Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Matthias Negri"'
Autor:
Alessandro Spadaro, Matthias Negri, Sandrine Marchais-Oberwinkler, Emmanuel Bey, Martin Frotscher
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29252 (2012)
17β-estradiol (E2), the most potent estrogen in humans, known to be involved in the development and progession of estrogen-dependent diseases (EDD) like breast cancer and endometriosis. 17β-HSD1, which catalyses the reduction of the weak estrogen e
Externí odkaz:
https://doaj.org/article/8b5b42ff1bff47bcaee02bfde7a2d7c2
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e22990 (2011)
17β-Hydroxysteroid dehydrogenase type 1 (17β-HSD1) catalyzes the reduction of estrone to estradiol, which is the most potent estrogen in humans. Inhibition of 17β-HSD1 and thereby reducing the intracellular estradiol concentration is thus a promis
Externí odkaz:
https://doaj.org/article/45cc11ccb04c4095995648f3d3a5c1df
Publikováno v:
PLoS ONE, Vol 5, Iss 8, p e12026 (2010)
BACKGROUND: Bisubstrate enzymes, such as 17beta-hydroxysteroid dehydrogenase type 1 (17beta-HSD1), exist in solution as an ensemble of conformations. 17beta-HSD1 catalyzes the last step of the biosynthesis of estradiol and, thus, it is a potentially
Externí odkaz:
https://doaj.org/article/e66fec5fcce04a089132eb3c77e52ffa
Autor:
Pauline Banachowicz, Rolf W. Hartmann, Susanne Maria Weber, Christoph P. Sager, Matthias Negri, Gabriele Möller, Sandrine Marchais-Oberwinkler, Jerzy Adamski
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 206:105790
17β-Hydroxysteroid dehydrogenase type 2 (17β-HSD2) catalyzes the conversion of highly active estrogens and androgens into their less active forms using NAD+ as cofactor. Substrate and cofactor specificities of 17β-HSD2 have been reported and poten
Autor:
Christina Zimmer, Alessandra Bisi, Rolf W. Hartmann, Qingzhong Hu, Silvia Gobbi, Matthias Negri, Federica Belluti, Angela Rampa
Publikováno v:
Journal of Medicinal Chemistry. 56:1723-1729
Imidazolylmethylflavones previously reported by us as aromatase inhibitors proved to be able to interact with aldosterone synthase (CYP11B2), a cytochrome P450 enzyme involved in the biosynthesis of the mineralcorticoid hormone aldosterone, and were
Autor:
Rolf W. Hartmann, Matthias Negri, Matthias Groh, Stefan Hinsberger, Jörg Haupenthal, Kristina Hüsecken
Publikováno v:
Journal of Medicinal Chemistry. 56:8332-8338
The bacterial RNA polymerase (RNAP) is a validated target for broad spectrum antibiotics. However, the efficiency of drugs is reduced by resistance. To discover novel RNAP inhibitors, a pharmacophore based on the alignment of described inhibitors was
Autor:
Alberto Plaza, Andrea Braunshausen, Anke Steinbach, Elisabeth Weidel, Michael P. Storz, Christian Brengel, Matthias Negri, Johannes C. de Jong, Rolf W. Hartmann, Rolf Müller
Publikováno v:
Journal of Medicinal Chemistry. 56:6146-6155
Pseudomonas aeruginosa employs a characteristic pqs quorum sensing (QS) system that functions via the signal molecules PQS and its precursor HHQ. They control the production of a number of virulence factors and biofilm formation. Recently, we have sh
Publikováno v:
European Journal of Medicinal Chemistry. 65:223-231
Rising resistance against current antibiotics necessitates the development of antibacterial agents with alternative targets. The “switch region” of RNA polymerase (RNAP), addressed by the myxopyronins, could be such a novel target site. Based on
Peptide-Based Investigation of the Escherichia coli RNA Polymerase σ70:Core Interface As Target Site
Autor:
Rolf W. Hartmann, Stefan Boettcher, Joerg Haupenthal, Kristina Hüsecken, Martina Fruth, Matthias Negri
Publikováno v:
ACS Chemical Biology. 8:758-766
The number of bacterial strains that are resistant against antibiotics increased dramatically during the past decades. This fact stresses the urgent need for the development of new antibacterial agents with novel modes of action targeting essential e
Autor:
Jerzy Adamski, Rolf W. Hartmann, Marie Wetzel, Sandrine Marchais-Oberwinkler, Enrico Perspicace, Alex Odermatt, Gabriele Möller, Arne Meyer, Matthias Negri, Kuiying Xu
Publikováno v:
Journal of Medicinal Chemistry. 56:167-181
Inhibition of 17β-HSD2 is an attractive mechanism for the treatment of osteoporosis. We report here the optimization of human 17β-HSD2 inhibitors in the 2,5-thiophene amide class by varying the size of the linker (n equals 0 and 2) between the amid