Aaron T. Smith
Affiliations: | University of Maryland, Baltimore County, Baltimore, MD, United States |
Area:
bioinorganic chemistry, structural biology, spectroscopyWebsite:
https://sites.google.com/a/umbc.edu/smithlab/Google:
"Aaron Smith"Mean distance: (not calculated yet)
Parents
Sign in to add mentorJudith N. Burstyn | grad student | 2007-2012 | UW Madison | |
(Spectral characterization of thiolate-mediated metalloporphyrin-protein interactions and their functional implications.) | ||||
Amy C. Rosenzweig | post-doc | 2012-2016 | Northwestern |
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Publications
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Brown JB, Lee MA, Smith AT. (2022) The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry |
Sestok AE, O'Sullivan SM, Smith AT. (2022) A general protocol for the expression and purification of the intact transmembrane transporter FeoB. Biochimica Et Biophysica Acta. Biomembranes. 1864: 183973 |
Sestok AE, Brown JB, Obi JO, et al. (2022) A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB. The Journal of Biological Chemistry. 101808 |
Smith AT, Linkous RO, Max NJ, et al. (2019) The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive. Biochemistry |
Linkous RO, Sestok AE, Smith AT. (2019) The Crystal Structure of Klebsiella pneumoniae FeoA Reveals A Site For Protein-Protein Interactions. Proteins |
Sestok AE, Linkous RO, Smith AT. (2018) Toward a mechanistic understanding of Feo-mediated ferrous iron uptake. Metallomics : Integrated Biometal Science |
Smith AT, Sestok AE. (2017) Expression and purification of functionally active ferrous iron transporter FeoB from Klebsiella pneumoniae. Protein Expression and Purification |
Smith AT, Ross MO, Hoffman BM, et al. (2016) Metal Selectivity of a Cd-, Co-, and Zn-Transporting P1B-type ATPase. Biochemistry |
Hines JP, Smith AT, Jacob JP, et al. (2016) CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry |
Kathman SG, Span I, Smith AT, et al. (2015) A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism. Journal of the American Chemical Society. 137: 12442-5 |