Author

S. Bothe

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 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:drug response / drug discovery· 2 Research Focus:cell type annotation· 1 Organism:mouse· 1 Organism:plant (other)· 1 Assay:proteomics· 1

Frequent Co-Authors

H. Schindelin· 3 shared A. A. Holder· 1 shared A. Gohla· 1 shared A. Keller· 1 shared A. P. Snijders· 1 shared A. Prommaban· 1 shared B. Stieglitz· 1 shared C. Sotriffer· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 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

H. Schindelin

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

7,8-Dihydroxyflavone is a direct inhibitor of pyridoxal phosphatase

M. Brenner, C. Zink, L. Witzinger, A. Keller, K. Hadamek, S. Bothe, M. Neuenschwander, C. Villmann, J. P. von Kries, H. Schindelin, E. Jeanclos, A. Gohla

This study identifies 7,8-dihydroxyflavone as a direct inhibitor of pyridoxal phosphatase, increasing PLP levels in mouse hippocampal neurons and validating PDXP as a druggable target.

bioRxiv · Oct 4, 2023Biochemistry

Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97

S. Bothe, P. Haenzelmann, S. Boehler, J. Kehrein, C. Wiedemann, U. Hellmich, R. Brenk, H. Schindelin, C. Sotriffer

The paper uses biolayer interferometry to identify small molecule ligands targeting the SHP-motif binding site of p97, leading to the first structure of a small molecule complex with the N-domain of p97.

bioRxiv · Jun 1, 2022Biochemistry

Protein ubiquitylation is essential for the schizont to merozoite transition in Plasmodium falciparum blood-stage development

Y. Wu, V. Encheva, J. L. Green, E. Lasonder, A. Prommaban, S. Kunzelmann, E. Christodoulou, M. Grainger, N. Truongvan, S. Bothe, V. Sharma, W. Song, I. Pinzuti, C. Uthaipibull, S. Srichairatanakool, , A. A. Holder

This paper identifies ubiquitylation sites in Plasmodium falciparum and shows that ubiquitylation is essential for the schizont to merozoite transition.

bioRxiv · Sep 4, 2019 · PreprintMicrobiology