OBSIL GROUP
Biophysical Chemistry of Protein Complexes
POSITIONS AVAILABLE / HLEDÁME NOVÉ STUDENTY !!!

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

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

Accepted paper in Protein Science: April 2022

Mandal R, Kohoutova K, Petrvalska O, Horvath M, Srb P, Veverka V, Obsilova V, Obsil T

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

Lab photo February 2022

Accepted paper in Biophysical Journal: February 2022

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.

Lab photo 2021

Two accepted papers in Communications Biology: July and August 2021

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)

Succesfull defences in 2021

PhD Thesis: Domenico Lentini Santo

Master thesis: Nicola Koupilová

Accepted paper in FEBS Journal: March 2021

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

Accepted paper in ACS Chem Biol: November 2020

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

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

Succesfull defences in 2020

Master thesis: Klára Kohoutová and Martina Mikulů

Bachelor thesis: Adéla Hofmanová

Accepted paper in FEBS Journal: August 2020

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

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

Accepted paper in FEBS Journal: April 2020

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

Photo together with Obsilova group at BIOCEV, 2019

Photo together with Obsilova group at BIOCEV, 2017

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

© 2017 Cenek Albl