Tomáš Obšil

ORCID: 0000-0003-4602-1272
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About
Contact & Profiles
Research Areas
  • 14-3-3 protein interactions
  • Ubiquitin and proteasome pathways
  • Microbial Natural Products and Biosynthesis
  • FOXO transcription factor regulation
  • Fungal and yeast genetics research
  • ATP Synthase and ATPases Research
  • Heat shock proteins research
  • Redox biology and oxidative stress
  • Protein Kinase Regulation and GTPase Signaling
  • Adenosine and Purinergic Signaling
  • Microbial metabolism and enzyme function
  • Hippo pathway signaling and YAP/TAZ
  • Lipid Membrane Structure and Behavior
  • Ion Transport and Channel Regulation
  • Genetics, Aging, and Longevity in Model Organisms
  • Genomics, phytochemicals, and oxidative stress
  • Receptor Mechanisms and Signaling
  • Photoreceptor and optogenetics research
  • Neuroscience of respiration and sleep
  • Circadian rhythm and melatonin
  • Research on Leishmaniasis Studies
  • RNA regulation and disease
  • Microtubule and mitosis dynamics
  • Neuroendocrine regulation and behavior
  • Neonatal Health and Biochemistry

Czech Academy of Sciences, Institute of Physiology
2015-2024

Charles University
2015-2024

Czech Academy of Sciences
2014-2023

Institute of Macromolecular Chemistry
2014-2016

Candy’s Place
2014

Czech Academy of Sciences, Institute of Physics
2005-2012

Czech Academy of Sciences, Institute of Biotechnology
2011

Griffith University
2011

Veterinary Research Institute
2011

National Institutes of Health
2001-2011

Huaying Zhao Rodolfo Ghirlando Carlos Alfonso Fumio Arisaka Ilan Attali and 95 more David L. Bain Marina Bakhtina Donald Becker Gregory J. Bedwell Ahmet Bekdemir Tabot M. D. Besong Catherine Birck Chad A. Brautigam William Brennerman Olwyn Byron Agnieszka Bzowska Jonathan B. Chaires Catherine T. Chaton Helmut Cölfen Keith D. Connaghan Kimberly A. Crowley Ute Curth Tina Daviter William L. Dean Ana I. Díez Christine Ebel Debra M. Eckert Leslie E. Eisele Edward Eisenstein Patrick England Carlos Escalante Jeffrey Fagan Robert Fairman Ron M. Finn Wolfgang Fischle José Garcı́a de la Torre Jayesh Gor Henning Gustafsson Damien Hall Stephen E. Harding José G. Hernández Cifre Andrew B. Herr Elizabeth E. Howell R. Stefan Isaac Shu-Chuan Jao Davis Jose Soon-Jong Kim Bashkim Kokona Jack A. Kornblatt Dalibor Košek Elena Krayukhina Daniel Krzizike Eric A. Kusznir Hye-Won Kwon Adam G. Larson Thomas M. Laue Aline Le Roy Andrew Leech Hauke Lilie Karolin Luger Juan R. Luque-Ortega Jia Ma C.A. May Ernest L. Maynard Anna Modrak‐Wójcik Yee-Foong Mok Norbert Mücke Luitgard Nagel‐Steger Geeta J. Narlikar Masanori Noda Amanda Nourse Tomáš Obšil Chad K. Park Jin-Ku Park Peter D. Pawelek Erby E. Perdue Stephen J. Perkins Matthew A. Perugini Craig L. Peterson Martin G. Peverelli Grzegorz Piszczek Gali Prag Peter E. Prevelige Bertrand Raynal Lenka Řežábková Klaus Richter Alison E. Ringel Rose Rosenberg Arthur J. Rowe Arne C. Rufer David J. Scott Javier Seravalli Alexandra S. Solovyova Renjie Song David Staunton Caitlin I. Stoddard Katherine Stott Holger M. Strauss Werner Streicher John P. Sumida

Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules their complexes, reporting on size shape in free solution. The purpose this multi-laboratory study was establish the precision accuracy basic data dimensions AUC validate previously proposed calibration techniques. Three kits cell assemblies containing radial temperature tools bovine serum albumin (BSA) reference sample were...

10.1371/journal.pone.0126420 article EN public-domain PLoS ONE 2015-05-21

The daily rhythm in melatonin levels is controlled by cAMP through actions on the penultimate enzyme synthesis, arylalkylamine N -acetyltransferase (AANAT; serotonin -acetyltransferase, EC 2.3.1.87 ). Results presented here describe a regulatory/binding sequence AANAT that encodes cAMP-operated binding switch which cAMP-regulated protein kinase-catalyzed phosphorylation [RRHTLPAN → RRHpTLPAN] promotes formation of complex with 14-3-3 proteins. Formation this AANAT/14-3-3 enhances production...

