{"id":22,"date":"2023-02-24T15:12:47","date_gmt":"2023-02-24T02:12:47","guid":{"rendered":"https:\/\/blogs.otago.ac.nz\/fellner\/?page_id=22"},"modified":"2026-04-13T11:45:15","modified_gmt":"2026-04-12T23:45:15","slug":"publications","status":"publish","type":"page","link":"https:\/\/blogs.otago.ac.nz\/fellner\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n

Peer-reviewed journal articles<\/h1>\n\n\n\n

*equal first authors<\/p>\n\n\n\n

38) Randall, G.*; Meden, A.*; Rutledge, M. T.; Prestre\u0161i, L.; Rambaher, M. H.; Chen, S.; Zdovc, I.; Gobec, S.; Knez, D.; Fellner, M.<\/strong> (2026) Carbamoyl fluorides as serine hydrolase inhibitors: a case study on FphI from Staphylococcus aureus<\/em>. Bioorg Chem 176<\/em>, 109834. 10.1016\/j.bioorg.2026.109834. 10.1016\/j.bioorg.2026.109834<\/a><\/p>\n\n\n\n

37) Jo, J.*; Upadhyay, T; You, X; Bennett, J. M.; Lee, H.; Bogyo, M.; Fellner, M.<\/strong>* (2026) Unique structural and ligand-binding properties of the Staphylococcus aureus serine hydrolase FphE.<\/em> Proc. Natl. Acad. Sci. U.S.A. 123 (13) e2532683123. 10.1073\/pnas.2532683123<\/a><\/p>\n\n\n\n

36) Sun, M.; Fellner, M.<\/strong>; Lv, C.; Carne, A.; Zang, J.; Zhao, G.; Bekhit, A. E. A.; Zhang, T. (2025) Dual mechanisms of digestion-resistant proteins in food systems: structural resistance and enzyme inhibition.<\/em> Crit Rev Food Sci Nutr, 1-22. 10.1080\/10408398.2025.2551784<\/a><\/p>\n\n\n\n

35) Upadhyay, T.; Woods, E. C.; Dela Ahator, S.; Julin, K.; Faucher, F. F.; Uddin, M. J.; Hollander, M. J.; Pedowitz, N. J.; Abegg, D.; Hammond, I.; Eke, I. E.; Wang, S.; Chen, S.; Bennett, J. M.; Jo, J.; Lentz, C. S.; Adibekian, A.; Fellner, M.<\/strong>; Bogyo, M. (2025) Identification of covalent inhibitors of Staphylococcus aureus serine hydrolases important for virulence and biofilm formation<\/em>. Nat Commun 16 (1), 5046. 10.1038\/s41467-025-60367-3<\/a><\/p>\n\n\n\n

34) Warring, S. L.; Sisson, H. M.; Randall, G.; Grimon, D.; Dams, D.; Gutierrez, D.; Fellner, M.<\/strong>; Fagerlund, R. D.; Briers, Y.; Jackson, S. A.; Fineran, P. C. (2025) Engineering an antimicrobial chimeric endolysin that targets the phytopathogen Pseudomonas syringae pv. actinidiae<\/em>. J Biol Chem, 110224. DOI: 10.1016\/j.jbc.2025.110224<\/a><\/p>\n\n\n\n

33) Wang, S.; Woods, E. C.; Jo, J.; Zhu, J.; Hansel-Harris, A.; Holcomb, M.; Llanos, M.; Pedowitz, N. J.; Upadhyay, T.; Bennett, J.; Fellner, M.<\/strong>; Park K. W.; Zhang A.; Valdez T. A.; Forli S.; Chan A. I.; Cunningham C. N.; Bogyo M. (2025) An mRNA Display Approach for Covalent Targeting of a Staphylococcus aureus Virulence Factor<\/em>. Journal of the American Chemical Society 147 (10), 8312-8325. DOI: 10.1021\/jacs.4c15713<\/a><\/p>\n\n\n\n

32) Nair, S. S.; Kleffmann, T.; Smith, B., Morris, V.; Goebl, C.; Pletzer, D.; Fellner, M. <\/strong>(2025), Comparative lipidomics profiles of planktonic and biofilms of methicillin-resistant and -susceptible Staphylococcus aureus<\/em>, Anal Biochem, 115746. DOI: 10.1016\/j.ab.2024.115746<\/a><\/p>\n\n\n\n

