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Health Sciences profile

Dr Matthias Fellner

PositionPostdoctoral Fellow
DepartmentDepartment of Biochemistry
Research summaryStructural biochemistry/chemistry

Research

I study protein structure-function relationships and use this knowledge to answer fundamental questions of chemistry/biochemistry, especially relating to human disease.

Publications

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(10), 2771-2782. doi: 10.1021/acsinfecdis.0c00503

Chen, S., Lovell, S., Lee, S., Fellner, M., Mace, P. D., & Bogyo, M. (2020). Identification of highly selective covalent inhibitors by phage display. Nature Biotechnology. Advance online publication. doi: 10.1038/s41587-020-0733-7

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 enzymatic function. Journal of Biological Chemistry, 295(24), 8272-8284. doi: 10.1074/jbc.RA120.013227

Desguin, B., Urdiain-Arraiza, J., Da Costa, M., Fellner, M., Hu, J., Hausinger, R. 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., 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

Chapter in Book - Research

Fellner, M., Rankin, J. A., Hu, J., & Hausinger, R. P. (2017). Lactate racemase. In R. A. Scott (Ed.), Encyclopedia of inorganic and bioinorganic chemistry. John Wiley & Sons. doi: 10.1002/9781119951438.eibc2508

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Journal - Research Article

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(10), 2771-2782. 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

Desguin, B., Urdiain-Arraiza, J., Da Costa, M., Fellner, M., Hu, J., Hausinger, R. 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

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 enzymatic function. Journal of Biological Chemistry, 295(24), 8272-8284. doi: 10.1074/jbc.RA120.013227

Chen, S., Lovell, S., Lee, S., Fellner, M., Mace, P. D., & Bogyo, M. (2020). Identification of highly selective covalent inhibitors by phage display. Nature Biotechnology. Advance online publication. doi: 10.1038/s41587-020-0733-7

Fellner, M., Hausinger, R. P., & Hu, J. (2018). A structural perspective on the PP-loop ATP pyrophosphatase family. Critical Reviews in Biochemistry & Molecular Biology, 53(6), 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(38), 5513-5523. doi: 10.1021/acs.biochem.8b00601

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(34), 11980-11988. doi: 10.1021/jacs.7b06186

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(8), 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. PNAS, 114(34), 9074-9079. doi: 10.1073/pnas.1704967114

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(9), 1362-1371. doi: 10.1021/acs.biochem.5b01203

Tchesnokov, E. P., Faponle, A. S., Davies, C. G., Quesne, M. G., Turner, R., Fellner, M., Souness, R. J., Wilbanks, S. M., … 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

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(40), 24424-24437. doi: 10.1074/jbc.M114.635672

Fellner, M., Doughty, L. M., Jameson, G. N. L., & 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

Davies, C. G., Fellner, M., Tchesnokov, E. P., Wilbanks, S. M., & Jameson, G. N. L. (2014). The Cys-Tyr crosslink of cysteine dioxygenase changes the optimal pH of the reaction without structural change. Biochemistry, 53(50), 7961-7968. doi: 10.1021/bi501277a

Fellner, M., Gruber, L., & Steiner, I. (2012). Migrationspotenzial von Kaffeefilter-Papieren. Deutsche Lebensmittel-Rundschau, 108(6), 305-312.

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Journal - Research Other

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), 1-15. doi: 10.3390/ijms21217837

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