10.1073/pnas.141118798 article EN Proceedings of the National Academy of Sciences 2001-06-26

Abstract The proapoptotic protein Noxa, a member of the BH3-only Bcl-2 family, can effectively induce apoptosis in cancer cells, although relevant regulatory pathways have been obscure. Previous studies cytotoxic effects α-tocopheryl succinate (α-TOS) on cells identified mechanism whereby α-TOS caused requiring Noxa-Bak axis. In present study, ab initio analysis revealed conserved FoxO-binding site (DBE; DAF-16 binding element) NOXA promoter, and specific affinity FoxO proteins to this DBE...

10.1158/0008-5472.can-10-2203 article EN Cancer Research 2011-01-19

The 14-3-3 proteins are a family of regulatory signaling molecules that interact with other in phosphorylation-dependent manner. thought to play direct role the regulation subcellular localization FoxO forkhead transcription factors. It has been suggested interaction protein affects binding target DNA and interferes function nuclear sequence (NLS). Masking or obscuring NLS could inhibit between factors importing machinery thus shift equilibrium toward cytoplasm. According our best knowledge,...

10.1021/bi050618r article EN Biochemistry 2005-08-01

The 14-3-3 proteins, a family of dimeric regulatory are involved in many biologically important processes. common feature proteins is their ability to bind other phosphorylation-dependent manner. Through these binding interactions, work as molecular scaffolds, modulating the biological functions partners. recognize short motifs containing phosphorylated serine or threonine residue. In this study, we have quantitatively characterized vitro interactions among 14-3-3, Forkhead transcription...

10.1021/bi0352724 article EN Biochemistry 2003-12-01

Significance 14-3-3 proteins are conserved scaffolding expressed in all eukaryotic cells, where they regulate the function of several hundreds partner by constraining their conformation. Yeast neutral trehalases (Nth), enzymes responsible for hydrolysis trehalose, compared with from other organisms, possess distinct structure and regulation involving phosphorylation followed binding to 14-3-3. Here we present crystal structures yeast Nth1 its complex protein propose a molecular mechanism...

10.1073/pnas.1714491114 article EN Proceedings of the National Academy of Sciences 2017-10-30

14-3-3 proteins are abundant binding involved in many biologically important processes. bind to other a phosphorylation-dependent manner and function as scaffold molecules modulating the activity of their partners. In this work, we studied conformational changes C-terminal stretch, region implicated playing role regulation 14-3-3. Time-resolved fluorescence molecular dynamics were used investigate structural stretch induced by phosphopeptide phosphorylation at Thr232, casein kinase I site...

10.1074/jbc.m306939200 article EN cc-by Journal of Biological Chemistry 2004-01-30

FoxO4 belongs to the "O" subset of forkhead transcription factors, which participate in various cellular processes. The DNA binding domain (DBD) consists three-helix bundle resting on a small antiparallel β-sheet from two extended loops protrude and create wing-like structures. wing W2 FoxO factors contains 14-3-3 protein-binding motif that is phosphorylated by protein kinase B response insulin or growth factors. In this report, we investigated role N-terminal loop (portion located upstream...

10.1074/jbc.m605682200 article EN cc-by Journal of Biological Chemistry 2007-01-24

The role of 14-3-3 proteins in the regulation FOXO forkhead transcription factors is at least 2-fold. First, binding inhibits interaction between and target DNA. Second, prevent nuclear reimport by masking their localization signal. exact mechanisms these processes are still unclear, mainly due to lack structural data. In this work, we used fluorescence spectroscopy investigate mechanism protein-dependent inhibition FOXO4 DNA-binding properties. Time-resolved measurements revealed that...

10.1074/jbc.m109.002725 article EN cc-by Journal of Biological Chemistry 2009-05-06

FOXO4 is a member of the FOXO subgroup forkhead transcription factors that constitute key components conserved signalling pathway connects growth and stress signals to transcriptional control. Here, 1.9 Å resolution crystal structure DNA-binding domain human (FOXO4-DBD) bound 13 bp DNA duplex containing consensus binding sequence reported. The shows similar recognition core as has been shown for two other proteins. Helix H3 docked into major groove provides all base-specific contacts, while...

10.1107/s0907444910042228 article EN Acta Crystallographica Section D Biological Crystallography 2010-11-15

Trehalases are important highly conserved enzymes found in a wide variety of organisms and responsible for the hydrolysis trehalose that serves as carbon energy source well universal stress protectant. Emerging evidence indicates enzymatic activity neutral trehalase Nth1 yeast is enhanced by 14-3-3 protein binding phosphorylation-dependent manner through an unknown mechanism. In present study, we investigated detail interaction between Saccharomyces cerevisiae isoforms Bmh1 Bmh2. We...

10.1042/bj20111615 article EN Biochemical Journal 2012-02-10

FOXO transcription factors regulate cellular homeostasis, longevity and response to stress. FOXO1 (also known as FKHR) is a key regulator of hepatic glucose production lipid metabolism, its specific inhibition may have beneficial effects on diabetic hyperglycemia by reducing production. Moreover, all proteins are considered potential drug targets for resistance prevention in cancer therapy. However, the development inhibitors requires detailed understanding structural differences between...

10.3390/cells8090966 article EN cc-by Cells 2019-08-24
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