Author

N. Dimos

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:bacteria (other)· 1 Assay:cryo-EM· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Organism:plant (other)· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

B. Loll· 3 shared A. M. Chanique· 1 shared B. G. Keller· 1 shared B. Koksch· 1 shared B. Kuropka· 1 shared C. P. O. Helmer· 1 shared D. Ghilarov· 1 shared F. Ghaziasaeedi· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 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 papersMicrobiology

B. Loll

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Gene amplifications cause high-level resistance against albicidin in Gram-negative bacteria

M. Saathoff, S. Kosol, T. Semmler, S. A. Wolf, N. Dimos, J. Kupke, M. Seidel, F. Ghaziasaeedi, K. Tedin, B. Kuropka, W. Czyszczon, D. Ghilarov, S. Graetz, J. G. Heddle, B. Loll, , M. Fulde

This study identifies gene amplification as a mechanism conferring high-level resistance to albicidin in Gram-negative bacteria, validated across multiple species.

bioRxiv · Sep 15, 2022Microbiology

Water network in the binding pocket of fluorinated BPTI-Trypsin complexes - insights from simulation and experiment

L. Wehrhan, J. Leppkes, N. Dimos, B. Loll, B. Koksch, B. G. Keller

The paper investigates how fluorination of amino acid side chains in BPTI affects inhibitor strength by analyzing water networks in the binding pocket using simulations and experiments.

bioRxiv · Jun 17, 2022 · PreprintBiochemistry

Rapid high-resolution structure analysis of small, biotechnologically relevant enzymes by cryo-electron microscopy

N. Dimos, C. P. O. Helmer, A. M. Chanique, M. C. Wahl, R. Kourist, T. Hilal, B. Loll

This study demonstrates that cryo-EM can achieve high-resolution structures of small plant enzymes, enabling faster development of biocatalysts for terpenes and terpenoids.

bioRxiv · Jun 15, 2021 · PreprintBiophysics