Publications

Peer-reviewed journal articles

*equal first authors

• 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.
• Nair, S. S., Kleffmann, T., Smith, B., Morris, V., Goebl, C., Pletzer, D., Fellner, M. (2024) Comparative lipidomics profiles of planktonic and biofilms of methicillin-resistant and -susceptible Staphylococcus aureus. Anal Biochem, 115746. DOI: 10.1016/j.ab.2024.115746
• Putha, L., Kok, L. K., Fellner, M., Rutledge, M. T., Gamble, A. B., Wilbanks, S. M., Vernall, A., 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
• 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, Biochemistry 63, 1038-1050. DOI: 10.1021/acs.biochem.4c00031
• Jo, J., Upadhyay, T., Woods, E. C., Park, K. W., Pedowitz, N.J., Jaworek-Korjakowska, J., Wang, S., Valdez, T. A., Fellner, M., and Bogyo M. (2024) Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection of Staphylococcus aureus Infections. JACS 146 (10), 6880-6892. DOI: doi.org/10.1021/jacs.3c13974
• 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
• 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
• 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
• 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
• 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
• 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
• Fellner, M. (2021) Newly discovered Staphylococcus aureus serine hydrolase probe and drug targets. ADMET & DMPK, 10, 107-114. DOI: 10.5599/admet.1137
• 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. (Chosen as the cover article) DOI: 10.1021/acsinfecdis.0c00503
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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
• 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. (Chosen as the cover article) DOI: 10.1016/j.ab.2014.05.008
• Fellner, M., Steiner, I., Gruber, L. (2012), Migrationspotenzial von Kaffeefilter-Papieren. Deutsche Lebensmittel-Rundschau, 108, 305-312. TUWien: ID=208850

Peer reviewed book chapters

• Fellner, M., Rankin, J. A., Hu, J., Hausinger, R. P. (2017), Lactate Racemase. Encyclopedia of Inorganic and Bioinorganic Chemistry, 1-8 DOI: 10.1002/9781119951438.eibc2508