|
2024
|
| 31.
|
Chekan, J. R.#, Mydy, L. S., Pasquale, M. A., and Kersten, R. D.# (2024) Plant peptides – redefining an area of ribosomally synthesized and post-translationally modified peptides. Nat. Prod. Rep. (doi: 10.1039/D3NP00042G)
|
|
2023
|
| 31. |
Gallardo, I. A., Todd, D. A., Lima, S. T., Chekan, J. R., Chiu, N. H., and Taylor, E. W. (2023) SARS-CoV-2 Main Protease Targets Host Selenoproteins and Glutathione Biosynthesis for Knockdown via Proteolysis, Potentially Disrupting the Thioredoxin and Glutaredoxin Redox Cycles. Antioxidants. 12, 559 (doi: 10.3390/antiox12030559) |
| 30.
|
Lima, S. T.*, Ampolini, B. G.*, Underwood, E. B.*, Graf, T. N., Earp, C. E., Khedi, I. C., Pasquale, M. A., and Chekan, J. R. (2023) A Widely Distributed Biosynthetic Cassette Is Responsible for Diverse Plant Side Chain Cross-Linked Cyclopeptides. Angew. Chem. Int. Ed Engl. (doi: 10.1002/anie.202218082)
|
|
2022
|
| 29. |
Smith, A. B., and Chekan, J. R. (2022) Engineering yeast for industrial-level production of the antimalarial drug artemisinin (Spotlight). Trends Biotechnol. (doi: 10.1016/j.tibtech.2022.12.007) |
| 28. |
Kandy, S. K., and Chekan, J. R. (2022) Biosynthesis of the Plant-Produced Toxin Strychnine Elucidated (Highlight). Angew. Chem. Int. Ed Engl. 61, e202212301 (doi: 10.1002/anie.202212301) |
| 27. |
Chen, P. Y.-T., Adak, S., Chekan, J. R., Liscombe, D. K., Miyanaga, A., Bernhardt, P., Diethelm, S., Fielding, E. N., George, J. H., Miles, Z. D., Murray, L. A. M., Steele, T. S., Winter, J. M., Noel, J. P., and Moore, B. S. (2022) Structural Basis of Stereospecific Vanadium-Dependent Haloperoxidase Family Enzymes in Napyradiomycin Biosynthesis. Biochemistry. (doi: 10.1021/acs.biochem.2c00338) |
| 26. |
Lima, S. T., Fallon, T. R., Cordoza, J. L., Chekan, J. R., Delbaje, E., Hopiavuori, A. R., Alvarenga, D. O., Wood, S. M., Luhavaya, H., Baumgartner, J. T., Dörr, F. A., Etchegaray, A., Pinto, E., McKinnie, S. M. K., Fiore, M. F., and Moore, B. S. (2022) Biosynthesis of Guanitoxin Enables Global Environmental Detection in Freshwater Cyanobacteria. J. Am. Chem. Soc. 144, 9372–9379 (doi: 10.1021/jacs.2c01424) |
| 25. |
Steele, T. S., Brunson, J. K., Maeno, Y., Terada, R., Allen, A. E., Yotsu-Yamashita, M., Chekan, J. R.#, and Moore, B. S.# (2022) Domoic acid biosynthesis in the red alga Chondria armata suggests a complex evolutionary history for toxin production. Proc. Natl. Acad. Sci. 119, e2117407119 (doi: 10.1073/pnas.2117407119) |
|
2021
|
| 24.
|
Bauman, K. D., Butler, K. S., Moore, B. S.#, and Chekan, J. R.# (2021) Genome mining methods to discover bioactive natural products. Nat. Prod. Rep. (doi: 10.1039/d1np00032b)
|
| 23. |
Griffin, S. L., Chekan, J. R., Lira, J. M., Robinson, A. E., Yerkes, C. N., Siehl, D. L., Wright, T. R., Nair, S. K., and Cicchillo, R. M. (2021) Characterization of a Glyphosate-Tolerant Enzyme from Streptomyces svecius: A Distinct Class of 5-Enolpyruvylshikimate-3-phosphate Synthases. J. Agric. Food Chem. 69, 5096–5104 (doi: 10.1021/acs.jafc.1c00439) |
|
2020
|
| 22. |
Chekan, J. R., Fallon, T. R., and Moore, B. S. (2020) Biosynthesis of marine toxins. Curr. Opin. Chem. Biol. 59, 119–129 (doi:10.1016/j.cbpa.2020.06.009) |
| 21. |
Chekan, J. R., McKinnie, S. M. K., Noel, J. P., and Moore, B. S. (2020) Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an N -prenyltransferase. Proc. Natl. Acad. Sci. (doi:10.1073/pnas.2001325117) |
| 20. |
Fiore, M. F., de Lima, S. T., Carmichael, W. W., McKinnie, S. M. K., Chekan, J. R., and Moore, B. S. (2020) Guanitoxin, re-naming a cyanobacterial organophosphate toxin. Harmful Algae. 92, 101737 (doi:10.1016/j.hal.2019.101737) |
|
2019
|
| 19. |
Chekan, J. R., Ongpipattanakul, C., and Nair, S. K. (2019) Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 116, 24049–24055 (doi:10.1073/pnas.1908364116) |
| 18. |
Chekan, J. R., Lee, G. Y., El Gamal, A., Purdy, T. N., Houk, K. N., and Moore, B. S. (2019) Bacterial tetrabromopyrrole debrominase shares a reductive dehalogenation strategy with human thyroid deiodinase. Biochemistry. 58, 5329–5338 (doi:10.1021/acs.biochem.9b00318) |
| 17. |
