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Zhou, Y., Wei, Y., Nanjaraj Urs, A. N., Lin, L., Xu, T., Hu, Y., ... Zhang, Y. (2019). Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacterium Bifidobacterium kashiwanohense. Bioscience Reports, 39(6), [Y]. https://doi.org/10.1042/BSR20190715
Wei, Y., Tan, Y. L., Ang, E. L., & Zhao, H. (Accepted/In press). Identification and Characterization of Citrus Peel Uronic Acid Oxidase. ChemBioChem. https://doi.org/10.1002/cbic.201900546
Schlein, L. J., Fadl-Alla, B., Pondenis, H. C., Lezmi, S., Eberhart, C. G., LeBlanc, A. K., ... Fan, T. M. (2019). Immunohistochemical characterization of procaspase-3 overexpression as a druggable target with PAC-1, a procaspase-3 activator, in canine and human brain cancers. Frontiers in Oncology, 9(FEB), [96]. https://doi.org/10.3389/fonc.2019.00096
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Neumann, E. K., Ellis, J. F., Triplett, A. E., Rubakhin, S., & Sweedler, J. V. (2019). Lipid Analysis of 30 000 Individual Rodent Cerebellar Cells Using High-Resolution Mass Spectrometry. Analytical chemistry. https://doi.org/10.1021/acs.analchem.9b01689
Jijakli, K., & Jensen, P. A. (2019). Metabolic modeling of Streptococcus mutans reveals complex nutrient requirements of an oral pathogen. mSystems, 4(5), [e00529]. https://doi.org/10.1128/mSystems.00529-19
Nayak, D. D., & Metcalf, W. W. (2019). Methylamine-specific methyltransferase paralogs in Methanosarcina are functionally distinct despite frequent gene conversion. ISME Journal. https://doi.org/10.1038/s41396-019-0428-6
Chekan, J. R., Ongpipattanakul, C., Wright, T. R., Zhang, B., Martin Bollinger, J., Rajakovich, L. J., ... Nair, S. K. (2019). Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants. Proceedings of the National Academy of Sciences of the United States of America, 116(27), 13299-13304. https://doi.org/10.1073/pnas.1900711116
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Bouvier, J. T., Sernova, N. V., Ghasempur, S., Rodionova, I. A., Vetting, M. W., Al-Obaidi, N. F., ... Rodionov, D. A. (2019). Novel metabolic pathways and regulons for hexuronate utilization in Proteobacteria. Journal of bacteriology, 201(2), [e00431-18]. https://doi.org/10.1128/JB.00431-18
Acedo, J. Z., Bothwell, I. R., An, L., Trouth, A., Frazier, C., & Van Der Donk, W. A. (2019). O-Methyltransferase-Mediated Incorporation of a β-Amino Acid in Lanthipeptides. Journal of the American Chemical Society, 141(42), 16790-16801. https://doi.org/10.1021/jacs.9b07396
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Richter, M. F., & Hergenrother, P. J. (2019). The challenge of converting gram-positive-only compounds into broad-spectrum antibiotics. Annals of the New York Academy of Sciences, 1435(1), 18-38. https://doi.org/10.1111/nyas.13598
Bougioukou, D. J., Ting, C. P., Peck, S. C., Mukherjee, S., & van der Donk, W. A. (2019). Use of the dehydrophos biosynthetic enzymes to prepare antimicrobial analogs of alaphosphin. Organic and Biomolecular Chemistry, 17(4), 822-829. https://doi.org/10.1039/c8ob02860e
Jeon, S., Li, Q., Rubakhin, S., Sweedler, J. V., Smith, J. W., Neuringer, M., ... Erdman, J. W. (2019). 13C-lutein is differentially distributed in tissues of an adult female rhesus macaque following a single oral administration: a pilot study. Nutrition Research, 61, 102-108. https://doi.org/10.1016/j.nutres.2018.10.007
