EFI - Training Resources: Publications

5 US Patents

US2019/0144798A1, Cleaning composition. The Procter & Gamble Company, Cincinnati, OH. May 16, 2019.
US2019/0144801, Cleaning composition. The Procter & Gamble Company, Cincinnati, OH. May 16, 2019.
US2019/0194599A1, Methods for generating a bacterial hemoglobin library and uses thereof. Zymergen, Inc., Emeryville, CA. June 27, 2019.
US2019/0209625A1, Engineering therapeutic probiotic system and method. National University of Singapore, Singapore. July 11, 2019.
US2019/0225663A1, Discovery of cationic nonribosomal peptides as gram-negative antibiotics through global genome mining. Hong Kong University of Science and Technology, China Ocean Mineral Resources R&D Association, Hong Kong CN. July 25, 2019.

288 Journal Articles

Dunbar, K.L., J.R. Chekan, C.L. Cox, B.J. Burkhart, S.K. Nair, D.A. Mitchell, Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Nature Chemical Biology, 2014. 10(10): p. 823–829. http://doi.org/10.1038/nchembio.1608
Wichelecki, D.J., B.M. Balthazor, A.C. Chau, M.W. Vetting, A.A. Fedorov, E.V. Fedorov, T. Lukk, Y.V. Patskovsky, M.B. Stead, B.S. Hillerich, R.D. Seidel, S.C. Almo, J.A. Gerlt, Discovery of Function in the Enolase Superfamily: D-Mannonate and D-Gluconate Dehydratases in the D-Mannonate Dehydratase Subgroup. Biochemistry, 2014. 53(16): p. 2722–2731. http://doi.org/10.1021/bi500264p
Wichelecki, D.J., D.C. Graff, N. Al-Obaidi, S.C. Almo, J.A. Gerlt, Identification of the in Vivo Function of the High-Efficiency D-Mannonate Dehydratase in Caulobacter crescentus NA1000 from the Enolase Superfamily. Biochemistry, 2014. 53(25): p. 4087–4089. http://doi.org/10.1021/bi500683x
Anders, K., L.-O. Essen, The family of phytochrome-like photoreceptors: diverse, complex and multi-colored, but very useful. Current Opinion in Structural Biology, 2015. 35: p. 7–16. http://doi.org/10.1016/j.sbi.2015.07.005
Burkhart, B.J., G.A. Hudson, K.L. Dunbar, D.A. Mitchell, A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nature Chemical Biology, 2015. 11(8): p. 564–570. http://doi.org/10.1038/nchembio.1856
Celis, A.I., J.L. DuBois, Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme. Archives of Biochemistry and Biophysics, 2015. 574: p. 3–17. http://doi.org/10.1016/j.abb.2015.03.004
Colin, P.-Y., B. Kintses, F. Gielen, C.M. Miton, G. Fischer, M.F. Mohamed, M. Hyvönen, D.P. Morgavi, D.B. Janssen, F. Hollfelder, Ultrahigh-throughput discovery of promiscuous enzymes by picodroplet functional metagenomics. Nature Communications, 2015. 6(1):. http://doi.org/10.1038/ncomms10008
Cox, C.L., J.R. Doroghazi, D.A. Mitchell, The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles. BMC Genomics, 2015. 16(1):. http://doi.org/10.1186/s12864-015-2008-0
Huang, H., M.S. Carter, M.W. Vetting, N. Al-Obaidi, Y. Patskovsky, S.C. Almo, J.A. Gerlt, A General Strategy for the Discovery of Metabolic Pathways: D-Threitol, L-Threitol, and Erythritol Utilization in Mycobacterium smegmatis. Journal of the American Chemical Society, 2015. 137(46): p. 14570–14573. http://doi.org/10.1021/jacs.5b08968
Latham, J.A., A.T. Iavarone, I. Barr, P.V. Juthani, J.P. Klinman, PqqD Is a Novel Peptide Chaperone That Forms a Ternary Complex with the Radical S-Adenosylmethionine Protein PqqE in the Pyrroloquinoline Quinone Biosynthetic Pathway. Journal of Biological Chemistry, 2015. 290(20): p. 12908–12918. http://doi.org/10.1074/jbc.m115.646521
Liu, F., J. Geng, R.H. Gumpper, A. Barman, I. Davis, A. Ozarowski, D. Hamelberg, A. Liu, An Iron Reservoir to the Catalytic Metal. Journal of Biological Chemistry, 2015. 290(25): p. 15621–15634. http://doi.org/10.1074/jbc.m115.650259
Petronikolou, N., S.K. Nair, Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel. Chemistry & Biology, 2015. 22(11): p. 1480–1490. http://doi.org/10.1016/j.chembiol.2015.09.011
Rao, G., B. O'Dowd, J. Li, K. Wang, E. Oldfield, IspH–RPS1 and IspH–UbiA: "Rosetta stone" proteins. Chemical Science, 2015. 6(12): p. 6813–6822. http://doi.org/10.1039/c5sc02600h
Roche, D., D. Brackenridge, L. McGuffin, Proteins and Their Interacting Partners: An Introduction to Protein–Ligand Binding Site Prediction Methods. International Journal of Molecular Sciences, 2015. 16(12): p. 29829–29842. http://doi.org/10.3390/ijms161226202
San Francisco, B., X. Zhang, K. Whalen, J. Gerlt, A Novel Pathway for Bacterial Ethanolamine Metabolism. The FASEB Journal, 2015. 29(1_supplement): p. 573.45.
