Profil

2000-2005 Biochemistry Master Degree, Faculty of Natural Sciences, Charles University

2004-2005- Master Thesis with Pavlina Maloy Rezacova- Inhibition of resistant HIV protease variants by recombinant antibodies
2005-2009 PhD Thesis, Department of Virology, University Hospital Heidelberg, Germany, Supervisor Hans-Georg Kraeusslich, Inhibition of HIV capsid assembly
2009-2017 Post-doc with Michael Ehrmann in University of Duisburg-Essen, projects with HtrA1 proteases and Tau protein
2017- now IOCB Prague, Structural biology group

Vybrané publikace

A ubiquitous disordered protein interaction module orchestrates transcription elongation
A ubiquitous disordered protein interaction module orchestrates transcription elongation
Science 374 (6571): 1113-1121 (2021)
The high degree of conservation in protein sequences thought to be unstructured has hinted that these regions may have important biological functions. Although unstructured regions are widely viewed to be crucial for protein signaling, localization, and stability, their roles in many other settings have remained mysterious. Čermáková et al. discovered that prominent members of the transcription elongation machinery are linked through a network of interactions involving transcription elongation factor TFIIS N-terminal domains (TNDs) and conserved unstructured sequences called “TND-interacting motifs” (TIMs). The researchers found that mutation of a single TIM in a central organizing protein of this network abolished key protein interactions and induced widespread defects in transcription elongation dynamics.