biol, 2010. 399(5): p. 665-79.
13.          McClure, C.P. and A.L. Lucius, Implementing and Evaluating a Chemistry Course in Chemical Ethics and Civic Responsibility. Journal of Chemical Education, 2010. 87(11): p. 1171-1175.
14.          Chenna, B.C., J.R. King, B.A. Shinkre, A.L. Glover, A.L. Lucius, and S.E. Velu, Synthesis and structure activity relationship studies of novel Staphylococcus aureus Sortase A inhibitors. Eur J Med Chem, 2010. 45(9): p. 3752-61.
15.          Veronese, P.K., R.P. Stafford, and A.L. Lucius, The Escherichia coli ClpA Molecular Chaperone Self-Assembles into Tetramers. Biochemistry, 2009. 48(39): p. 9221-9233.
16.          Chenna, B.C., B.A. Shinkre, J.R. King, A.L. Lucius, S.V. Narayana, and S.E. Velu, Identification of novel inhibitors of bacterial surface enzyme Staphylococcus aureus Sortase A. Bioorg Med Chem Lett, 2008. 18(1): p. 380-5.
17.          Lucius, A.L., M.J. Jezewska, A. Roychowdhury, and W. Bujalowski, Kinetic Mechanisms of the Nucleotide Cofactor Binding to the Strong and Weak Nucleotide-Binding Site of the Escherichia coli PriA Helicase. 2. Biochemistry, 2006. 45(23): p. 7217-7236.
18.          Lucius, A.L., M.J. Jezewska, and W. Bujalowski, The Escherichia coli PriA Helicase Has Two Nucleotide-Binding Sites Differing Dramatically in Their Affinities for Nucleotide Cofactors. 1. Intrinsic Affinities, Cooperativities, and Base Specificity of Nucleotide Cofactor Binding. Biochemistry, 2006. 45(23): p. 7202-7216.
19.          Lucius, A.L., M.J. Jezewska, and W. Bujalowski, Allosteric Interactions between the Nucleotide-Binding Sites and the ssDNA-Binding Site in the PriA Helicase-ssDNA Complex. 3. Biochemistry, 2006. 45(23): p. 7237-7255.
20.          Jezewska, M.J., A. Marcinowicz, A.L. Lucius, and W. Bujalowski, DNA polymerase X from African swine fever virus: quantitative analysis of the enzyme-ssDNA interactions and the functional structure of the complex. J Mol Biol, 2006. 356(1): p. 121-41.
21.          Wong, C.J., A.L. Lucius, and T.M. Lohman, Energetics of DNA end binding by E.coli RecBC and RecBCD helicases indicate loop formation in the 3'-single-stranded DNA tail. J Mol Biol, 2005. 352(4): p. 765-82.
22.          Jezewska, M.J., A.L. Lucius, and W. Bujalowski, Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 1. Direct evidence of cooperative interactions between the nucleotide-binding sites of a hexameric helicase. Biochemistry, 2005. 44(10): p. 3865-76.
23.          Jezewska, M.J., A.L. Lucius, and W. Bujalowski, Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 2. Base specificity, nucleotide structure, magnesium, and salt effect on the cooperative binding of the cofactors. Biochemistry, 2005. 44(10): p. 3877-90.
24.          Jason Wong, C., A.L. Lucius, and T.M. Lohman, Energetics of DNA end binding by E.coli RecBC and RecBCD helicases indicate loop formation in the 3'-single-stranded DNA tail. J Mol Biol, 2005. 352(4): p. 765-82.
25.          Lucius, A.L., C.J. Wong, and T.M. Lohman, Fluorescence stopped-flow studies of single turnover kinetics of E.coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol, 2004. 339(4): p. 731-50.
26.          Lucius, A.L. and T.M. Lohman, Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol, 2004. 339(4): p. 751-71.
27.          Lucius, A.L., C. Jason Wong, and T.M. Lohman, Fluorescence stopped-flow studies of single turnover kinetics of E.coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol, 2004. 339(4): p. 731-50.
28.          Lucius, A.L., N.K. Maluf, C.J. Fischer, and T.M. Lohman, General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophys J, 2003. 85(4): p. 2224-39.
29.          Lucius, A.L., A. Vindigni, R. Gregorian, J.A. Ali, A.F. Taylor, G.R. Smith, and T.M. Lohman, DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies. J Mol Biol, 2002. 324(3): p. 409-28.