Howe, G. W., & van der Donk, W. A. (2018). 18 O Kinetic Isotope Effects Reveal an Associative Transition State for Phosphite Dehydrogenase Catalyzed Phosphoryl Transfer Journal of the American Chemical Society, 140(51), 17820-17824. https://doi.org/10.1021/jacs.8b06301
Rack, J. G. M., Ariza, A., Drown, B. S., Henfrey, C., Bartlett, E., Shirai, T., ... Ahel, I. (2018). (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition. Cell chemical biology, 25(12), 1533-1546.e12. https://doi.org/10.1016/j.chembiol.2018.11.001
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Reyes, A. C., Plache, D. C., Koudelka, A. P., Amyes, T. L., Gerlt, J. A., & Richard, J. P. (2018). Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5′-Monophosphate Decarboxylase for Catalysis. Journal of the American Chemical Society, 140(50), 17580-17590. https://doi.org/10.1021/jacs.8b09609
Jeong, H., Moye, L. S., Southey, B. R., Hernandez, A. G., Dripps, I., Romanova, E. V., ... Rodriguez-Zas, S. L. (2018). Gene network dysregulation in the trigeminal ganglia and nucleus accumbens of a model of chronic migraine-associated hyperalgesia. Frontiers in Systems Neuroscience, 12, [63]. https://doi.org/10.3389/fnsys.2018.00063
Singh, R. K., Singh, R., Sivakumar, D., Kondaveeti, S., Kim, T., Li, J., ... Lee, J. K. (2018). Insights into Cell-Free Conversion of CO2 to Chemicals by a Multienzyme Cascade Reaction. ACS Catalysis, 8(12), 11085-11093. https://doi.org/10.1021/acscatal.8b02646
Tapsin, S., Sun, M., Shen, Y., Zhang, H., Lim, X. N., Susanto, T. T., ... Wan, Y. (2018). Genome-wide identification of natural RNA aptamers in prokaryotes and eukaryotes. Nature communications, 9(1), [1289]. https://doi.org/10.1038/s41467-018-03675-1
Wang, K. K. A., Ng, T. L., Wang, P., Huang, Z., Balskus, E. P., & van der Donk, W. A. (2018). Glutamic acid is a carrier for hydrazine during the biosyntheses of fosfazinomycin and kinamycin. Nature communications, 9(1), [3687]. https://doi.org/10.1038/s41467-018-06083-7
Liu, D., Wei, Y., Liu, X., Zhou, Y., Jiang, L., Yin, J., ... Zhang, Y. (2018). Indoleacetate decarboxylase is a glycyl radical enzyme catalysing the formation of malodorant skatole. Nature communications, 9(1), [4224]. https://doi.org/10.1038/s41467-018-06627-x
Zhuo, Y., Choi, J. S., Marin, T., Yu, H., Harley, B. A., & Cunningham, B. T. (2018). Quantitative analysis of focal adhesion dynamics using photonic resonator outcoupler microscopy (PROM). Light: Science and Applications, 7(1), [7538]. https://doi.org/10.1038/s41377-018-0001-5
Cronan, J. E. (2018). Advances in synthesis of biotin and assembly of lipoic acid. Current Opinion in Chemical Biology, 47, 60-66. https://doi.org/10.1016/j.cbpa.2018.08.004
Zallot, R., Oberg, N. O., & Gerlt, J. A. (2018). ‘Democratized’ genomic enzymology web tools for functional assignment. Current Opinion in Chemical Biology, 47, 77-85. https://doi.org/10.1016/j.cbpa.2018.09.009
Gerlt, J. A., & Erb, T. J. (2018). Editorial overview: Novel enzymes, coenzymes, and metabolic pathways. Current Opinion in Chemical Biology, 47, A4-A6. https://doi.org/10.1016/j.cbpa.2018.11.008
Svec, R. L., Furiassi, L., Skibinski, C. G., Fan, T. M., Riggins, G. J., & Hergenrother, P. J. (2018). Tunable Stability of Imidazotetrazines Leads to a Potent Compound for Glioblastoma. ACS chemical biology, 13(11), 3206-3216. https://doi.org/10.1021/acschembio.8b00864
