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. 

Photo together with Obsilova group at BIOCEV, November 2023

Accepted paper in Protein Science: October 2023

Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T.

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

Prize of the CSSB for an outstanding student presentation

25 March 2023: Karolina Honzejková won the Czech Society for Structural Biology Award for Outstanding Student Presentation.

Accepted papers in ACS Omega and Frontiers in Molecular Biosciences: February 2022

Klara Kohoutova, Vojtěch Dočekal, Michael J. Ausserlechner, Nora Kaiser, Andrej Tekel, Raju Mandal, Matej Horvath, Veronika Obsilova, Jan Vesely, Judith Hagenbuchner and Tomas Obsil

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

 

Veronika Obsilova and Tomas Obsil

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

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