Stuart S. Licht, PhD - Related publications

Affiliations: 
2002-2008 Massachusetts Institute of Technology, Cambridge, MA, United States 
 2008-2010 Novartis, Basel, Basel-Stadt, France 
 2010- sanofi-aventis, St. Louis, MO, United States 
Website:
https://www.linkedin.com/pub/stuart-licht/7/57a/610
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50 most relevant papers in past 60 days:
Year Citation  Score
2020 Mamounis KJ, Yukl ET, Davidson VL. Roles of active site residues in catalysis, substrate binding, cooperativity and the reaction mechanism of the quinoprotein glycine oxidase. The Journal of Biological Chemistry. PMID 32234764 DOI: 10.1074/jbc.RA120.013198   
2020 Sun P, Bai T, Ma T, Ding J. Molecular mechanism of the dual regulatory roles of ATP on the αγ heterodimer of human NAD-dependent isocitrate dehydrogenase. Scientific Reports. 10: 6225. PMID 32277159 DOI: 10.1038/s41598-020-63425-6   
2020 Dockalova V, Sanchez-Carnerero EM, Dunajova Z, Palao E, Slanska M, Buryska T, Damborsky J, Klán P, Prokop Z. Fluorescent substrates for haloalkane dehalogenases: Novel probes for mechanistic studies and protein labeling. Computational and Structural Biotechnology Journal. 18: 922-932. PMID 32346465 DOI: 10.1016/j.csbj.2020.03.029   
2020 Kwon JH, Lee HJ, Escher BI. Bioavailability of hydrophobic organic chemicals on an in vitro metabolic transformation using rat liver S9 fraction. Toxicology in Vitro : An International Journal Published in Association With Bibra. 104835. PMID 32224166 DOI: 10.1016/j.tiv.2020.104835   
2020 Songsiriritthigul C, Narawongsanont R, Tantitadapitak C, Guan HH, Chen CJ. Structure-function study of AKR4C14, an aldo-keto reductase from Thai jasmine rice (Oryza sativa L. ssp. indica cv. KDML105). Acta Crystallographica. Section D, Structural Biology. 76: 472-483. PMID 32355043 DOI: 10.1107/S2059798320004313   
2020 Kari J, Schiano-di-Cola C, Hansen SF, Badino SF, Sørensen TH, Cavaleiro AM, Borch K, Westh P. A Steady-State Approach for inhibition of Heterogeneous Enzyme reactions. The Biochemical Journal. PMID 32391552 DOI: 10.1042/BCJ20200083   
2020 Takahashi RH, Grandner JM, Bobba S, Liu Y, Beroza P, Zhang D, Ma S. Novel Homodimer Metabolites of GDC-0994 via Cytochrome P450-Catalyzed Radical Coupling. Drug Metabolism and Disposition: the Biological Fate of Chemicals. PMID 32234735 DOI: 10.1124/dmd.119.090019   
2020 Hwang J, Jeong CS, Lee CW, Shin SC, Kim HW, Lee SG, Youn UJ, Lee CS, Oh TJ, Kim HJ, Park H, Park HH, Lee JH. Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase. Journal of Microbiology (Seoul, Korea). PMID 32323197 DOI: 10.1007/s12275-020-0089-1   
2020 Hotra A, Ragunathan P, Ng PS, Seankongsuk P, Harikishore A, Sarathy JP, Geok SW, Lakshmanan U, Sae-Lao P, Kalia NP, Shin J, Kalyanasundaram R, Anbarasu S, Parthasarathy K, Pradeep CN, et al. Discovery of a novel Mycobacterial F-ATP synthase inhibitor and its potency in combination with diarylquinolines. Angewandte Chemie (International Ed. in English). PMID 32337801 DOI: 10.1002/anie.202002546   
2020 Lang X, Hong X, Baker CA, Otto TC, Wheeldon I. Molecular Binding Scaffolds Increase Local Substrate Concentration Enhancing the Enzymatic Hydrolysis of VX Nerve Agent. Biotechnology and Bioengineering. PMID 32239488 DOI: 10.1002/bit.27346   