Chekan, J. R.*, Ongpipattanakul, C.*, Wright, T. R., Zhang, B., Bollinger, J. M., Rajakovich, L. J., Krebs, C., Cicchillo, R. M., and Nair, S. K. (2019) Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants. Proc. Natl. Acad. Sci. 116, 13299–13304 (doi:10.1073/pnas.1900711116) |
| 16. |
Chekan, J. R., McKinnie, S. M. K., Moore, M. L., Poplawski, S. G., Michael, T. P., and Moore, B. S. (2019) Scalable biosynthesis of the seaweed neurochemical, kainic acid. Angew. Chemie Int. Ed. 58, 8454–8457 (doi:10.1002/anie.201902910) |
| 15. |
Luhavaya, H., Sigrist, R., Chekan, J. R., McKinnie, S. M. K., and Moore, B. S. (2019) Biosynthesis of L-4-chlorokynurenine, an antidepressant prodrug and a non-proteinogenic amino acid found in lipopeptide antibiotics. Angew. Chemie Int. Ed. 58, 8394–8399 (doi:10.1002/anie.201901571) |
|
2018
|
| 14. |
Chekan, J. R., and Moore, B. S. (2018) Preparation and characterization of tetrabromopyrrole debrominase from marine proteobacteria. Methods Enzymol. 605, 253–65 (doi:10.1016/bs.mie.2018.01.031) |
| 13. |
Brunson, J. K.*, McKinnie, S. M. K.*, Chekan, J. R., McCrow, J. P., Miles, Z. D., Bertrand, E. M., Bielinski, V. A., Luhavaya, H., Oborník, M., Smith, G. J., Hutchins, D. A., Allen, A. E., and Moore, B. S. (2018) Biosynthesis of the neurotoxin domoic acid in a bloom-forming diatom. Science. 361, 1356–8 (doi:10.1126/science.aau0382) |
| 12. |
Chekan, J. R., and Moore, B. S. (2018) Biosynthesis of the antibiotic bicyclomycin in soil and pathogenic bacteria (Viewpoint). Biochemistry. 57, 897–898 (doi:10.1021/acs.biochem.7b01204) |
|
2017
|
| 11. |
Chekan, J. R., Estrada, P., Covello, P. S., and Nair, S. K. (2017) Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants. Proc. Natl. Acad. Sci. U. S. A. 114, 6551–6556 (doi:10.1073/pnas.1620499114) |
| 10. |
Repka, L. M.*, Chekan, J. R.*, Nair, S. K., and van der Donk, W. A. (2017) Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes. Chem. Rev. 117, 5457–5520 (doi:10.1021/acs.chemrev.6b00591) |
| 9. |
Olivares, P.*, Ulrich, E. C.*, Chekan, J. R.*, van der Donk, W. A., and Nair, S. K. (2017) Characterization of Two Late-Stage Enzymes Involved in Fosfomycin Biosynthesis in Pseudomonads. ACS Chem. Biol. 12, 456–463 (doi:10.1021/acschembio.6b00939) |
|
2016
|
| 8. |
Chekan, J. R., Koos, J. D., Zong, C., Maksimov, M. O., Link, A. J., and Nair, S. K. (2016) Structure of the lasso peptide isopeptidase identifies a topology for processing threaded substrates. J. Am. Chem. Soc. 138, 16452–16458 (doi:10.1021/jacs.6b10389) |
| 7. |
Chekan, J. R.*, Cogan, D. P.*, and Nair, S. K. (2016) Molecular basis for resistance against phosphonate antibiotics and herbicides. Med. Chem. Commun. 7, 28–36 (doi:10.1039/C5MD00351B) |
|
2015
|
| 6. |
Peck, S. C., Chekan, J. R., Ulrich, E. C., Nair, S. K., and van der Donk, W. A. (2015) A common late-stage intermediate in catalysis by 2-hydroxyethyl-phosphonate dioxygenase and methylphosphonate synthase. J. Am. Chem. Soc. 137, 3217–20 (doi:10.1021/jacs.5b00282) |
|
2014
|
| 5. |
Chekan, J. R.*, Kwon, I. H.*, Agarwal, V.*, Dodd, D., Revindran, V., Mackie, R. I., Cann, I., and Nair, S. K. (2014) Structural and biochemical basis for mannan utilization by Caldanaerobius polysaccharolyticus strain ATCC BAA-17. J. Biol. Chem. 289, 34965–77 (doi:10.1074/jbc.M114.579904) |
| 4. |
Zhang, M.*, Chekan, J. R.*, Dodd, D.*, Hong, P.-Y., Radlinski, L., Revindran, V., Nair, S. K., Mackie, R. I., and Cann, I. (2014) Xylan utilization in human gut commensal bacteria is orchestrated by unique modular organization of polysaccharide-degrading enzymes. Proc. Natl. Acad. Sci. U. S. A. 111, E3708–17 (doi:10.1073/pnas.1406156111) |
| 3. |
Dunbar, K. L.*, Chekan, J. R.*, Cox, C. L., Burkhart, B. J., Nair, S. K., and Mitchell, D. A. (2014) Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Nat. Chem. Biol. 10, 823–9 (doi:10.1038/nchembio.1608) |
| 2. |
Hung, J. E., Fogle, E. J., Garg, N., Chekan, J. R., Nair, S. K., and van der Donk, W. A. (2014) Chemical rescue and inhibition studies to determine the role of Arg301 in phosphite dehydrogenase. PLoS One. 9, e87134 (doi:10.1371/journal.pone.0087134) |
| 1. |
Agarwal, V., Peck, S. C., Chen, J.-H., Borisova, S. A., Chekan, J. R., van der Donk, W. A., and Nair, S. K. (2014) Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation. Chem. Biol. 21, 125–35 (doi:10.1016/j.chembiol.2013.11.006) |