31)<\/strong> Fellner, M.<\/strong>; Randall, G.; Bitac, I.; Warrender, A. K.; Sethi, A.; Jelinek, R.; Kass, I. (2024) Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.<\/em> Proteins, 93<\/em> (5), 1009-1021. DOI: 10.1002\/prot.26785<\/a><\/p>\n\n\n\n

30) Yin, S.; Duan, M.; Fellner, M.<\/strong>; Wang, Z.; Lv, C.; Zang, J.; Zhao, G.; Zhang, T. (2024) pH\/Glucose dual-responsive protein-based hydrogels with enhanced adhesive and antibacterial properties for diabetic wound healing<\/em>. Food Innovation and Advances, 3, 332-343. DOI: 10.48130\/fia-0024-0032<\/a><\/p>\n\n\n\n

29) Putha, L.; Kok, L. K.; Fellner, M.;<\/strong> Rutledge, M. T.; Gamble, A. B.; Wilbanks, S. M.; Vernall, A. J.; Tyndall, J. D. A. (2024) Covalent isothiocyanate inhibitors of macrophage migration inhibitory factor as potential colorectal cancer treatments. ChemMedChem, e202400394. DOI: 10.1002\/cmdc.202400394<\/a><\/p>\n\n\n\n

28) Chatterjee, S.*; Fellner, M.*;<\/strong> Rankin, J.; Thomas, M. G.; SB, J. S. R.; Christov, C. Z.; Hu, J.; Hausinger, R. P. (2024) Structural, Spectroscopic, and Computational Insights from Canavanine-Bound and Two Catalytically Compromised Variants of the Ethylene-Forming Enzyme<\/em>. Biochemistry, 63, 1038-1050. DOI: 10.1021\/acs.biochem.4c00031<\/a><\/p>\n\n\n\n

27) Jo, J.; Upadhyay, T.; Woods, E. C.; Park, K. W.; Pedowitz, N.J.; Jaworek-Korjakowska, J.; Wang, S.; Valdez, T. A.; Fellner, M.;<\/strong> Bogyo M. (2024) Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection of Staphylococcus aureus Infections<\/em>, Journal of the American Chemical Society, 146 (10), 6880-6892. DOI: doi.org\/10.1021\/jacs.3c13974<\/a><\/p>\n\n\n\n

26) Fellner, M.;<\/strong> Walsh, A.; Dela Ahator, S.; Aftab, N.; Sutherland, B.; Tan, E. W.; Bakker, A. T.; Martin, N. I.; van der Stelt, M.; Lentz, C. S. (2023) Biochemical and Cellular Characterization of the Function of Fluorophosphonate-Binding Hydrolase H (FphH) in Staphylococcus aureus Support a Role in Bacterial Stress Response.<\/em> ACS Infectious Diseases, 9 (11), 2119-2132. DOI: 10.1021\/acsinfecdis.3c00246<\/a><\/p>\n\n\n\n

25) Tessadori, F.; Duran, K.; Knapp, K.; Fellner, M.;<\/strong> (and 61 others) (2022) Recurrent de novomissense variants across multiple histone H4 genes underlie a neurodevelopmental syndrome<\/em>, American Journal of Human Genetics, 109, 750-758. DOI: 10.1016\/j.ajhg.2022.02.003<\/a><\/p>\n\n\n\n

24) Fellner, M.;<\/strong> Parakra, R.; McDonald, K. O.; Kass, I.; Jameson, G. N. L.; Wilbanks, S. M.; Ledgerwood, E. C. (2021) Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activity<\/em>, Biochem Journal, 478, 669-684. DOI: 10.1042\/BCJ20200793<\/a><\/p>\n\n\n\n

23) Fellner, M.<\/strong> (2021) Unique cesium-binding sites in proteins, a case study with the sacrificial sulfur transferase LarE<\/em>, Journal of Life Sciences, 3, 1, 2021:50-62. DOI: https:\/\/doi.org\/f86n <\/a><\/p>\n\n\n\n