2020 Duff MR, Redzic JS, Ryan LP, Paukovich N, Zhao R, Nix JC, Pitts TM, Agarwal P, Eisenmesser EZ. Structure, dynamics, and function of the evolutionarily changing biliverdin reductase B family. Journal of Biochemistry. PMID 32246827 DOI: 10.1093/jb/mvaa039   
2020 Ortega Ugalde S, Wallraven K, Speer A, Bitter W, Grossmann TN, Commandeur JNM. Acetylene containing cyclo(L-Tyr-L-Tyr)-analogs as mechanism-based inhibitors of CYP121A1 from Mycobacterium tuberculosis. Biochemical Pharmacology. 177: 113938. PMID 32224137 DOI: 10.1016/j.bcp.2020.113938   
2020 Zhang X, Xu N, Li J, Ma Z, Wei L, Liu Q, Liu J. Engineering of L-glutamate oxidase as the whole-cell biocatalyst for the improvement of α-ketoglutarate production. Enzyme and Microbial Technology. 136: 109530. PMID 32331723 DOI: 10.1016/j.enzmictec.2020.109530   
2020 Wang H, He S, Deng W, Zhang Y, Li G, Sun J, Zhao W, Guo Y, Yin Z, Li D, Shang L. Comprehensive Insights into the Catalytic Mechanism of Middle East Respiratory Syndrome 3C-Like Protease and Severe Acute Respiratory Syndrome 3C-Like Protease. Acs Catalysis. 10: 5871-5890. PMID 32391184 DOI: 10.1021/acscatal.0c00110   
2020 Tsuji A, Akao T, Masuya T, Murai M, Miyoshi H. IACS-010759, a potent inhibitor of glycolysis-deficient hypoxic tumor cells, inhibits mitochondrial respiratory complex I through a unique mechanism. The Journal of Biological Chemistry. PMID 32295842 DOI: 10.1074/jbc.RA120.013366   
2020 Stockinger P, Roth S, Müller M, Pleiss J. Systematic Evaluation of Imine-Reducing Enzymes Common Principles in Imine Reductases, β-Hydroxyacid Dehydrogenases, and Short-Chain Dehydrogenases/Reductases. Chembiochem : a European Journal of Chemical Biology. PMID 32311225 DOI: 10.1002/cbic.202000213   
2020 Zhang J, Balsbaugh JL, Gao S, Ahn NG, Klinman JP. Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol -methyltransferase reaction. Proceedings of the National Academy of Sciences of the United States of America. PMID 32371482 DOI: 10.1073/pnas.1917219117   
2020 Fink T, Stevović B, Verwaal R, Roubos JA, Gaber R, Benčina M, Jerala R, Gradišar H. Metabolic enzyme clustering by coiled coils improves the biosynthesis of resveratrol and mevalonate. Amb Express. 10: 97. PMID 32448937 DOI: 10.1186/s13568-020-01031-5   
2020 Liu H, Wu S, Ran D, Xie W. Structure of a tRNA-specific deaminase with compromised deamination activity. The Biochemical Journal. PMID 32270856 DOI: 10.1042/BCJ20190858   
2020 Mindrebo JT, Patel A, Kim WE, Davis TD, Chen A, Bartholow TG, La Clair JJ, McCammon JA, Noel JP, Burkart MD. Gating mechanism of elongating β-ketoacyl-ACP synthases. Nature Communications. 11: 1727. PMID 32265440 DOI: 10.1038/s41467-020-15455-x   
2020 Go MK, Zhao LN, Xue B, Supekar S, Robinson RC, Fan H, Yew WS. Directed Computational Evolution of Quorum-Quenching Lactonases from the Amidohydrolase Superfamily. Structure (London, England : 1993). PMID 32320671 DOI: 10.1016/j.str.2020.03.011   
2020 Takehara S, Sakuraba S, Mikami B, Yoshida H, Yoshimura H, Itoh A, Endo M, Watanabe N, Nagae T, Matsuoka M, Ueguchi-Tanaka M. A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin. Nature Communications. 11: 2143. PMID 32358569 DOI: 10.1038/s41467-020-16068-0   
2020 Brown CA, Hu L, Sun Z, Patel MP, Singh S, Porter JR, Sankaran B, Prasad BVV, Bowman GR, Palzkill T. Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance. The Journal of Biological Chemistry. PMID 32299911 DOI: 10.1074/jbc.RA119.012489   
