POSITIONS AVAILABLE FOR MOTIVATED STUDENTS (Bc., NMgr., Ph.D. study)
Please contact prof. Tomas Obsil (obsil@natur.cuni.cz) for more details.
Honzejkova K, Kosek D, Obsilova V, Obsil T.
The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1.
Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T.
25 March 2023: Karolina Honzejková won the Czech Society for Structural Biology Award for Outstanding Student Presentation.
Klara Kohoutova, Vojtěch Dočekal, Michael J. Ausserlechner, Nora Kaiser, Andrej Tekel, Raju Mandal, Matej Horvath, Veronika Obsilova, Jan Vesely, Judith Hagenbuchner and Tomas Obsil
Veronika Obsilova and Tomas Obsil
Structural insights into the functional roles of 14-3-3 proteins
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
Matej Horvath, Olivia Petrvalska, Petr Herman, Veronika Obsilova and Tomas Obsil
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.