Author

A. Wohlkonig

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· 2 Bioengineering· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:cryo-EM· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Research Focus:benchmarking· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

J. Steyaert· 4 shared B. Fischer· 3 shared E. Pardon· 2 shared S. Ballet· 2 shared S. Gonzalez· 2 shared T. Uchanski· 2 shared T. Zogg· 2 shared W. Versees· 2 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBioengineering

J. Steyaert

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Nanobody CDR3 mimetics enhance SOS1-catalyzed nucleotide exchange on RAS

K. Van holsbeeck, B. Fischer, S. Gonzalez, C. Gadais, W. Versees, J. C. Martins, C. Martin, A. Wohlkonig, J. Steyaert, S. Ballet

This study shows that CDR3 mimetics can enhance SOS1-catalyzed nucleotide exchange on RAS, demonstrating functional modulation of protein-protein interactions through structural mimicry of a nanobody.

bioRxiv · Dec 9, 2022 · PreprintBioengineering

Competitive, connective and allosteric Nanobodies that modulate the SOS1-RAS protein-protein interactions and tune the nucleotide exchange rate as a starting point for drug design

B. Fischer, T. Uchanski, A. Sheryazdanova, S. Gonzalez, A. N. Volkov, E. Brosens, T. Zogg, V. V. Kalichuk, S. Ballet, W. Versees, A. A. Sablina, E. Pardon, A. Wohlkonig, J. Steyaert

The paper introduces methods to discover Nanobodies that modulate SOS1-RAS interactions and nucleotide exchange rates, with potential applications in drug design.

bioRxiv · Dec 6, 2022 · PreprintBioengineering

Crystal and cryo-EM structures of the cytosolic G protein alpha chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1

L. J. McClelland, K. Zhang, T.-C. Mou, J. Johnston, C. Yates-Hansen, S. li, C. J. Thomas, T. I. Doukov, S. Triest, A. Wohlkonig, G. G. Tall, J. Steyaert, W. Chiu, S. R. Sprang

This study reports the crystal and cryo-EM structures of Ric-8A bound to Gαi1, revealing its mechanism of GTP exchange and chaperone activity through structural interactions.

bioRxiv · Jan 4, 2020 · PreprintBiochemistry

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

T. Uchanski, S. Masiulis, B. Fischer, V. Kalichuk, A. Wohlkonig, T. Zogg, H. Remaut, W. Vranken, A. R. Aricescu, E. Pardon, J. Steyaert

The paper introduces megabodies, engineered nanobodies that improve cryo-EM resolution by addressing particle size and orientation issues, and demonstrates their application in solving a membrane protein structure.

bioRxiv · Oct 22, 2019Biochemistry