Author

G. Koenig

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Assay:structural biology· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

A. Bacchin· 1 shared A. Hausch· 1 shared A. Henras· 1 shared A. Loef· 1 shared C. Dominique· 1 shared E. Kostenis· 1 shared F. Andres· 1 shared G. Schertler· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiochemistry

A. Bacchin

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Cyclic peptide inhibitors stabilize Gq/11 heterotrimers

J. Muehle, M. J. Rodrigues, J. Alenfelder, L. Juergenliemke, R. Guixa-Gonzalez, A. Bacchin, F. Andres, M. Hennig, H. Schihada, M. Cruesemann, G. Koenig, E. Kostenis, G. Schertler, X. Deupi

This study determines the crystal structures of FR and YM bound to G11, revealing they stabilize Gq/11 heterotrimers by reinforcing the G and Gβ interface.

bioRxiv · Oct 24, 2023 · PreprintBiochemistry

The Ribosome Maturation Factor Rea1 utilizes nucleotide independent and ATP hydrolysis driven Linker remodelling for the removal of ribosome assembly factors

J. Busselez, G. Koenig, T. Klos, P. Sosnowski, N. Marechal, H. Gizardin-Fredon, S. Cianferani, C. Dominique, Y. Henry, A. Henras, H. Schmidt

This study investigates how Rea1 removes ribosome assembly factors by showing its linker undergoes nucleotide-independent and ATP hydrolysis-driven remodelling to interact with the MIDAS domain.

bioRxiv · Nov 3, 2022Biochemistry

A Conformational Transition of Von Willebrand Factor's D'D3 Domain Primes It For Multimerization

S. Gruber, A. Loef, A. Hausch, R. Joehr, T. Obser, G. Koenig, R. Schneppenheim, M. A. Brehm, M. Benoit, J. Lipfert

This study uses single-molecule force spectroscopy to show that a conformational change in VWF's DD3 domain, triggered by pH changes and stabilized by FVIII, primes it for multimerization.

bioRxiv · Nov 29, 2021 · PreprintBiophysics