POSITIONS AVAILABLE FOR MOTIVATED STUDENTS (Bc., NMgr., Ph.D. study)

Please contact prof. Tomas Obsil (obsil@natur.cuni.cz) for more details. 

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

Joshi R, Pohl P, Strachotova D, Herman P, Obsil T, Obsilova V.

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

Pavel Pohl, Rohit Joshi, Olivia Petrvalska, Tomas Obsil and Veronika Obsilova

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains | Communications Biology (nature.com)

Matej Horvath, Olivia Petrvalska, Petr Herman, Veronika Obsilova and Tomas Obsil 

14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites | Communications Biology (nature.com)

PhD Thesis: Domenico Lentini Santo

Master thesis: Nicola Koupilová

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

https://www.ncbi.nlm.nih.gov/pubmed/32979285

Stabilization of Protein-Protein Interactions between CaMKK2 and 14-3-3 by Fusicoccins

https://www.ncbi.nlm.nih.gov/pubmed/33146997

Master thesis: Klára Kohoutová and Martina Mikulů

Bachelor thesis: Adéla Hofmanová

14-3-3 protein binding blocks the dimerization interface of caspase-2

https://www.ncbi.nlm.nih.gov/pubmed/31961068

The redox-active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress

https://www.ncbi.nlm.nih.gov/pubmed/31623019

Recently taken photo together with Obsilova group at BIOCEV in Vestec.