Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Zuzana Jaseňáková"'
Autor:
Nicola, Salvi, Vojtěch, Zapletal, Zuzana, Jaseňáková, Milan, Zachrdla, Petr, Padrta, Subhash, Narasimhan, Thorsten, Marquardsen, Jean-Max, Tyburn, Lukáš, Žídek, Martin, Blackledge, Fabien, Ferrage, Pavel, Kadeřávek
Publikováno v:
Biophysical Journal
Biophysical Journal, 2022, 121 (20), pp.3785-3794. ⟨10.1016/j.bpj.2022.09.016⟩
Biophysical Journal, 2022, 121 (20), pp.3785-3794. ⟨10.1016/j.bpj.2022.09.016⟩
International audience; Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core, and their conform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5898807fff2dd8639a7294778ef9a36
https://hal.science/hal-03861375/file/Salvi_BJ_text_preaccepted_4FF.pdf
https://hal.science/hal-03861375/file/Salvi_BJ_text_preaccepted_4FF.pdf
Autor:
Jozef Hritz, Markéta Makovická, Petr Lousa, Arnošt Mládek, Zuzana Jaseňáková, Alice Laníková, Vojtěch Kubáň, Lukáš Žídek, Erik Nomilner, Vojtěch Zapletal, Kateřina Melková
Publikováno v:
Biophys J
Biomolecular force fields optimized for globular proteins fail to properly reproduce properties of intrinsically disordered proteins. In particular, parameters of the water model need to be modified to improve applicability of the force fields to bot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6a0a7af1714640c2942750a1d8c7fbd
https://europepmc.org/articles/PMC7136338/
https://europepmc.org/articles/PMC7136338/
Autor:
Jean-Max Tyburn, Vojtěch Zapletal, Milan Zachrdla, Nicolas Bolik-Coulon, Pavel Kadeřávek, Petr Padrta, Zuzana Jaseňáková, Thorsten Marquardsen, Fabien Ferrage, Lukáš Žídek
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩
Journal of Biomolecular NMR, Springer Verlag, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩
Journal of Biomolecular NMR, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩
Journal of Biomolecular NMR, Springer Verlag, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩
Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90dcc5a617604f244d5912c64a7b4cde
https://doi.org/10.1007/s10858-019-00298-6
https://doi.org/10.1007/s10858-019-00298-6
Autor:
Zuzana Gelová, Jozef Hritz, Michaela Wimmerová, Petr Padrta, Blanka Pekárová, Olga Otrusinová, Jan Hejátko, Zuzana Jaseňáková, Agnieszka Szmitkowska, Pavel Kadeřávek, Lubomír Janda, Milan Zachrdla, Jaromír Marek, Hideo Iwaï, Séverine Jansen, Tomáš Klumpler, Lukáš Žídek, Gabriel Demo
Publikováno v:
Journal of Biological Chemistry. 292:17525-17540
Multistep phosphorelay (MSP) cascades mediate responses to a wide spectrum of stimuli, including plant hormonal signaling, but several aspects of MSP await elucidation. Here, we provide first insight into the key step of MSP-mediated phosphotransfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33d499b0afebbfc6b334af28280d2ccc
https://doi.org/10.1074/jbc.m117.790212
https://doi.org/10.1074/jbc.m117.790212
Autor:
Zuzana, Jaseňáková, Vojtěch, Zapletal, Petr, Padrta, Milan, Zachrdla, Nicolas, Bolik-Coulon, Thorsten, Marquardsen, Jean-Max, Tyburn, Lukáš, Žídek, Fabien, Ferrage, Pavel, Kadeřávek
Publikováno v:
Journal of biomolecular NMR. 74(2-3)
Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::89e9c5c4d71347d6906489cd6c794db1
https://pubmed.ncbi.nlm.nih.gov/31960224
https://pubmed.ncbi.nlm.nih.gov/31960224
Autor:
Milan Zachrdla, Aleksandra Gruca, Petr Padrta, Malene Ringkjøbing Jensen, Vojtěch Kubáň, Libor Krásný, Hana Šanderová, Martin Blackledge, Marcin Grynberg, Zuzana Jaseňáková, Patryk Jarnot, Tomáš Koval, Lukáš Žídek, Dragana Vítovská, Hana Stegnerova, Pavel Srb, Joanna Ziemska-Legiecka, Jan Dohnálek
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2019, 141 (42), pp.16817-16828. ⟨10.1021/jacs.9b07837⟩
Journal of the American Chemical Society, American Chemical Society, 2019, 141 (42), pp.16817-16828. ⟨10.1021/jacs.9b07837⟩
Journal of the American Chemical Society, 2019, 141 (42), pp.16817-16828. ⟨10.1021/jacs.9b07837⟩
Journal of the American Chemical Society, American Chemical Society, 2019, 141 (42), pp.16817-16828. ⟨10.1021/jacs.9b07837⟩
International audience; Electrostatic interactions play important roles in the functional mechanisms exploited by intrinsically disordered proteins (IDPs). The atomic resolution description of long-range and local structural propensities that can bot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac06acd53f1d3d29f2cb037ef3dccf1e
https://hal.univ-grenoble-alpes.fr/hal-02416081
https://hal.univ-grenoble-alpes.fr/hal-02416081
Publikováno v:
Plant Structural Biology: Hormonal Regulations ISBN: 9783319913513
Application of nuclear magnetic resonance (NMR) in protein studies is briefly described. The basic physical principles of the method are introduced, and relation of NMR spectra to chemical structure is explained. The basic technique of isotope labeli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5025d1c14bc33bb87dafa3242a687f2a
https://doi.org/10.1007/978-3-319-91352-0_12
https://doi.org/10.1007/978-3-319-91352-0_12