EFI - Training Resources: Publications

5 US Patents

1.
US2019/0144798A1, Cleaning composition. The Procter & Gamble Company, Cincinnati, OH. May 16, 2019.
2.
US2019/0144801, Cleaning composition. The Procter & Gamble Company, Cincinnati, OH. May 16, 2019.
3.
US2019/0194599A1, Methods for generating a bacterial hemoglobin library and uses thereof. Zymergen, Inc., Emeryville, CA. June 27, 2019.
4.
US2019/0209625A1, Engineering therapeutic probiotic system and method. National University of Singapore, Singapore. July 11, 2019.
5.
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

1.
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
2.
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
3.
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
4.
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
5.
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
6.
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
7.
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
8.
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
9.
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
10.
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
11.
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
12.
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
13.
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
14.
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
15.
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.
16.
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
17.
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
18.
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
19.
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
20.
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
21.
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
22.
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
23.
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
24.
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
25.
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
26.
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
27.
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
28.
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
29.
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
30.
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
31.
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
32.
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
33.
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
34.
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
35.
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
36.
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
37.
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
38.
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
39.
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
40.
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
41.
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
42.
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
43.
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
44.
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
45.
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
46.
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
47.
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
48.
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
49.
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
50.
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
51.
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
52.
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
53.
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
54.
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
55.
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
56.
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
57.
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
58.
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
59.
Glasner, M.E., Finding enzymes in the gut metagenome. Science, 2017. 355(6325): p. 577–578. http://doi.org/10.1126/science.aam7446
60.
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
61.
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
62.
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
63.
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
64.
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
65.
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
66.
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
67.
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
68.
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
69.
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
70.
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
71.
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
72.
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
73.
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
74.
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
75.
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
76.
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
77.
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
78.
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
79.
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