T
Tomáš Klumpler
Researcher at Central European Institute of Technology
Publications - 17
Citations - 204
Tomáš Klumpler is an academic researcher from Central European Institute of Technology. The author has contributed to research in topics: Paracoccus denitrificans & Oxidoreductase. The author has an hindex of 7, co-authored 17 publications receiving 167 citations. Previous affiliations of Tomáš Klumpler include Masaryk University.
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Journal ArticleDOI
Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
Blanka Pekárová,Blanka Pekárová,Tomáš Klumpler,Tomáš Klumpler,Olga Třísková,Olga Třísková,Jakub Horák,Jakub Horák,Séverine Jansen,Séverine Jansen,Radka Dopitová,Radka Dopitová,Petra Borkovcová,Veronika Papoušková,Veronika Papoušková,Eliška Nejedlá,Eliška Nejedlá,Vladimír Sklenář,Vladimír Sklenář,Jaromír Marek,Jaromír Marek,Lukáš Žídek,Lukáš Žídek,Jan Hejátko,Jan Hejátko,Lubomír Janda,Lubomír Janda +26 more
TL;DR: It is shown that the C-terminal receiver domain of HK CKI1 (CKI1(RD) ) is responsible for the recognition of CKI 1 downstream signaling partners, and specifically interacts with AHP2, AHP3 and AHP5 with different affinities.
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Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding.
Filip Trčka,Michal Durech,Pavla Vankova,Pavla Vankova,Josef Chmelík,Josef Chmelík,Veronika Martinková,Jiri Hausner,Jiri Hausner,Alan Kadek,Alan Kadek,Julien Marcoux,Tomáš Klumpler,Borivoj Vojtesek,Petr Müller,Petr Man,Petr Man +16 more
TL;DR: Structural evidence of robust ATP-dependent antiparallel dimerization of human inducible Hsp70 protein is provided and a novel role of TPR domain cochaperones in multichaperone complexes involving HSp70 ATP-bound dimers is suggested.
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The structural and functional basis of catalysis mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans.
TL;DR: The new evidence for a cryptic flavin reductase activity of FerB justifies the previous inclusion of this enzyme in the protein family of NADPH-dependent FMN reductases.
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Structure and dynamics of the RNAPII CTDsome with Rtt103.
TL;DR: This work used integrative structural biology to visualize the architecture of the CTD in complex with Rtt103, a 3′-end RNA-processing and transcription termination factor, and underpin the importance of the structural plasticity of theCTD, which is templated by a particular set of CTD-binding proteins.
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Designing Artificial 3D Helicates: Unprecedented Self‐Assembly of Homo‐octanuclear Tetrapods with Europium
TL;DR: The rational design, preparation and characterization of a novel homo-octanuclear helicate, which results from a spatial extension of the central tetranuclear platform, and which offers attractive perspectives for further applications.