2020 Lubkowski J, Vanegas JM, Chan WK, Lorenzi PL, Weinstein JN, Sukharev S, Fushman D, Rempe S, Anishkin A, Wlodawer A. The mechanism of catalysis by L-asparaginase. Biochemistry. PMID 32364696 DOI: 10.1021/acs.biochem.0c00116   
2020 Lu C, Peng X, Lu D, Liu Z. Global and Kinetic Profiles of Substrate Diffusion in Lipase B: Molecular Dynamics with the Markov-State Model. Acs Omega. 5: 9806-9812. PMID 32391467 DOI: 10.1021/acsomega.9b04432   
2020 Tamman H, Van Nerom K, Takada H, Vandenberk N, Scholl D, Polikanov Y, Hofkens J, Talavera A, Hauryliuk V, Hendrix J, Garcia-Pino A. A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes. Nature Chemical Biology. PMID 32393900 DOI: 10.1038/s41589-020-0520-2   
2020 Hausman JM, Kenny S, Iyer S, Babar A, Qiu J, Fu J, Luo ZQ, Das C. The Two Deubiquitinating Enzymes from Have Distinct Ubiquitin Recognition Properties. Biochemistry. PMID 32275137 DOI: 10.1021/acs.biochem.9b01107   
2020 Dong CS, Zhang WL, Wang Q, Li YS, Wang X, Zhang M, Liu L. Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase. Proceedings of the National Academy of Sciences of the United States of America. PMID 32234783 DOI: 10.1073/pnas.1920244117   
2020 Maršavelski A, Sabljić I, Sugimori D, Kojić-Prodić B. The substrate selectivity of the two homologous SGNH hydrolases from Streptomyces bacteria: Molecular dynamics and experimental study. International Journal of Biological Macromolecules. PMID 32348859 DOI: 10.1016/j.ijbiomac.2020.04.198   
2020 Cristobal JR, Reyes AC, Richard JP. The Organization of Active Site Side Chains at Glycerol 3-Phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes. Biochemistry. PMID 32250105 DOI: 10.1021/acs.biochem.0c00175   
2020 Hammers DS, Donaghy CM, Heiss SL, Harris LM, Gordon JM, Stevens JW, Murray LP, Schwab AD, Hester BC, Culpepper MA. Identification and Characterization of a DmoB Flavin Oxidoreductase from a Putative Two-Component DMS -Monooxygenase. Acs Omega. 5: 9830-9838. PMID 32391470 DOI: 10.1021/acsomega.9b04489   
2020 Alaei L, Izadi Z, Jafari S, Jahanshahi F, Jaymand M, Mohammadi P, Paray BA, Hasan A, Falahati M, Shiri Varnamkhasti B, Saboury AA, Moosavi-Nejad Z, Sheikh-Hosseini M, Derakhshankhah H. Irreversible Thermal Inactivation and Conformational Lock of Alpha Glucosidase. Journal of Biomolecular Structure & Dynamics. 1-11. PMID 32345145 DOI: 10.1080/07391102.2020.1762742   
2020 Jiang HW, Chen Q, Pan J, Zheng GW, Xu JH. Rational Engineering of Formate Dehydrogenase Substrate/Cofactor Affinity for Better Performance in NADPH Regeneration. Applied Biochemistry and Biotechnology. PMID 32405732 DOI: 10.1007/s12010-020-03317-7   
2020 Unciuleac MC, Goldgur Y, Shuman S. Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation. Nucleic Acids Research. PMID 32315072 DOI: 10.1093/nar/gkaa238   
2020 Su L, Yao K, Wu J. Improved Activity of Maltooligosyltrehalose Synthase through Directed Evolution. Journal of Agricultural and Food Chemistry. PMID 32227942 DOI: 10.1021/acs.jafc.0c00948   
2020 Bashore C, Jaishankar P, Skelton NJ, Fuhrmann J, Hearn BR, Liu PS, Renslo AR, Dueber EC. Cyanopyrrolidine Inhibitors of Ubiquitin Specific Protease 7 Mediate Desulfhydration of the Active-Site Cysteine. Acs Chemical Biology. PMID 32302100 DOI: 10.1021/acschembio.0c00031   