Svec, R. L., & Hergenrother, P. (2018). Oxygen Starvation Unmasks a Killer. Cell chemical biology, 25(11), 1313-1314. https://doi.org/10.1016/j.chembiol.2018.10.028
Haley, H. M. S., Hill, A. G., Greenwood, A. I., Woerly, E. M., Rienstra, C. M., & Burke, M. D. (2018). Peridinin Is an Exceptionally Potent and Membrane-Embedded Inhibitor of Bilayer Lipid Peroxidation. Journal of the American Chemical Society, 140(45), 15227-15240. https://doi.org/10.1021/jacs.8b06933
Sweedler, J. V. (2018). Science Research - Looking in the Mirror. Analytical chemistry, 90(21), 12323-12324. https://doi.org/10.1021/acs.analchem.8b04786
Rodriguez-Zas, S. L., Wu, C., Southey, B. R., O'Connor, J. C., Nixon, S. E., Garcia, R., ... Dantzer, R. (2018). Disruption of microglia histone acetylation and protein pathways in mice exhibiting inflammation-associated depression-like symptoms. Psychoneuroendocrinology, 97, 47-58. https://doi.org/10.1016/j.psyneuen.2018.06.024
Li, B., Neumann, E. K., Ge, J., Gao, W., Yang, H., Li, P., & Sweedler, J. V. (2018). Interrogation of spatial metabolome of Ginkgo biloba with high-resolution matrix-assisted laser desorption/ionization and laser desorption/ionization mass spectrometry imaging. Plant Cell and Environment, 41(11), 2693-2703. https://doi.org/10.1111/pce.13395
Lian, J., Mishra, S., & Zhao, H. (2018). Recent advances in metabolic engineering of Saccharomyces cerevisiae: New tools and their applications. Metabolic Engineering, 50, 85-108. https://doi.org/10.1016/j.ymben.2018.04.011
Dowd, S. E., Mustroph, M. L., Romanova, E. V., Southey, B. R., Pinardo, H., Rhodes, J. S., & Sweedler, J. V. (2018). Exploring Exercise- and Context-Induced Peptide Changes in Mice by Quantitative Mass Spectrometry. ACS Omega, 3(10), 13817-13827. https://doi.org/10.1021/acsomega.8b01713
Ongpipattanakul, C., & Nair, S. K. (2018). Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis. ACS chemical biology, 13(10), 2989-2999. https://doi.org/10.1021/acschembio.8b00668
Ren, H., Biswas, S., Ho, S., Van Der Donk, W. A., & Zhao, H. (2018). Rapid Discovery of Glycocins through Pathway Refactoring in Escherichia coli. ACS chemical biology, 13(10), 2966-2972. https://doi.org/10.1021/acschembio.8b00599
Neumann, E. K., Comi, T. J., Spegazzini, N., Mitchell, J. W., Rubakhin, S. S., Gillette, M. U., ... Sweedler, J. V. (2018). Multimodal Chemical Analysis of the Brain by High Mass Resolution Mass Spectrometry and Infrared Spectroscopic Imaging. Analytical chemistry, 90(19), 11572-11580. https://doi.org/10.1021/acs.analchem.8b02913
Mand, T. D., Kulkarni, G., & Metcalf, W. W. (2018). Genetic, biochemical, and molecular characterization of methanosarcina barkeri mutants lacking three distinct classes of hydrogenase. Journal of bacteriology, 200(20), [e00342]. https://doi.org/10.1128/JB.00342-18
Kelliher, J. L., Radin, J. N., & Kehl-Fie, T. (2018). PhoPR contributes to staphylococcus aureus Growth during phosphate starvation and pathogenesis in an environment- specific manner. Infection and immunity, 86(10), [e00371-18]. https://doi.org/10.1128/IAI.00371-18
An, L., Cogan, D. P., Navo, C. D., Jiménez-Osés, G., Nair, S. K., & van der Donk, W. A. (2018). Substrate-assisted enzymatic formation of lysinoalanine in duramycin. Nature chemical biology, 14(10), 928-933. https://doi.org/10.1038/s41589-018-0122-4
Hudson, G. A., & Mitchell, D. A. (2018). RiPP antibiotics: biosynthesis and engineering potential. Current Opinion in Microbiology, 45, 61-69. https://doi.org/10.1016/j.mib.2018.02.010