Vetting, M.W., N. Al-Obaidi, S. Zhao, B. San Francisco, J. Kim, D.J. Wichelecki, J.T. Bouvier, J.O. Solbiati, H. Vu, X. Zhang, D.A. Rodionov, J.D. Love, B.S. Hillerich, R.D. Seidel, R.J. Quinn, A.L. Osterman, J.E. Cronan, M.P. Jacobson, J.A. Gerlt, S.C. Almo, Experimental Strategies for Functional Annotation and Metabolism Discovery: Targeted Screening of Solute Binding Proteins and Unbiased Panning of Metabolomes. Biochemistry, 2015. 54(3): p. 909–931. http://doi.org/10.1021/bi501388y
Wichelecki, D.J., M.W. Vetting, L. Chou, N. Al-Obaidi, J.T. Bouvier, S.C. Almo, J.A. Gerlt, ATP-binding Cassette (ABC) Transport System Solute-binding Protein-guided Identification of Novel D-Altritol and Galactitol Catabolic Pathways in Agrobacterium tumefaciens C58. Journal of Biological Chemistry, 2015. 290(48): p. 28963–28976. http://doi.org/10.1074/jbc.m115.686857
Zhang, X., R. Kumar, M.W. Vetting, S. Zhao, M.P. Jacobson, S.C. Almo, J.A. Gerlt, A Unique cis-3-Hydroxy-L-proline Dehydratase in the Enolase Superfamily. Journal of the American Chemical Society, 2015. 137(4): p. 1388–1391. http://doi.org/10.1021/ja5103986
Ahmed, F.H., A.E. Mohamed, P.D. Carr, B.M. Lee, K. Condic-Jurkic, M.L. O'Mara, C.J. Jackson, Rv2074 is a novel F420H2-dependent biliverdin reductase in Mycobacterium tuberculosis. Protein Science, 2016. 25(9): p. 1692–1709. http://doi.org/10.1002/pro.2975
Atkinson, J.T., I. Campbell, G.N. Bennett, J.J. Silberg, Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways. Biochemistry, 2016. 55(51): p. 7047–7064. http://doi.org/10.1021/acs.biochem.6b00831
Baier, F., J.N. Copp, N. Tokuriki, Evolution of Enzyme Superfamilies: Comprehensive Exploration of Sequence–Function Relationships. Biochemistry, 2016. 55(46): p. 6375–6388. http://doi.org/10.1021/acs.biochem.6b00723
Bhandari, D.M., D. Fedoseyenko, T.P. Begley, Tryptophan Lyase (NosL): A Cornucopia of 5′-Deoxyadenosyl Radical Mediated Transformations. Journal of the American Chemical Society, 2016. 138(50): p. 16184–16187. http://doi.org/10.1021/jacs.6b06139
Chekan, J.R., J.D. Koos, C. Zong, M.O. Maksimov, A.J. Link, S.K. Nair, Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates. Journal of the American Chemical Society, 2016. 138(50): p. 16452–16458. http://doi.org/10.1021/jacs.6b10389
Colabroy, K.L., Tearing down to build up: Metalloenzymes in the biosynthesis lincomycin, hormaomycin and the pyrrolo [1,4]benzodiazepines. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2016. 1864(6): p. 724–737. http://doi.org/10.1016/j.bbapap.2016.03.001
Dassama, L.M.K., G.E. Kenney, S.Y. Ro, E.L. Zielazinski, A.C. Rosenzweig, Methanobactin transport machinery. Proceedings of the National Academy of Sciences, 2016. 113(46): p. 13027–13032. http://doi.org/10.1073/pnas.1603578113
Davey, L., S.A. Halperin, S.F. Lee, Thiol-Disulfide Exchange in Gram-Positive Firmicutes. Trends in Microbiology, 2016. 24(11): p. 902–915. http://doi.org/10.1016/j.tim.2016.06.010
Desai, J., Y.-L. Liu, H. Wei, W. Liu, T.-P. Ko, R.-T. Guo, E. Oldfield, Structure, Function, and Inhibition of Staphylococcus aureus Heptaprenyl Diphosphate Synthase. ChemMedChem, 2016. 11(17): p. 1915–1923. http://doi.org/10.1002/cmdc.201600311
