Michael A Funk - Publications

Affiliations: 
2017- AAAS 
Area:
biochemistry, structural biology, enzymology, microbiology

14 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Ting CP, Funk MA, Halaby SL, Zhang Z, Gonen T, van der Donk WA. Use of a scaffold peptide in the biosynthesis of amino acid-derived natural products. Science (New York, N.Y.). 365: 280-284. PMID 31320540 DOI: 10.1126/science.aau6232  0.36
2018 Orman M, Bodea S, Funk MA, Campo AM, Bollenbach M, Drennan CL, Balskus EP. Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. Journal of the American Chemical Society. PMID 30557011 DOI: 10.1021/jacs.8b04883  0.8
2018 Chen PY, Funk MA, Brignole EJ, Drennan CL. Disruption of an oligomeric interface prevents allosteric inhibition of class Ia ribonucleotide reductase. The Journal of Biological Chemistry. PMID 29700111 DOI: 10.1074/jbc.RA118.002569  0.8
2017 Backman LRF, Funk MA, Dawson CD, Drennan CL. New tricks for the glycyl radical enzyme family. Critical Reviews in Biochemistry and Molecular Biology. 1-22. PMID 28901199 DOI: 10.1080/10409238.2017.1373741  0.8
2017 Funk MA, van der Donk WA. Ribosomal Natural Products, Tailored To Fit. Accounts of Chemical Research. PMID 28682627 DOI: 10.1021/acs.accounts.7b00175  0.36
2016 Bodea S, Funk MA, Balskus EP, Drennan CL. Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase. Cell Chemical Biology. PMID 27642068 DOI: 10.1016/j.chembiol.2016.07.020  0.8
2016 Oyala PH, Ravichandran KR, Funk MA, Stucky PA, Stich TA, Drennan CL, Britt RD, Stubbe J. Biophysical characterization of fluorotyrosine probes site-specifically incorporated into enzymes: E. coli ribonucleotide reductase as an example. Journal of the American Chemical Society. PMID 27276098 DOI: 10.1021/jacs.6b03605  0.8
2016 Zimanyi CM, Chen PY, Kang G, Funk MA, Drennan CL. Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Elife. 5. PMID 26754917 DOI: 10.7554/eLife.07141  0.8
2015 Funk MA, Marsh EN, Drennan CL. Substrate-bound Structures of Benzylsuccinate Synthase Reveal How Toluene Is Activated in Anaerobic Hydrocarbon Degradation. The Journal of Biological Chemistry. 290: 22398-22408. PMID 26224635 DOI: 10.1074/jbc.M115.670737  0.48
2014 Wei Y, Funk MA, Rosado LA, Baek J, Drennan CL, Stubbe J. The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proceedings of the National Academy of Sciences of the United States of America. 111: E3756-65. PMID 25157154 DOI: 10.1073/pnas.1414396111  0.48
2014 Funk MA, Judd ET, Marsh EN, Elliott SJ, Drennan CL. Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity. Proceedings of the National Academy of Sciences of the United States of America. 111: 10161-6. PMID 24982148 DOI: 10.1073/pnas.1405983111  0.48
2011 Ando N, Brignole EJ, Zimanyi CM, Funk MA, Yokoyama K, Asturias FJ, Stubbe J, Drennan CL. Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proceedings of the National Academy of Sciences of the United States of America. 108: 21046-51. PMID 22160671 DOI: 10.1073/pnas.1112715108  0.48
2010 Vey JL, Al-Mestarihi A, Hu Y, Funk MA, Bachmann BO, Iverson TM. Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis . Biochemistry. 49: 9306-17. PMID 20866105 DOI: 10.1021/bi101336u  0.48
2009 Preininger AM, Funk MA, Oldham WM, Meier SM, Johnston CA, Adhikary S, Kimple AJ, Siderovski DP, Hamm HE, Iverson TM. Helix dipole movement and conformational variability contribute to allosteric GDP release in Galphai subunits. Biochemistry. 48: 2630-42. PMID 19222191 DOI: 10.1021/bi801853a  0.48
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