Lei Shi, Ph.D.
Molecular Targets and Medications Discovery Branch, Computational Chemistry and Molecular Biophysics Unit
Triad Technology Center
333 Cassell Drive
Baltimore, MD 21224
Lee KH, Fant AD, Guo J, Guan A, Jung J, Kudaibergenova M, Miranda WE, Ku T, Cao J, Wacker S, Duff HJ, Newman AH, Noskov SY, Shi L. Toward Reducing hERG Affinities for DAT Inhibitors with a Combined Machine Learning and Molecular Modeling Approach. J Chem Inf Model. 2021.
Lane JR, Abramyan AM, Adhikari P, Keen AC, Lee KH, Sanchez J, Verma RK, Lim HD, Yano H, Javitch JA, Shi L. Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism. Elife. 2020;9.
Abramyan AM, Yano H, Xu M, Liu L, Naing S, Fant AD, Shi L. The Glu102 mutation disrupts higher-order oligomerization of the sigma 1 receptor. Comput Struct Biotechnol J. 2020;18:199-206.
Abramyan AM, Slack RD, Meena S, Davis BA, Newman AH, Singh SK, Shi L. Computation-guided analysis of paroxetine binding to hSERT reveals functionally important structural elements and dynamics. Neuropharmacology. 2019;161:107411.
Verma RK, Abramyan AM, Michino M, Free RB, Sibley DR, Javitch JA, Lane JR, Shi L. The E2.65A mutation disrupts dynamic binding poses of SB269652 at the dopamine D2 and D3 receptors. PLoS Comput Biol. 2018;14(1):e1005948.
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This page was last updated on August 25th, 2021