22) Chen, S.; Lovell, S. D.; Lee, S.; Fellner, M.;<\/strong> Mace, P. D.; Bogyo, M. (2021), Identification of highly selective covalent inhibitors by phage display<\/em>. Nature Biotechnology, 39, 490-498. DOI: 10.1038\/s41587-020-0733-7<\/a><\/p>\n\n\n\n

21) Fellner, M.<\/strong> (2021) Newly discovered Staphylococcus aureus serine hydrolase probe and drug targets<\/em>. ADMET & DMPK, 10, 107-114. DOI: 10.5599\/admet.1137<\/a><\/p>\n\n\n\n

20) Fellner, M.;<\/strong> Lentz, C. S.; Jamieson, S. A.; Brewster, J. L.; Chen, L.; Bogyo, M.; Mace, P. D. (2020), Structural Basis for the Inhibitor and Substrate Specificity of the Unique Fph Serine Hydrolases of Staphylococcus aureus<\/em>. ACS Infectious Diseases, 6, 2771-2782. DOI: 10.1021\/acsinfecdis.0c00503<\/a><\/p>\n\n\n\n

19) Fellner, M.;<\/strong> Huizenga, K. G.; Hausinger, R. P.; Hu, J. (2020), Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE<\/em>. Scientific Reports, 10, 5830. DOI: 10.1038\/s41598-020-62847-6<\/a><\/p>\n\n\n\n

18) Good, N. M.*; Fellner, M.*;<\/strong> Demirer, K.; Hu, J.; Hausinger, R. P.; Martinez-Gomez, N. C. (2020), Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and function<\/em>. Journal of Biological Chemistry, 295, 8272-8284. DOI: 10.1074\/jbc.RA120.013227<\/a><\/p>\n\n\n\n

17) Reddington, C. J.; Fellner, M.;<\/strong> Burgess, A. E.; Mace, P. D. (2020), Molecular Regulation of the Polycomb Repressive-Deubiquitinase<\/em>, International Journal of Molecular Sciences, 21 (21), 7837. DOI: 10.3390\/ijms21217837<\/a><\/p>\n\n\n\n

16) Desguin, B.; Urdiain-Arraiza, J.; Da Costa, M.; Fellner, M.;<\/strong> Hu, J.; Hausinger, R. P.; Desmet, T.; Hols, P., Soumillion, P. (2020), Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases, Scientific Reports, 10, 18123. DOI: 10.1038\/s41598-020-74802-6<\/a><\/p>\n\n\n\n

15) Fellner, M.;<\/strong> Hausinger, R. P.; Hu, J. (2018), A structural perspective on the PP-loop ATP pyrophosphatase family.<\/em> Critical Reviews in Biochemistry and Molecular Biology, 53, 607-622. DOI: 10.1080\/10409238.2018.1516728<\/a><\/p>\n\n\n\n

14) Fellner, M.*;<\/strong> Rankin, J. A.*; Desguin, B., Hu, J.; Hausinger, R. P. (2018), Analysis of the Active Site Cysteine Residue of the Sacrificial Sulfur Insertase LarE from<\/em> Lactobacillus plantarum<\/em>. Biochemistry, 57, 5513-5523. DOI: 10.1021\/acs.biochem.8b00601<\/a><\/p>\n\n\n\n

13) Desguin, B.*; Fellner, M.*;<\/strong> Riant, O.; Hu, J.; Hausinger, R. P.; Hols, P.; Soumillion, P. (2018), Biosynthesis of the nickel-pincer nucleotide cofactor of lactate racemase requires a CTP-dependent cyclometallase.<\/em> Journal of Biological Chemistry, 293, 12303-12317. DOI: 10.1074\/jbc.RA118.003741<\/a><\/p>\n\n\n\n

12) Hausinger, R. P.; Desguin, B.; Fellner, M.;<\/strong> Rankin, J. A.; Hu, J. (2018), Nickel-pincer nucleotide cofactor.<\/em> Current Opinion in Chemical Biology, 47, 18-23. DOI: 10.1016\/j.cbpa.2018.06.019<\/a><\/p>\n\n\n\n

11) Rankin, J. A.; Mauban, R. C.; Fellner, M.;<\/strong> Desguin, B.; McCracken, J.; Hu, J.; Varganov, S. A.; Hausinger, R. P. (2018)<\/em>, Lactate Racemase Nickel-Pincer Cofactor Operates by a Proton-Coupled Hydride Transfer Mechanism.<\/em> Biochemistry, 57, 3244-3251. DOI: 10.1021\/acs.biochem.8b00100<\/a><\/p>\n\n\n\n

