External academic staff at Faculty of Science, Central Library of Charles University
Publications
- 14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices2023 | Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
- Structural insights into the functional roles of 14-3-3 proteins2022 | Faculty of Science, Central Library of Charles University
- 14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites2021 | Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
- Structural Insights Support Targeting ASK1 Kinase for Therapeutic Interventions2021 | Faculty of Science, Central Library of Charles University
- The redox-active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress2020 | Faculty of Science, Central Library of Charles University
- Stabilization of Protein–Protein Interactions between CaMKK2 and 14–3–3 by Fusicoccins2020 | Faculty of Science, Central Library of Charles University
- The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases2020 | Faculty of Science, Central Library of Charles University
- CaMKK2 kinase domain interacts with the autoinhibitory region through the N-terminal lobe including the RP insert2018 | Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
- 14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2)2018 | Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
- Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1)2016 | Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
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