Livezey, M., Huang, R., Hergenrother, P., & Shapiro, D. J. (2018). Strong and sustained activation of the anticipatory unfolded protein response induces necrotic cell death. Cell Death and Differentiation, 25(10), 1796-1807. https://doi.org/10.1038/s41418-018-0143-2
Si, T., Tian, Q., Min, Y., Zhang, L., Sweedler, J. V., Van Der Donk, W. A., & Zhao, H. (2018). Rapid Screening of Lanthipeptide Analogs via In-Colony Removal of Leader Peptides in Escherichia coli. Journal of the American Chemical Society, 140(38), 11884-11888. https://doi.org/10.1021/jacs.8b05544
Tasker, S. Z., Cowfer, A. E., & Hergenrother, P. (2018). Preparation of Structurally Diverse Compounds from the Natural Product Lycorine. Organic Letters, 20(18), 5894-5898. https://doi.org/10.1021/acs.orglett.8b02562
O'Reilly, M. C., Dong, S. H., Rossi, F. M., Karlen, K. M., Kumar, R. S., Nair, S. K., & Blackwell, H. E. (2018). Structural and Biochemical Studies of Non-native Agonists of the LasR Quorum-Sensing Receptor Reveal an L3 Loop “Out” Conformation for LasR. Cell chemical biology, 25(9), 1128-1139.e3. https://doi.org/10.1016/j.chembiol.2018.06.007
Wang, P., Liang, J., Shi, L. Z., Wang, Y., Zhang, P., Ouyang, M., ... Wang, Y. (2018). Visualizing Spatiotemporal Dynamics of Intercellular Mechanotransmission upon Wounding. ACS Photonics, 5(9), 3565-3574. https://doi.org/10.1021/acsphotonics.8b00383
Kapoor, I., & Nair, S. K. (2018). Structure-Guided Analyses of a Key Enzyme Involved in the Biosynthesis of an Antivitamin. Biochemistry, 57(36), 5282-5288. https://doi.org/10.1021/acs.biochem.8b00576
Sweedler, J. V. (2018). Where Do Our Manuscripts Come From? Analytical chemistry, 90(17). https://doi.org/10.1021/acs.analchem.8b03710
Lian, J., HamediRad, M., & Zhao, H. (2018). Advancing Metabolic Engineering of Saccharomyces cerevisiae Using the CRISPR/Cas System. Biotechnology Journal, 13(9), [1700601]. https://doi.org/10.1002/biot.201700601
Fine, J. D., Shpigler, H. Y., Ray, A. M., Beach, N. J., Sankey, A. L., Cash-Ahmed, A., ... Robinson, G. E. (2018). Quantifying the effects of pollen nutrition on honey bee queen egg laying with a new laboratory system. PloS one, 13(9), [e0203444]. https://doi.org/10.1371/journal.pone.0203444
McLaughlin, M. I., & van der Donk, W. A. (2018). Stereospecific Radical-Mediated B12-Dependent Methyl Transfer by the Fosfomycin Biosynthesis Enzyme Fom3. Biochemistry, 57(33), 4967-4971. https://doi.org/10.1021/acs.biochem.8b00616
Lim, Y. H., Wong, F. T., Yeo, W. L., Ching, K. C., Lim, Y. W., Heng, E., ... Zhao, H. (2018). Auroramycin: A Potent Antibiotic from Streptomyces roseosporus by CRISPR-Cas9 Activation. ChemBioChem, 19(16), 1716-1719. https://doi.org/10.1002/cbic.201800266
Litman, Z. C., Wang, Y., Zhao, H., & Hartwig, J. F. (2018). Cooperative asymmetric reactions combining photocatalysis and enzymatic catalysis. Nature, 560(7718), 355-359. https://doi.org/10.1038/s41586-018-0413-7
Peh, J., Boudreau, M. W., Smith, H. M., & Hergenrother, P. (2018). Overcoming Resistance to Targeted Anticancer Therapies through Small-Molecule-Mediated MEK Degradation. Cell chemical biology, 25(8), 996-1005.e4. https://doi.org/10.1016/j.chembiol.2018.05.008
Romanova, E. V., & Sweedler, J. V. (2018). Animal Model Systems in Neuroscience. ACS Chemical Neuroscience, 9(8), 1869-1870. https://doi.org/10.1021/acschemneuro.8b00380