Ding, W., Q. Li, Y. Jia, X. Ji, H. Qianzhu, Q. Zhang, Emerging Diversity of the Cobalamin-Dependent Methyltransferases Involving Radical-Based Mechanisms. ChemBioChem, 2016. 17(13): p. 1191–1197. http://doi.org/10.1002/cbic.201600107
Gerlt, J.A., Tools and strategies for discovering novel enzymes and metabolic pathways. Perspectives in Science, 2016. 9: p. 24–32. http://doi.org/10.1016/j.pisc.2016.07.001
Ghodge, S.V., K.A. Biernat, S.J. Bassett, M.R. Redinbo, A.A. Bowers, Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A. Journal of the American Chemical Society, 2016. 138(17): p. 5487–5490. http://doi.org/10.1021/jacs.5b13529
Hao, Y., E. Pierce, D. Roe, M. Morita, J.A. McIntosh, V. Agarwal, T.E. Cheatham, E.W. Schmidt, S.K. Nair, Molecular basis for the broad substrate selectivity of a peptide prenyltransferase. Proceedings of the National Academy of Sciences, 2016. 113(49): p. 14037–14042. http://doi.org/10.1073/pnas.1609869113
Tietz, J.I., D.A. Mitchell, Using Genomics for Natural Product Structure Elucidation. Current Topics in Medicinal Chemistry, 2016. 16(15): p. 1645–1694. http://doi.org/10.2174/1568026616666151012111439
Ji, X., Y. Li, L. Xie, H. Lu, W. Ding, Q. Zhang, Expanding Radical SAM Chemistry by Using Radical Addition Reactions and SAM Analogues. Angewandte Chemie International Edition, 2016. 55(39): p. 11845–11848. http://doi.org/10.1002/anie.201605917
Ji, X., W.-Q. Liu, S. Yuan, Y. Yin, W. Ding, Q. Zhang, Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions. Chemical Communications, 2016. 52(69): p. 10555–10558. http://doi.org/10.1039/c6cc05661j
Kumar, G., J.L. Johnson, P.A. Frantom, Improving Functional Annotation in the DRE-TIM Metallolyase Superfamily through Identification of Active Site Fingerprints. Biochemistry, 2016. 55(12): p. 1863–1872. http://doi.org/10.1021/acs.biochem.5b01193
Li, D., R. Moorman, T. Vanhercke, J. Petrie, S. Singh, C.J. Jackson, Classification and substrate head-group specificity of membrane fatty acid desaturases. Computational and Structural Biotechnology Journal, 2016. 14: p. 341–349. http://doi.org/10.1016/j.csbj.2016.08.003
Machovina, M.M., R.J. Usselman, J.L. DuBois, Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations. Journal of Biological Chemistry, 2016. 291(34): p. 17816–17828. http://doi.org/10.1074/jbc.m116.730051
Maxson, T., J.I. Tietz, G.A. Hudson, X.R. Guo, H.-C. Tai, D.A. Mitchell, Targeting Reactive Carbonyls for Identifying Natural Products and Their Biosynthetic Origins. Journal of the American Chemical Society, 2016. 138(46): p. 15157–15166. http://doi.org/10.1021/jacs.6b06848
Molloy, E.M., J.I. Tietz, P.M. Blair, D.A. Mitchell, Biological characterization of the hygrobafilomycin antibiotic JBIR-100 and bioinformatic insights into the hygrolide family of natural products. Bioorganic & Medicinal Chemistry, 2016. 24(24): p. 6276–6290. http://doi.org/10.1016/j.bmc.2016.05.021
Plach, M.G., B. Reisinger, R. Sterner, R. Merkl, Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation. PLOS Genetics, 2016. 12(1): p. e1005836. http://doi.org/10.1371/journal.pgen.1005836
Prunetti, L., B.E. Yacoubi, C.R. Schiavon, E. Kirkpatrick, L. Huang, M. Bailly, M.E. Badawi-Sidhu, K. Harrison, J.F. Gregory, O. Fiehn, A.D. Hanson, V. de Crécy-Lagard, Evidence that COG0325 proteins are involved in PLP homeostasis. Microbiology, 2016. 162(4): p. 694–706. http://doi.org/10.1099/mic.0.000255
