CS
Dr. rer. nat. Vanda Lux

Dr. rer. nat. Vanda Lux

mail vanda.luxinvalid-email-name@invalid-email-domainuochb.cas.cz
phone +420 608 275 236
phone +420 220 183 374
Deputy group leader
Václav Veverka Group
Chromatin Structural Biology

Profile

Short CV

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

2004-2005 Master Thesis under supervision of Pavlina Maloy Rezacova, IMG, CAS- 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 in group of Michael Ehrmann at the University of Duisburg-Essen, projects studying HtrA1 protease and their ability to degrade both Tau protein and Tau insoluble fibrils

2017- now IOCB Prague, Structural biology group, Structural studies of transcription elongation factors

All publications

Selected papers

A ubiquitous disordered protein interaction module orchestrates transcription elongation
A ubiquitous disordered protein interaction module orchestrates transcription elongation
K. Čermáková J. Demeulemeester V. Lux M. Nedomová S. R. Goldman E. A. Smith P. Srb R. Hexnerová M. Fábry M. Mádlíková M. Hořejší J. De Rijck Z. Debyser K. Adelman H. C. Hodges V. Veverka
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.
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All publications

Latest publications

The Impact of Lens Epithelium-Derived Growth Factor p75 Dimerization on Its Tethering Function
T. Brouns V. Lux S. Van Belle F. Christ V. Veverka Z. Debyser
Cells 13 (3): 227 (2024)
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