Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Denys Pogoryelov"'
Autor:
Shivam Yadav, Martin Centola, Mathilda Glaesmann, Denys Pogoryelov, Roman Ladig, Mike Heilemann, L. C. Rai, Özkan Yildiz, Enrico Schleiff
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
Cyclophilins are proteins found in many organisms, where they can play roles as chaperones, in signal transduction, or other functions. Here, Yadav et al. show that a cyanobacterial cyclophilin is involved in stress responses and in assembly of photo
Externí odkaz:
https://doaj.org/article/aeb1a1382d184d9496b491da6eb13521
Publikováno v:
FEBS Open Bio, Vol 10, Iss 2, Pp 221-228 (2020)
During translation initiation, the heterotrimeric archaeal translation initiation factor 2 (aIF2) recruits the initiator tRNAi to the small ribosomal subunit. In the stationary growth phase and/or during nutrient stress, Sulfolobus solfataricus aIF2
Externí odkaz:
https://doaj.org/article/1bf83389f2c44451b1d0e5ff73795c09
Autor:
René Blöcher, Kerstin Hiesinger, Sandra K. Wittmann, Jana Gerstmeier, Denys Pogoryelov, Annika Schott, Ewgenij Proschak, Finja Witt, Dieter Steinhilber, Oliver Werz, Jan S. Kramer
Publikováno v:
ACS Medicinal Chemistry Letters. 11:298-302
Multitarget anti-inflammatory drugs interfering with the arachidonic acid cascade exhibit superior efficacy. In this study, a prototype dual inhibitor of soluble epoxide hydrolase (sEH) and LTA4 hy...
Discovery of the First in Vivo Active Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain
Autor:
Stefano Woltersdorf, Thomas Duflot, Christophe Morisseau, Victor Hernandez-Olmos, Ewgenij Proschak, Apirat Chaikuad, Franca-M Klingler, Sandra K. Wittmann, Felix Knöll, Dieter Steinhilber, Jan S. Kramer, Felix F Lillich, Angelo Sala, Kerstin Hiesinger, Daniel Merk, Sylvain Fraineau, Jeremy Bellien, Bruce D. Hammock, Jan Heering, Steffen Brunst, Stefan Knapp, G. Enrico Rovati, Julie Rondeaux, Denys Pogoryelov, Carola Buccellati, Matthieu Leuillier
Publikováno v:
J Med Chem
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, 2019, 62 (18), pp.8443-8460. ⟨10.1021/acs.jmedchem.9b00445⟩
Journal of medicinal chemistry, vol 62, iss 18
Journal of Medicinal Chemistry, American Chemical Society, 2019, 62 (18), pp.8443-8460. ⟨10.1021/acs.jmedchem.9b00445⟩
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, 2019, 62 (18), pp.8443-8460. ⟨10.1021/acs.jmedchem.9b00445⟩
Journal of medicinal chemistry, vol 62, iss 18
Journal of Medicinal Chemistry, American Chemical Society, 2019, 62 (18), pp.8443-8460. ⟨10.1021/acs.jmedchem.9b00445⟩
International audience; The emerging pharmacological target soluble epoxide hydrolase (sEH) is a bifunctional enzyme exhibiting two different catalytic activities that are located in two distinct domains. Although the physiological role of the C-term
Autor:
Bettina Hofmann, Kerstin Hiesinger, Steffen Brunst, Timon Eckes, Carlo Angioni, Ewgenij Proschak, Dieter Steinhilber, Jan S. Kramer, Manfred Schubert-Zsilavecz, Gerd Geisslinger, Achim Schmidtko, Josef Pfeilschifter, Simon B.M. Kretschmer, Lilia Weizel, Sandra K. Wittmann, Sven George, Stephanie Schwalm, Sandra Beyer, Jan Heering, Cathrin Flauaus, Astrid Kaiser, Denys Pogoryelov
Publikováno v:
Journal of medicinal chemistry. 63(20)
Inhibition of multiple enzymes of the arachidonic acid cascade leads to synergistic anti-inflammatory effects. Merging of 5-lipoxygenase (5-LOX) and soluble epoxide hydrolase (sEH) pharmacophores led to the discovery of a dual 5-LOX/sEH inhibitor, wh
Autor:
Shivam, Yadav, Martin, Centola, Mathilda, Glaesmann, Denys, Pogoryelov, Roman, Ladig, Mike, Heilemann, L C, Rai, Özkan, Yildiz, Enrico, Schleiff
Publikováno v:
Nature communications. 13(1)
Cyclophilins, or immunophilins, are proteins found in many organisms including bacteria, plants and humans. Most of them display peptidyl-prolyl cis-trans isomerase activity, and play roles as chaperones or in signal transduction. Here, we show that
Autor:
Daniel Kohnhäuser, Markus Hartmann, Denia Frank, Sandra K. Wittmann, Dominik Büttner, Thomas A. Wichelhaus, Jan S. Kramer, Denys Pogoryelov, Christian Kurz, Lilia Weizel, Franca Maria Klingler, Astrid Brüggerhoff, Dieter Steinhilber, Ewgenij Proschak
Publikováno v:
ACS Infectious Diseases. 4:360-372
Pathogens, expressing metallo-β-lactamases (MBLs), become resistant against most β-lactam antibiotics. Besides the dragging search for new antibiotics, development of MBL inhibitors would be an alternative weapon against resistant bacterial pathoge
Autor:
Kerstin, Hiesinger, Annika, Schott, Jan S, Kramer, René, Blöcher, Finja, Witt, Sandra K, Wittmann, Dieter, Steinhilber, Denys, Pogoryelov, Jana, Gerstmeier, Oliver, Werz, Ewgenij, Proschak
Publikováno v:
ACS Med Chem Lett
[Image: see text] Multitarget anti-inflammatory drugs interfering with the arachidonic acid cascade exhibit superior efficacy. In this study, a prototype dual inhibitor of soluble epoxide hydrolase (sEH) and LTA(4) hydrolase (LTA(4)H) with submicromo
Autor:
Kerstin Hiesinger, Jan S. Kramer, Janosch Achenbach, Daniel Moser, Julia Weber, Sandra K. Wittmann, Christophe Morisseau, Carlo Angioni, Gerd Geisslinger, Astrid S. Kahnt, Astrid Kaiser, Anna Proschak, Dieter Steinhilber, Denys Pogoryelov, Karen Wagner, Bruce D. Hammock, Ewgenij Proschak
Publikováno v:
ACS Med Chem Lett
ACS medicinal chemistry letters, vol 10, iss 6
ACS medicinal chemistry letters, vol 10, iss 6
[Image: see text] Selective optimization of side activities is a valuable source of novel lead structures in drug discovery. In this study, a computer-aided approach was used to deorphanize the pleiotropic cholesterol-lowering effects of the beta-blo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17d0bd79212ad879a0f7127a657eeefd
https://publica.fraunhofer.de/handle/publica/258815
https://publica.fraunhofer.de/handle/publica/258815
Autor:
René Bloecher, Lena Kalinowsky, Dieter Steinhilber, Jan S. Kramer, Stefan Knapp, Ewgenij Proschak, Jan Heering, Denys Pogoryelov, Sandra K. Wittmann
Publikováno v:
Bioorganic & Medicinal Chemistry. 24:5243-5248
The leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme, containing a peptidase and a hydrolase activity both activities having opposing functions regulating inflammatory response. The hydrolase activity is responsible for the conversion of leu