Rao, G., E. Oldfield, Structure and Function of Four Classes of the 4Fe–4S Protein, IspH. Biochemistry, 2016. 55(29): p. 4119–4129. http://doi.org/10.1021/acs.biochem.6b00474
Thotsaporn, K., R. Tinikul, S. Maenpuen, J. Phonbuppha, P. Watthaisong, P. Chenprakhon, P. Chaiyen, Enzymes in the p-hydroxyphenylacetate degradation pathway of Acinetobacter baumannii. Journal of Molecular Catalysis B: Enzymatic, 2016. 134: p. 353–366. http://doi.org/10.1016/j.molcatb.2016.09.003
Zallot, R., K. Harrison, B. Kolaczkowski, V. de Crécy-Lagard, Functional Annotations of Paralogs: A Blessing and a Curse. Life, 2016. 6(3): p. 39. http://doi.org/10.3390/life6030039
Zhang, X., M.S. Carter, M.W. Vetting, B. San Francisco, S. Zhao, N.F. Al-Obaidi, J.O. Solbiati, J.J. Thiaville, V. de Crécy-Lagard, M.P. Jacobson, S.C. Almo, J.A. Gerlt, Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proceedings of the National Academy of Sciences, 2016. 113(29): p. E4161–E4169. http://doi.org/10.1073/pnas.1605546113
Ahmed, M.N., E. Reyna-González, B. Schmid, V. Wiebach, R.D. Süssmuth, E. Dittmann, D.P. Fewer, Phylogenomic Analysis of the Microviridin Biosynthetic Pathway Coupled with Targeted Chemo-Enzymatic Synthesis Yields Potent Protease Inhibitors. ACS Chemical Biology, 2017. 12(6): p. 1538–1546. http://doi.org/10.1021/acschembio.7b00124
Bearne, S.L., The interdigitating loop of the enolase superfamily as a specificity binding determinant or `flying buttress'. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2017. 1865(5): p. 619–630. http://doi.org/10.1016/j.bbapap.2017.02.006
Benjdia, A., A. Guillot, P. Ruffié, J. Leprince, O. Berteau, Post-translational modification of ribosomally synthesized peptides by a radical SAM epimerase in Bacillus subtilis. Nature Chemistry, 2017. 9(7): p. 698–707. http://doi.org/10.1038/nchem.2714
Blin, K., T. Wolf, M.G. Chevrette, X. Lu, C.J. Schwalen, S.A. Kautsar, H.G.S. Duran, E.L.C. de los Santos, H.U. Kim, M. Nave, J.S. Dickschat, D.A. Mitchell, E. Shelest, R. Breitling, E. Takano, S.Y. Lee, T. Weber, M.H. Medema, antiSMASH 4.0—improvements in chemistry prediction and gene cluster boundary identification. Nucleic Acids Research, 2017. 45(W1): p. W36–W41. http://doi.org/10.1093/nar/gkx319
Chowdhary, J., F.E. Löffler, J.C. Smith, Community detection in sequence similarity networks based on attribute clustering. PLOS ONE, 2017. 12(7): p. e0178650. http://doi.org/10.1371/journal.pone.0178650
Cogan, D.P., G.A. Hudson, Z. Zhang, T.V. Pogorelov, W.A. van der Donk, D.A. Mitchell, S.K. Nair, Structural insights into enzymatic [4+2] aza-cycloaddition in thiopeptide antibiotic biosynthesis. Proceedings of the National Academy of Sciences, 2017. 114(49): p. 12928–12933. http://doi.org/10.1073/pnas.1716035114
Ding, W., W. Ji, Y. Wu, R. Wu, W.-Q. Liu, T. Mo, J. Zhao, X. Ma, W. Zhang, P. Xu, Z. Deng, B. Tang, Y. Yu, Q. Zhang, Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ. Nature Communications, 2017. 8(1):. http://doi.org/10.1038/s41467-017-00439-1
Dong, S.-H., N.D. Frane, Q.H. Christensen, E.P. Greenberg, R. Nagarajan, S.K. Nair, Molecular basis for the substrate specificity of quorum signal synthases. Proceedings of the National Academy of Sciences, 2017. 114(34): p. 9092–9097. http://doi.org/10.1073/pnas.1705400114