2020 Burckhardt RM, Escalante-Semerena JC. Small-Molecule Acetylation by GCN5-Related -Acetyltransferases in Bacteria. Microbiology and Molecular Biology Reviews : Mmbr. 84. PMID 32295819 DOI: 10.1128/MMBR.00090-19   
2020 Beaumont V, Reiss K, Qu Z, Allen B, Batista VS, Loria JP. The allosteric impact of the variable insert loop in Vaccinia H1-related (VHR) phosphatase. Biochemistry. PMID 32348128 DOI: 10.1021/acs.biochem.0c00245   
2020 Caparco AA, Bommarius BR, Bommarius AS, Champion JA. Protein-Inorganic Calcium-Phosphate Supraparticles as a Robust Platform for Enzyme Co-Immobilization. Biotechnology and Bioengineering. PMID 32255509 DOI: 10.1002/bit.27348   
2020 Nguyen GT, Kim YG, Ahn JW, Chang JH. Structural Basis for Broad Substrate Selectivity of Alcohol Dehydrogenase YjgB from . Molecules (Basel, Switzerland). 25. PMID 32455802 DOI: 10.3390/molecules25102404   
2020 Zhu Y, Liang M, Li H, Ni H, Li L, Li Q, Jiang Z. A mutant of Pseudoalteromonas carrageenovora arylsulfatase with enhanced enzyme activity and its potential application in improvement of the agar quality. Food Chemistry. 320: 126652. PMID 32229399 DOI: 10.1016/j.foodchem.2020.126652   
2020 Pols T, Singh S, Deelman-Driessen C, Gaastra BF, Poolman B. Enzymology of the pathway for ATP production by arginine breakdown. The Febs Journal. PMID 32306469 DOI: 10.1111/febs.15337   
2020 Puvar K, Iyer S, Fu J, Kenny S, Negrón Terón KI, Luo ZQ, Brzovic PS, Klevit RE, Das C. Legionella effector MavC targets the Ube2N~Ub conjugate for noncanonical ubiquitination. Nature Communications. 11: 2365. PMID 32398758 DOI: 10.1038/s41467-020-16211-x   
2020 Deng X, Chen L, Hei M, Liu T, Feng Y, Yang G. Structure-guided reshaping of the acyl binding pocket of 'TesA thioesterase enhances octanoic acid production in E. coli. Metabolic Engineering. PMID 32339761 DOI: 10.1016/j.ymben.2020.04.010   
2020 Meghwanshi GK, Kaur N, Verma S, Dabi NK, Vashishtha A, Charan PD, Purohit P, Bhandari HS, Bhojak N, Kumar R. Enzymes for pharmaceutical and therapeutic applications. Biotechnology and Applied Biochemistry. PMID 32248597 DOI: 10.1002/bab.1919   
2020 Logeshwaran P, Krishnan K, Naidu R, Megharaj M. Purification and characterization of a novel fenamiphos hydrolysing enzyme from Microbacterium esteraromaticum MM1. Chemosphere. 252: 126549. PMID 32229357 DOI: 10.1016/j.chemosphere.2020.126549   
2020 Arya CK, Yadav S, Fine J, Casanal A, Chopra G, Ramanathan G, Vinothkumar KR, Subramanian R. A 2-Tyr-1-Carboxylate Mononuclear Iron Center is the Active Site of Dimethylformamidase. Angewandte Chemie (International Ed. in English). PMID 32452120 DOI: 10.1002/anie.202005332   
2020 Järvå MA, Dramicanin M, Lingford JP, Mao R, John A, Jarman KE, Grinter R, Goddard-Borger ED. Structural basis of substrate recognition and catalysis by fucosyltransferase 8. The Journal of Biological Chemistry. PMID 32220931 DOI: 10.1074/jbc.RA120.013291   
2020 Mintmier B, Nassif S, Stolz JF, Basu P. Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 32279136 DOI: 10.1007/s00775-020-01787-y   
2020 Usai R, Kaluka D, Mak PJ, Liu Y, Kincaid JR. Resonance Raman spectroscopic studies of peroxo and hydroperoxo intermediates in lauric acid (LA)-bound cytochrome P450 119. Journal of Inorganic Biochemistry. 208: 111084. PMID 32470906 DOI: 10.1016/j.jinorgbio.2020.111084