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Publications

Peer-reviewed journal articles

*equal first authors

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.; 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. Journal of the American Chemical Society. DOI: 10.1021/jacs.4c15713

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

31) Fellner, M.; 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. Proteins. DOI: 10.1002/prot.26785.

30) Yin, S.; Duan, M.; Fellner, M.; 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. Food Innovation and Advances, 3, 332-343. DOI: 10.48130/fia-0024-0032

29) Putha, L.; Kok, L. K.; Fellner, M.; 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

28) Chatterjee, S.*; Fellner, M.*; 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. Biochemistry, 63, 1038-1050. DOI: 10.1021/acs.biochem.4c00031

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

26) Fellner, M.; 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. ACS Infectious Diseases, 9 (11), 2119-2132. DOI: 10.1021/acsinfecdis.3c00246

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

24) Fellner, M.; 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, Biochem Journal, 478, 669-684. DOI: 10.1042/BCJ20200793

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

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

21) Fellner, M. (2021) Newly discovered Staphylococcus aureus serine hydrolase probe and drug targets. ADMET & DMPK, 10, 107-114. DOI: 10.5599/admet.1137

20) Fellner, M.; 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. ACS Infectious Diseases, 6, 2771-2782. DOI: 10.1021/acsinfecdis.0c00503

19) Fellner, M.; 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. Scientific Reports, 10, 5830. DOI: 10.1038/s41598-020-62847-6

18) Good, N. M.*; Fellner, M.*; 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. Journal of Biological Chemistry, 295, 8272-8284. DOI: 10.1074/jbc.RA120.013227

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

16) Desguin, B.; Urdiain-Arraiza, J.; Da Costa, M.; Fellner, M.; 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

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

14) Fellner, M.*; 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 Lactobacillus plantarum. Biochemistry, 57, 5513-5523. DOI: 10.1021/acs.biochem.8b00601

13) Desguin, B.*; Fellner, M.*; 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. Journal of Biological Chemistry, 293, 12303-12317. DOI: 10.1074/jbc.RA118.003741

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

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

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

9) Fellner, M.*; 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. Proceedings of the National Academy of Sciences, 114, 9074-9079. DOI: 10.1073/pnas.1704967114

8) Martinez, S.*; Fellner, M.*; 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. Journal of the American Chemical Society, 139, 11980–11988. DOI: 10.1021/jacs.7b06186

7) Tchesnokov, E. P.; Faponle, A. S.; Davies, C. G.; Quesne, M. G.; Turner, R.; Fellner, M.; 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. Chemical Communications, 52, 8814-8817. DOI: 10.1039/c6cc03904a

6) Fellner, M.; 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. Journal of Biological Inorganic Chemistry, 21, 501-510. DOI: 10.1007/s00775-016-1360-0

5) Fellner, M.; 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. Biochemistry, 55, 1362-1371. DOI: 10.1021/acs.biochem.5b01203

4) Tchesnokov, E. P.*; Fellner, M.*; 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. Journal of Biological Chemistry, 290, 24424-24437. DOI: 10.1074/jbc.M114.635672

3) Davies, C. G.; Fellner, M.; 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. Biochemistry, 53, 7961-7968. DOI: 10.1021/bi501277a

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

1) Fellner, M.; Steiner, I.; Gruber, L. (2012), Migrationspotenzial von Kaffeefilter-Papieren. Deutsche Lebensmittel-Rundschau, 108, 305-312. TUWien: ID=208850

Peer reviewed book chapters