Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Oliver Simoncik"'
Autor:
Oliver Simoncik, Vlastimil Tichy, Michal Durech, Lenka Hernychova, Filip Trcka, Lukas Uhrik, Miroslav Bardelcik, Philip J Coates, Borivoj Vojtesek, Petr Muller
Publikováno v:
PLoS ONE, Vol 19, Iss 11, p e0312524 (2024)
Stress responses play a vital role in cellular survival against environmental challenges, often exploited by cancer cells to proliferate, counteract genomic instability, and resist therapeutic stress. Heat shock factor protein 1 (HSF1), a central tra
Externí odkaz:
https://doaj.org/article/6dd347d083d24ae2a6d2adedd9e277ab
Autor:
Oliver Simoncik, Daniel Kavan, Pavla Vankova, Petr Müller, Petr Man, Filip Trčka, Michal Durech, Borivoj Vojtesek, Veronika Vandová
Publikováno v:
J Biol Chem
Translocase of outer mitochondrial membrane 34 (TOMM34) orchestrates heat shock protein 70 (HSP70)/HSP90–mediated transport of mitochondrial precursor proteins. Here, using in vitro phosphorylation and refolding assays, analytical size-exclusion ch
Autor:
Borivoj Vojtesek, Oliver Simoncik, Ted R. Hupp, Petr Müller, Miroslav Fojta, David P. Lane, Juliana M. Chan
Publikováno v:
Protein Science. 27:523-530
p53 is a tetrameric protein with a thermodynamically unstable deoxyribonucleic acid (DNA)-binding domain flanked by intrinsically disordered regulatory domains that control its activity. The unstable and disordered segments of p53 allow high flexibil
Publikováno v:
Klinicka onkologie. 31
Background The heat shock transcription factor, HSF1, is the main regulator of the proteotoxic stress response that orchestrates the adaptation of cells to stress conditions such as elevated temperature, oxidative stress, and proteotoxic stress. As s
Autor:
Catherine Mulholland, Ivana Jestřábová, Arghya Sett, Marek Ondruš, Veronika Sýkorová, C. Lorena Manzanares, Oliver Šimončík, Petr Muller, Michal Hocek
Publikováno v:
Communications Chemistry, Vol 6, Iss 1, Pp 1-11 (2023)
DNA aptamers can be selected against a wide range of therapeutic targets, however, the success rate of selective binding remains low due to the highly hydrophilic nature of the DNA backbone. Here, the authors design a hydrophobic 7-phenylbutyl-7-deaz
Externí odkaz:
https://doaj.org/article/fc3f7373278a45df9e2b1dd4a3b232c1
Autor:
Petr, Muller, Juliana M, Chan, Oliver, Simoncik, Miroslav, Fojta, David P, Lane, Ted, Hupp, Borivoj, Vojtesek
Publikováno v:
Protein science : a publication of the Protein Society. 27(2)
p53 is a tetrameric protein with a thermodynamically unstable deoxyribonucleic acid (DNA)‐binding domain flanked by intrinsically disordered regulatory domains that control its activity. The unstable and disordered segments of p53 allow high flexib