10) Zhang, T.; Liu J.; Fellner, M.;<\/strong> Zhang, C.; Sui, D.; Hu, J. (2017), Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway<\/em>. Science Advances, 3, e1700344. DOI: 10.1126\/sciadv.1700344<\/a><\/p>\n\n\n\n

9) Fellner, M.<\/strong>*; Desguin, B.*; Hausinger, R. P.; Hu, J. (2017), Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.<\/em> Proceedings of the National Academy of Sciences, 114, 9074-9079. DOI: 10.1073\/pnas.1704967114<\/a><\/p>\n\n\n\n

8) Martinez, S.*; Fellner, M.<\/strong>*; Herr, C. Q.; Ritchie, A.; Hu, J.; Hausinger, R. P. (2017), Structures and Mechanisms of the Non-Heme Fe (II)-and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates a Twist<\/em>. Journal of the American Chemical Society, 139, 11980\u201311988. DOI: 10.1021\/jacs.7b06186<\/a><\/p>\n\n\n\n

7) Tchesnokov, E. P.; Faponle, A. S.; Davies, C. G.; Quesne, M. G.; Turner, R.; Fellner, M.;<\/strong> Souness, R. J.; Wilbanks, S. M.; de Visser, S. P.; Jameson, G. N. L. (2016), An Iron-Oxygen Intermediate Formed During the Catalytic Cycle of Cysteine Dioxygenase<\/em>. Chemical Communications, 52, 8814-8817. DOI: 10.1039\/c6cc03904a<\/a><\/p>\n\n\n\n

6) Fellner, M.;<\/strong> Siakkou, E.; Faponle, A. S.; Tchesnokov, E. P.; de Visser, S. P.; Wilbanks, S. M.; Jameson, G. N. L. (2016), Influence of cysteine 164 on active site structure in rat cysteine dioxygenase<\/em>. Journal of Biological Inorganic Chemistry, 21, 501-510. DOI: 10.1007\/s00775-016-1360-0<\/a><\/p>\n\n\n\n

5) Fellner, M.;<\/strong> Aloi S.; Tchesnokov, E. P.; Wilbanks, S. M.; Jameson, G. N. L. (2016), Substrate and pH-Dependent Kinetic Profile of 3-Mercaptopropionate Dioxygenase from Pseudomonas aeruginosa<\/em>. Biochemistry, 55, 1362-1371. DOI: 10.1021\/acs.biochem.5b01203<\/a><\/p>\n\n\n\n

4) Tchesnokov, E. P.*; Fellner, M.<\/strong>*; Siakkou, E.; Kleffmann, T.; Martin, L. W.; Aloi, S.; Lamont, I. L., Wilbanks, S. M.; Jameson, G. N. L. (2015), The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa is a 3-Mercaptopropionate Dioxygenase<\/em>. Journal of Biological Chemistry, 290, 24424-24437. DOI: 10.1074\/jbc.M114.635672<\/a><\/p>\n\n\n\n

3) Davies, C. G.; Fellner, M.;<\/strong> Tchesnokov, E. P.; Wilbanks, S. M.; Jameson, G. N. L. (2014), The Cys-Tyr Cross-Link of Cysteine Dioxygenase Changes the Optimal pH of the Reaction without a Structural Change.<\/em> Biochemistry, 53, 7961-7968. DOI: 10.1021\/bi501277a<\/a><\/p>\n\n\n\n

2) Fellner, M.;<\/strong> Doughty, L. M.; Jameson, G. N.; Wilbanks, S. M. (2014), A chromogenic assay of substrate depletion by thiol dioxygenases<\/em>. Analytical Biochemistry, 459, 56-60. DOI: 10.1016\/j.ab.2014.05.008<\/a><\/p>\n\n\n\n

1) Fellner, M.;<\/strong> Steiner, I.; Gruber, L. (2012), Migrationspotenzial von Kaffeefilter-Papieren.<\/em> Deutsche Lebensmittel-Rundschau, 108, 305-312. TUWien: ID=208850<\/a><\/p>\n\n\n\n

Peer reviewed book chapters<\/h1>\n\n\n\n