Author

F. Leidner

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

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:structural biology· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

C. A. Schiffer· 3 shared N. Kurt-Yilmaz· 2 shared S. Hou· 2 shared A. Ali· 1 shared E. A. Nalivaika· 1 shared H. Matsuo· 1 shared J. Timm· 1 shared K. KosovrastiiD· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

C. A. Schiffer

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Deciphering complex mechanisms of resistance and loss of potency through coupled molecular dynamics and machine learning.

F. Leidner, N. Kurt-Yilmaz, C. A. Schiffer

This paper uses molecular dynamics and machine learning to identify conserved dynamic mechanisms of drug resistance in HIV-1 protease variants.

Journal of Chemical Theory and Computation · Apr 13, 2021Peer-reviewedBiophysics

Molecular and structural mechanism of pan-genotypic HCV NS3/4A protease inhibition by glecaprevir

J. Timm, K. Kosovrasti, M. Henes, F. Leidner, S. Hou, A. Ali, N. Kurt-Yilmaz, C. A. Schiffer

This study determines the crystal structures of HCV NS3/4A protease from multiple genotypes bound to glecaprevir, revealing molecular mechanisms of pan-genotypic inhibition and resistance-associated substitutions.

ACS Chemical Biology · Dec 23, 2019Peer-reviewedBiochemistry

Structural analysis of the active site and DNA binding of human cytidine deaminase APOBEC3B

S. Hou, T. V. Silvas, F. Leidner, E. A. Nalivaika, H. Matsuo, N. Kurt Yilmaz, C. A. Schiffer

This study identifies the structural basis for APOBEC3B's lower catalytic activity and DNA binding through molecular modeling and mutational analysis.

bioRxiv · Apr 18, 2018Biochemistry