Green, D. J., Huang, R. C., Sudlow, L., Hatcher, N., Potgieter, K., McCrohan, C., ... Gillette, R. (2018). CAMP, Ca2+, pHi, and NO Regulate H-like Cation Channels That Underlie Feeding and Locomotion in the Predatory Sea Slug Pleurobranchaea californica. ACS Chemical Neuroscience, 9(8), 1986-1993. https://doi.org/10.1021/acschemneuro.8b00187
Atkins, N., Ren, S., Hatcher, N., Burgoon, P. W., Mitchell, J. W., Sweedler, J. V., & Gillette, M. L. (2018). Functional Peptidomics: Stimulus- and Time-of-Day-Specific Peptide Release in the Mammalian Circadian Clock. ACS Chemical Neuroscience, 9(8), 2001-2008. https://doi.org/10.1021/acschemneuro.8b00089
Zhang, G., Yuan, W. D., Vilim, F. S., Romanova, E. V., Yu, K., Yin, S. Y., ... Jing, J. (2018). Newly Identified Aplysia SPTR-Gene Family-Derived Peptides: Localization and Function. ACS Chemical Neuroscience, 9(8), 2041-2053. https://doi.org/10.1021/acschemneuro.7b00513
Sweedler, J. V. (2018). Where Is the Data? Analytical chemistry, 90(15). https://doi.org/10.1021/acs.analchem.8b03212
Schwalen, C. J., Hudson, G. A., Kille, B., & Mitchell, D. A. (2018). Bioinformatic Expansion and Discovery of Thiopeptide Antibiotics. Journal of the American Chemical Society, 140(30), 9494-9501. https://doi.org/10.1021/jacs.8b03896
Sales, M. J., Herbert, W. G., Du, Y., Sandur, A. S., Stanley, N. M., & Jensen, P. A. (2018). Complete genome sequences of streptococcus sobrinus SL1 (ATCC 33478 DSM 20742), NIDR 6715-7 (ATCC 27351), NIDR 6715-15 (ATCC 27352), and NCTC 10919 (ATCC 33402). Microbiology Resource Announcements, 7(3), [e00804-18]. https://doi.org/10.1128/MRA.00804-18
Cao, X., Zhu, L., Song, X., Hu, Z., & Cronan, J. E. (2018). Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. Proceedings of the National Academy of Sciences of the United States of America, 115(30), E7063-E7072. https://doi.org/10.1073/pnas.1805862115
Gerlt, J. A. (2018). The Need for Manuscripts to Include Database Identifiers for Proteins. Biochemistry, 57(29), 4239-4240. https://doi.org/10.1021/acs.biochem.8b00705
Cao, X., Koch, T., Steffens, L., Finkensieper, J., Zigann, R., Cronan, J. E., & Dahl, C. (2018). Lipoate-binding proteins and specific lipoate-protein ligases in microbial sulfur oxidation reveal an atpyical role for an old cofactor. eLife, 7, [e37439]. https://doi.org/10.7554/eLife.37439
Petronikolou, N., & Nair, S. K. (2018). Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters. ACS Catalysis, 8(7), 6334-6344. https://doi.org/10.1021/acscatal.8b00787
Movassaghi, M., & van der Donk, W. A. (2018). Synthesis of Antibiotics and Related Molecules. Journal of Organic Chemistry, 83(13), 6826-6828. https://doi.org/10.1021/acs.joc.8b01330
Estrada, P., Morita, M., Hao, Y., Schmidt, E. W., & Nair, S. K. (2018). A Single Amino Acid Switch Alters the Isoprene Donor Specificity in Ribosomally Synthesized and Post-Translationally Modified Peptide Prenyltransferases. Journal of the American Chemical Society, 140(26), 8124-8127. https://doi.org/10.1021/jacs.8b05187
Weir, W. B., Fred, L. Y., Pike, M., Rubakhin, S. S., Ludwig, T. J., Shar, A. M., ... Sweedler, J. V. (2018). Expired Epinephrine Maintains Chemical Concentration and Sterility. Prehospital Emergency Care, 22(4), 414-418. https://doi.org/10.1080/10903127.2017.1402109
Kulkarni, G., Mand, T. D., & Metcalf, W. W. (2018). Energy conservation via hydrogen cycling in the methanogenic archaeon Methanosarcina barkeri. mBio, 9(4), [e01256-18]. https://doi.org/10.1128/mBio.01256-18