Erb, T.J., P.R. Jones, A. Bar-Even, Synthetic metabolism: metabolic engineering meets enzyme design. Current Opinion in Chemical Biology, 2017. 37: p. 56–62. http://doi.org/10.1016/j.cbpa.2016.12.023
Essen, L.-O., S. Franz, A. Banerjee, Structural and evolutionary aspects of algal blue light receptors of the cryptochrome and aureochrome type. Journal of Plant Physiology, 2017. 217: p. 27–37. http://doi.org/10.1016/j.jplph.2017.07.005
Estrada, P., M. Manandhar, S.-H. Dong, J. Deveryshetty, V. Agarwal, J.E. Cronan, S.K. Nair, The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes. Nature Chemical Biology, 2017. 13(6): p. 668–674. http://doi.org/10.1038/nchembio.2359
Gerlt, J.A., Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence–Function Space and Genome Context to Discover Novel Functions. Biochemistry, 2017. 56(33): p. 4293–4308. http://doi.org/10.1021/acs.biochem.7b00614
Giessen, T.W., P.A. Silver, Widespread distribution of encapsulin nanocompartments reveals functional diversity. Nature Microbiology, 2017. 2(6):. http://doi.org/10.1038/nmicrobiol.2017.29
Glasner, M.E., Finding enzymes in the gut metagenome. Science, 2017. 355(6325): p. 577–578. http://doi.org/10.1126/science.aam7446
Grim, K.P., B. San Francisco, J.N. Radin, E.B. Brazel, J.L. Kelliher, P.K.P. Solórzano, P.C. Kim, C.A. McDevitt, T.E. Kehl-Fie, The Metallophore Staphylopine Enables Staphylococcus aureus To Compete with the Host for Zinc and Overcome Nutritional Immunity. mBio, 2017. 8(5):. http://doi.org/10.1128/mbio.01281-17
Haase, E.M., Y. Kou, A. Sabharwal, Y.-C. Liao, T. Lan, C. Lindqvist, F.A. Scannapieco, Comparative genomics and evolution of the amylase-binding proteins of oral streptococci. BMC Microbiology, 2017. 17(1):. http://doi.org/10.1186/s12866-017-1005-7
Hetrick, K.J., W.A. van der Donk, Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era. Current Opinion in Chemical Biology, 2017. 38: p. 36–44. http://doi.org/10.1016/j.cbpa.2017.02.005
Holliday, G.L., S.D. Brown, E. Akiva, D. Mischel, M.A. Hicks, J.H. Morris, C.C. Huang, E.C. Meng, S.C. Pegg, T.E. Ferrin, P.C. Babbitt, Biocuration in the structure–function linkage database: the anatomy of a superfamily. Database, 2017. 2017:. http://doi.org/10.1093/database/bax006
Holliday, G.L., R. Davidson, E. Akiva, P.C. Babbitt, Evaluating Functional Annotations of Enzymes Using the Gene Ontology. Methods in Molecular Biology, 2016. http://doi.org/10.1007/978-1-4939-3743-1_9
Hopkins, D.H., N.J. Fraser, P.D. Mabbitt, P.D. Carr, J.G. Oakeshott, C.J. Jackson, Structure of an Insecticide Sequestering Carboxylesterase from the Disease Vector Culex quinquefasciatus: What Makes an Enzyme a Good Insecticide Sponge?. Biochemistry, 2017. 56(41): p. 5512–5525. http://doi.org/10.1021/acs.biochem.7b00774
Jia, B., X. Jia, K.H. Kim, Z.J. Pu, M.-S. Kang, C.O. Jeon, Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway. Scientific Reports, 2017. 7(1):. http://doi.org/10.1038/srep43489
Jia, B., X. Jia, K.H. Kim, C.O. Jeon, Integrative view of 2-oxoglutarate/Fe(II)-dependent oxygenase diversity and functions in bacteria. Biochimica et Biophysica Acta (BBA) - General Subjects, 2017. 1861(2): p. 323–334. http://doi.org/10.1016/j.bbagen.2016.12.001
