Zobrazeno 1 - 10
of 163
pro vyhledávání: '"Franz Bartl"'
Autor:
Johannes Oppermann, Paul Fischer, Arita Silapetere, Bernhard Liepe, Silvia Rodriguez-Rozada, José Flores-Uribe, Enrico Schiewer, Anke Keidel, Johannes Vierock, Joel Kaufmann, Matthias Broser, Meike Luck, Franz Bartl, Peter Hildebrandt, J. Simon Wiegert, Oded Béjà, Peter Hegemann, Jonas Wietek
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-1 (2024)
Externí odkaz:
https://doaj.org/article/768a4007f7834da395853386ee5bf11d
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 37, Iss 1, Pp 597-605 (2022)
The influence of base type, temperature, and solvent on regioselective C(9)/C(10) “click” modifications within the tropolone ring of colchiceine (2) is investigated. New ether derivatives of 2, bearing alkyne, azide, vinyl, or halide aryl groups
Externí odkaz:
https://doaj.org/article/601e3f30cb614f1a8f1821e49591e612
Autor:
Natalia Skrzypczak, Krystian Pyta, Piotr Ruszkowski, Przemysław Mikołajczak, Małgorzata Kucińska, Marek Murias, Maria Gdaniec, Franz Bartl, Piotr Przybylski
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 1898-1904 (2021)
Geldanamycin (GDM) has been modified by different type neutral/acidic/basic substituents (1–7) and by quinuclidine motif (8), transformed into ammonium salts (9–13) at C(17). These compounds have been characterised by spectroscopic and x-ray meth
Externí odkaz:
https://doaj.org/article/a4362250a3464123bb99d74ecf85e806
Autor:
Paul Fischer, Shatanik Mukherjee, Enrico Schiewer, Matthias Broser, Franz Bartl, Peter Hegemann
Publikováno v:
eLife, Vol 10 (2021)
Enzymerhodopsins represent a recently discovered class of rhodopsins which includes histidine kinase rhodopsin, rhodopsin phosphodiesterases, and rhodopsin guanylyl cyclases (RGCs). The regulatory influence of the rhodopsin domain on the enzyme activ
Externí odkaz:
https://doaj.org/article/9c4cde73b709437591d114b29a509df2
Autor:
Johannes Oppermann, Paul Fischer, Arita Silapetere, Bernhard Liepe, Silvia Rodriguez-Rozada, José Flores-Uribe, Enrico Schiewer, Anke Keidel, Johannes Vierock, Joel Kaufmann, Matthias Broser, Meike Luck, Franz Bartl, Peter Hildebrandt, J. Simon Wiegert, Oded Béjà, Peter Hegemann, Jonas Wietek
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Abstract Channelrhodopsins (ChRs) are algal light-gated ion channels widely used as optogenetic tools for manipulating neuronal activity. ChRs desensitize under continuous bright-light illumination, resulting in a significant decline of photocurrents
Externí odkaz:
https://doaj.org/article/4a9a09bdb29444b3a95997984a933cb5
Autor:
Urszula Majcher, Greta Klejborowska, Mahshad Moshari, Ewa Maj, Joanna Wietrzyk, Franz Bartl, Jack A. Tuszynski, Adam Huczyński
Publikováno v:
Cells, Vol 7, Iss 11, p 192 (2018)
Microtubules are tubulin polymer structures, which are indispensable for cell growth and division. Its constituent protein β-tubulin has been a common drug target for various diseases including cancer. Colchicine has been used to treat gout, but it
Externí odkaz:
https://doaj.org/article/bc58cb3dfff04eb3b0d94f1e05f5a24c
Autor:
Natalia Skrzypczak, Adam Buczkowski, Wiktor Bohusz, Ewelina Nowak, Klaudia Tokarska, Aleksandra Leśniewska, Attaa Mohammed Alzebari, Piotr Ruszkowski, Maria Gdaniec, Franz Bartl, Piotr Przybylski
Publikováno v:
European Journal of Medicinal Chemistry. 256:115450
Publikováno v:
Biophysical Journal. 122:231a
Autor:
Benjamin S. Krause, Eglof Ritter, Joel C.D. Kaufmann, Franz Bartl, Suliman Adam, Peter Hegemann, Igor Schapiro
Publikováno v:
Biophys J
The function of photoreceptors relies on efficient transfer of absorbed light energy from the chromophore to the protein to drive conformational changes that ultimately generate an output signal. In retinal-binding proteins, mainly two mechanisms exi
Publikováno v:
ChemMedChem. 15:1529-1551
Desosamines of azithromycin (AZM) and clarithromycin (CLA) were modified by N-alkylation or nucleophilic substitution at the carbonyl/CuAAC sequence. Biological studies revealed a higher antibacterial potency of quaternary N-alkylammonium bromides of