Carter, M. S., Zhang, X., Huang, H., Bouvier, J. T., Francisco, B. S., Vetting, M. W., ... Gerlt, J. A. (2018). Functional assignment of multiple catabolic pathways for d-apiose article. Nature chemical biology, 14(7), 696-705. https://doi.org/10.1038/s41589-018-0067-7
Bao, Z., HamediRad, M., Xue, P., Xiao, H., Tasan, I., Chao, R., ... Zhao, H. (2018). Genome-scale engineering of Saccharomyces cerevisiae with single-nucleotide precision. Nature Biotechnology, 36(6), 505-508. https://doi.org/10.1038/nbt.4132
Shi, S., Ang, E. L., & Zhao, H. (2018). In vivo biosensors: mechanisms, development, and applications. Journal of Industrial Microbiology and Biotechnology, 45(7), 491-516. https://doi.org/10.1007/s10295-018-2004-x
Katz, L., Chen, Y. Y., Gonzalez, R., Peterson, T. C., Zhao, H., & Baltz, R. H. (2018). Synthetic biology advances and applications in the biotechnology industry: a perspective. Journal of Industrial Microbiology and Biotechnology, 45(7), 449-461. https://doi.org/10.1007/s10295-018-2056-y
Shen, M., Qu, Z., Deslaurier, J., Welle, T. M., Sweedler, J. V., & Chen, R. (2018). Single Synaptic Observation of Cholinergic Neurotransmission on Living Neurons: Concentration and Dynamics. Journal of the American Chemical Society, 140(25), 7764-7768. https://doi.org/10.1021/jacs.8b01989
Drown, B. S., & Hergenrother, P. (2018). Going on offense against the gram-negative defense. Proceedings of the National Academy of Sciences of the United States of America, 115(26), 6530-6532. https://doi.org/10.1073/pnas.1807278115
Ongpipattanakul, C., & Nair, S. K. (2018). Biosynthetic Proteases That Catalyze the Macrocyclization of Ribosomally Synthesized Linear Peptides. Biochemistry, 57(23), 3201-3209. https://doi.org/10.1021/acs.biochem.8b00114
Li, B., Dunham, S. J. B., Ellis, J. F., Lange, J. D., Smith, J. R., Yang, N., ... Sweedler, J. V. (2018). A Versatile Strategy for Characterization and Imaging of Drip Flow Microbial Biofilms. Analytical chemistry, 90(11), 6725-6734. https://doi.org/10.1021/acs.analchem.8b00560
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Lian, J., Bao, Z., Hu, S., & Zhao, H. (2018). Engineered CRISPR/Cas9 system for multiplex genome engineering of polyploid industrial yeast strains. Biotechnology and bioengineering, 115(6), 1630-1635. https://doi.org/10.1002/bit.26569
HamediRad, M., Lian, J., Li, H., & Zhao, H. (2018). RNAi assisted genome evolution unveils yeast mutants with improved xylose utilization. Biotechnology and bioengineering, 115(6), 1552-1560. https://doi.org/10.1002/bit.26570
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Checco, J. W., Zhang, G., Yuan, W. D., Yu, K., Yin, S. Y., Roberts-Galbraith, R. H., ... Sweedler, J. V. (2018). Molecular and Physiological Characterization of a Receptor for d -Amino Acid-Containing Neuropeptides. ACS chemical biology, 13(5), 1343-1352. https://doi.org/10.1021/acschembio.8b00167
Morita, M., Hao, Y., Jokela, J. K., Sardar, D., Lin, Z., Sivonen, K., ... Schmidt, E. W. (2018). Post-Translational Tyrosine Geranylation in Cyanobactin Biosynthesis. Journal of the American Chemical Society, 140(19), 6044-6048. https://doi.org/10.1021/jacs.8b03137
Anapindi, K. D. B., Romanova, E. V., Southey, B. R., & Sweedler, J. V. (2018). Peptide identifications and false discovery rates using different mass spectrometry platforms. Talanta, 182, 456-463. https://doi.org/10.1016/j.talanta.2018.01.062
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