Jia, B., K. Tang, B.H. Chun, C.O. Jeon, Large-scale examination of functional and sequence diversity of 2-oxoglutarate/Fe(II)-dependent oxygenases in Metazoa. Biochimica et Biophysica Acta (BBA) - General Subjects, 2017. 1861(11): p. 2922–2933. http://doi.org/10.1016/j.bbagen.2017.08.019
Jia, B., X.F. Zhu, Z.J. Pu, Y.X. Duan, L.J. Hao, J. Zhang, L.-Q. Chen, C.O. Jeon, Y.H. Xuan, Integrative View of the Diversity and Evolution of SWEET and SemiSWEET Sugar Transporters. Frontiers in Plant Science, 2017. 8:. http://doi.org/10.3389/fpls.2017.02178
Kandlinger, F., M.G. Plach, R. Merkl, AGeNNT: annotation of enzyme families by means of refined neighborhood networks. BMC Bioinformatics, 2017. 18(1):. http://doi.org/10.1186/s12859-017-1689-6
Koppel, N., V.M. Rekdal, E.P. Balskus, Chemical transformation of xenobiotics by the human gut microbiota. Science, 2017. 356(6344): p. eaag2770. http://doi.org/10.1126/science.aag2770
Levin, B.J., Y.Y. Huang, S.C. Peck, Y. Wei, A.M. Campo, J.A. Marks, E.A. Franzosa, C. Huttenhower, E.P. Balskus, A prominent glycyl radical enzyme in human gut microbiomes metabolizestrans-4-hydroxy-L-proline. Science, 2017. 355(6325): p. eaai8386. http://doi.org/10.1126/science.aai8386
Liao, C., F.P. Seebeck, Convergent Evolution of Ergothioneine Biosynthesis in Cyanobacteria. ChemBioChem, 2017. 18(21): p. 2115–2118. http://doi.org/10.1002/cbic.201700354
Lohans, C.T., D.Y. Wang, J. Wang, R.B. Hamed, C.J. Schofield, Crotonases: Nature's Exceedingly Convertible Catalysts. ACS Catalysis, 2017. 7(10): p. 6587–6599. http://doi.org/10.1021/acscatal.7b01699
Macaisne, N., F. Liu, D. Scornet, A.F. Peters, A. Lipinska, M.-M. Perrineau, A. Henry, M. Strittmatter, S.M. Coelho, J.M. Cock, The Ectocarpus IMMEDIATE UPRIGHT gene encodes a member of a novel family of cysteine-rich proteins with an unusual distribution across the eukaryotes. Development, 2017. 144(3): p. 409–418. http://doi.org/10.1242/dev.141523
McFarland, B.J., Online Tools for Teaching Large Laboratory Courses: How the GENI Website Facilitates Authentic Research. ACS Symposium Series, 2017. http://doi.org/10.1021/bk-2017-1270.ch008
Ney, B., F.H. Ahmed, C.R. Carere, A. Biswas, A.C. Warden, S.E. Morales, G. Pandey, S.J. Watt, J.G. Oakeshott, M.C. Taylor, M.B. Stott, C.J. Jackson, C. Greening, The methanogenic redox cofactor F420 is widely synthesized by aerobic soil bacteria. The ISME Journal, 2016. 11(1): p. 125–137. http://doi.org/10.1038/ismej.2016.100
Ortega, M.A., D.P. Cogan, S. Mukherjee, N. Garg, B. Li, G.N. Thibodeaux, S.I. Maffioli, S. Donadio, M. Sosio, J. Escano, L. Smith, S.K. Nair, W.A. van der Donk, Two Flavoenzymes Catalyze the Post-Translational Generation of 5-Chlorotryptophan and 2-Aminovinyl-Cysteine during NAI-107 Biosynthesis. ACS Chemical Biology, 2017. 12(2): p. 548–557. http://doi.org/10.1021/acschembio.6b01031
Orth, C., N. Niemann, L. Hennig, L.-O. Essen, A. Batschauer, Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site. Journal of Biological Chemistry, 2017. 292(31): p. 12906–12920. http://doi.org/10.1074/jbc.m117.788869
Pimviriyakul, P., K. Thotsaporn, J. Sucharitakul, P. Chaiyen, Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA. Journal of Biological Chemistry, 2017. 292(12): p. 4818–4832. http://doi.org/10.1074/jbc.m116.774448
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