Tomáš Kovaľ

Institute of Biotechnology of the Czech Academy of Sciences

Czech Republic

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Professors in Molecular Biology

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Articles (14)

Year:

2025

Year:

2024

Year:

2024

Year:

2024

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2023

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2023

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2022

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2022

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2022

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2022

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2021

Year:

2021

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2021

Year:

2020

Collaborators (12)

Jan Dohnalek

Head

Institute of Physiology CAS

CZECH REPUBLIC

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Petra Lipovova

University of Chemistry and Technology

CZECH REPUBLIC

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Vojtech Spiwok

University of Chemistry and Technology

CZECH REPUBLIC

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Zahra Aliakbar Tehrani

Institute of Biotechnology

CZECH REPUBLIC

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Gustavo Fuertes Vives

Head of project "Dynamics of Biological Processes"

CZECH REPUBLIC

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Jarmila Hnilicova

Charles University

CZECH REPUBLIC

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Edita Poláchová

Institute of Organic Chemistry and Biochemistry

CZECH REPUBLIC

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Eva Benešová

University of Chemistry and Technology, Prague

CZECH REPUBLIC

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Petr Kolenko

České Vysoké Učení Technické v Praze Fakulta Jaderná a Fyzikálně inženýrská

CZECH REPUBLIC

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Bohdan Schneider

Director of the institute, Head of laboratory

Institute of Experimental Medicine ASCR

CZECH REPUBLIC

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Jiří Černý

since 2017 Head of Laboratory of Structural Bioinformatics of Proteins

Czech Academy of Sciences

CZECH REPUBLIC

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Kristýna Adámková

Institute of Biotechnology

CZECH REPUBLIC

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Tomáš Kovaľ

Research Interests

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Articles (14)

Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222

MoaB2, a newly identified transcription factor, binds to σ <sup>A</sup> in <i>Mycobacterium smegmatis</i>

Mycobacterial HelD connects RNA polymerase recycling with transcription initiation

Substrate preference, <scp>RNA</scp> binding and active site versatility of <i>Stenotrophomonas maltophilia</i> nuclease <scp>S</scp>m<scp>N</scp>uc1, explained by a structural study

Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

A highly active S1‐P1 nuclease from the opportunistic pathogen <i>Stenotrophomonas maltophilia</i> cleaves c‐di‐GMP

The first structure–function study of GH151 α‐l‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity

Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects

What the Hel: recent advances in understanding rifampicin resistance in bacteria

Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse

Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum

Erratum: Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum (Acta Cryst. (2021) D77 (755-775) DOI: 10.1107/S2059798321003533)

SHELIXIR: automation of experimental phasing procedures using SHELXC/D/E

Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.

Collaborators (12)

Jan Dohnalek

Petra Lipovova

Vojtech Spiwok

Zahra Aliakbar Tehrani

Gustavo Fuertes Vives

Jarmila Hnilicova

Edita Poláchová

Eva Benešová

Petr Kolenko

Bohdan Schneider

Jiří Černý

Kristýna Adámková

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