Author

M. Fellner

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Assay:proteomics· 3 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Bogyo· 2 shared C. S. Lentz· 1 shared E. C. Ledgerwood· 1 shared E. C. Woods· 1 shared G. N. L. Jameson· 1 shared I. Kass· 1 shared J. Hu· 1 shared J. Jaworek-Korjakowska· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersMicrobiology

M. Bogyo

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection of S. aureus Infections

J. Jo, T. Upadhyay, E. C. Woods, K. W. Park, N. J. Pedowitz, J. Jaworek-Korjakowska, S. Wang, T. A. Valdez, M. Fellner, M. Bogyo

The paper develops oxadiazolone-based probes targeting FphE to specifically detect S. aureus infections through covalent modification of the enzyme's active site.

bioRxiv · Dec 11, 2023 · PreprintMicrobiology

Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activity

M. Fellner, R. Parakra, K. O. McDonald, I. Kass, G. N. L. Jameson, S. M. Wilbanks, E. C. Ledgerwood

The paper investigates how pathogenic cytochrome c variants alter structure and dynamics, linking these changes to increased apoptotic activity and peroxidase function.

bioRxiv · Jun 14, 2020Biochemistry

Structural basis for active-site probes targeting Staphylococcus aureus serine hydrolase virulence factors

M. Fellner, C. S. Lentz, S. A. Jamieson, J. L. Brewster, L. Chen, M. Bogyo, P. D. Mace

The paper reports structures of Staphylococcus aureus serine hydrolases and their interactions with inhibitors, revealing functional insights and potential targets for therapeutic development.

bioRxiv · Apr 21, 2020 · PreprintBiochemistry

Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and function

N. M. Good, M. Fellner, K. Demirer, J. Hu, R. P. Hausinger, N. C. C. Martinez-Gomez

This study identifies an essential aspartate residue for lanthanide coordination and function in XoxF and ExaF dehydrogenases.

bioRxiv · Feb 25, 2020Biochemistry