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Biochemistry|August 12, 2015
Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1Min Luo, John J TannerJournal of Molecular Biology|June 11, 2013
Structural determinants of oligomerization of δ(1)-pyrroline-5-carboxylate dehydrogenase: identification of a hexamerization hot spotMin Luo, Ranjan K Singh, John J TannerACS Chemical Biology|January 3, 2015
Diethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1Min Luo, Kent S Gates, Michael T Henzl, et al.The Journal of Biological Chemistry|December 11, 2014
First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactionsNikhilesh Sanyal, Benjamin W Arentson, Min Luo, et al.Biochemistry|November 16, 2012
Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product releaseMin Luo, Benjamin W Arentson, Dhiraj Srivastava, et al.Biochemistry|July 22, 2014
Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization ABenjamin W Arentson, Min Luo, Travis A Pemberton, et al.The FEBS Journal|July 16, 2017
Biophysical investigation of type A PutAs reveals a conserved core oligomeric structureDavid A Korasick, Harkewal Singh, Travis A Pemberton, et al.Biochemistry|August 20, 2014
Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channelingMin Luo, Shelbi Christgen, Nikhilesh Sanyal, et al.The Journal of Biological Chemistry|September 29, 2016
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown FunctionMin Luo, Thameesha T Gamage, Benjamin W Arentson, et al.Biochemistry|April 27, 2026
Structural Principles of Covalent Flavin Modification in OxidoreductasesJohn J TannerPageof 173