Tomas Obsil

Head of department/Professor

Charles University, Faculty of Science

Czech Republic

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Professor Tomas Obsil is the Head of the Department at Charles University, Faculty of Science in the Czech Republic. His research focuses on structural biology, exploring the interactions and functional roles of proteins such as FOXO, 14-3-3, and BAX in cellular signaling and regulation. Recent publications include studies on the structural plasticity of protein interactions and the mechanisms of ubiquitin ligase regulation.

Articles (17)

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2025

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2025

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2024

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2024

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2024

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2023

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2023

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2022

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2022

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2022

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2022

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2021

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2021

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2021

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2021

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2021

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2020

Collaborators (6)

Judith Hagenbuchner

Head 3D Bioprinting Lab

Medical University of Innsbruck

AUSTRIA

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Petr Heřman

CZECH REPUBLIC

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Jan Veselý

Prof.

Charles University

CZECH REPUBLIC

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Luc Brunsveld

Prof. at Eindhoven University of Technology

Eindhoven University of Technology

NETHERLANDS

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Peter Cossar

Eindhoven University of Technology

NETHERLANDS

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Dita Strachotova

Charles University

CZECH REPUBLIC

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Tomas Obsil

Research Interests

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About

Articles (17)

Structural plasticity of the FOXO-DBD:p53-TAD interaction

Structural basis of ubiquitin ligase Nedd4-2 autoinhibition and regulation by calcium and 14-3-3 proteins

The minimal membrane requirements for BAX-induced pore opening upon exposure to oxidative stress

The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1

The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways

Molecular basis and dual ligand regulation of tetrameric Estrogen Receptor α/14-3-3ζ protein complex

14‐3‐3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C‐terminal helices

Structural insights into the functional roles of 14-3-3 proteins.

Lengthening the Guanidine-Aryl Linker of Phenylpyrimidinylguanidines Increases Their Potency as Inhibitors of FOXO3-Induced Gene Transcription.

FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA

Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains

Structural Insights Support Targeting ASK1 Kinase for Therapeutic Interventions

A Structural Study of the Cytoplasmic Chaperone Effect of 14-3-3 Proteins on Ataxin-1

14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains

Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer

The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases

Collaborators (6)

Judith Hagenbuchner

Petr Heřman

Jan Veselý

Luc Brunsveld

Peter Cossar

Dita Strachotova

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