Author

O. Hofnagel

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· 4

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 3 Research Focus:protein structure prediction· 3 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1 Organism:zebrafish· 1

Frequent Co-Authors

S. Raunser· 4 shared A. Belyy· 2 shared D. Vinayagam· 2 shared F. Merino· 2 shared A. Apelbaum· 1 shared A. Bothe· 1 shared A. Roy· 1 shared C. Gatsogiannis· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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4 shared papersBiochemistry

S. Raunser

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4 papers

Recent·Most cited

Structure and activation mechanism of the Makes caterpillars floppy 1 toxin

A. Belyy, P. Heilen, P. Hagel, O. Hofnagel, S. Raunser

This study determines the cryo-EM structure of Mcf1 toxin and elucidates its activation mechanism through conformational changes and autocleavage.

bioRxiv · Aug 14, 2023Biochemistry

Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments

W. Oosterheert, F. Blanc, A. Roy, A. Belyy, O. Hofnagel, G. Hummer, P. Bieling, S. Raunser

This study identifies a molecular backdoor mechanism for inorganic phosphate release from actin filaments, showing how a disease-linked mutation alters Pi release rates and filament structure.

bioRxiv · Mar 25, 2023Biochemistry

Structural basis of TRPC4 regulation by calmodulin and pharmacological agents

D. Vinayagam, D. Quentin, O. Sitsel, F. Merino, M. Stabrin, O. Hofnagel, M. Yu, M. W. Ledeboer, G. Malojcic, S. Raunser

The paper reports structures of TRPC4 in complex with inhibitors, activators, and calmodulin, revealing how ligand binding and calmodulin interaction regulate the channel's conformation.

bioRxiv · Jun 30, 2020Biochemistry

Electron cryo-microscopy structure of the canonical TRPC4 ion channel

D. Vinayagam, T. Mager, A. Apelbaum, A. Bothe, F. Merino, O. Hofnagel, C. Gatsogiannis, S. Raunser

The paper reports the cryo-EM structure of zebrafish TRPC4 in its closed, unliganded state, revealing key structural features and insights into its function and pharmacology.

bioRxiv · Mar 14, 2018Biochemistry