Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Veronika Škedelj"'
Autor:
Martina Hrast, Kaja Rožman, Iza Ogris, Veronika Škedelj, Delphine Patin, Matej Sova, Hélène Barreteau, Stanislav Gobec, Simona Golič Grdadolnik, Anamarija Zega
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 1010-1017 (2019)
The Mur ligases form a series of consecutive enzymes that participate in the intracellular steps of bacterial peptidoglycan biosynthesis. They therefore represent interesting targets for antibacterial drug discovery. MurC, D, E and F are all ATP-depe
Externí odkaz:
https://doaj.org/article/611a82a2fe88425aaa24c3fa2a9502bd
Autor:
Veronika Škedelj, Emilija Arsovska, Tihomir Tomašić, Ana Kroflič, Vesna Hodnik, Martina Hrast, Marija Bešter-Rogač, Gregor Anderluh, Stanislav Gobec, Julieanne Bostock, Ian Chopra, Alex J O'Neill, Christopher Randall, Anamarija Zega
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e39922 (2012)
BACKGROUND: ATP-dependent D-alanine:D-alanine ligase (Ddl) is a part of biochemical machinery involved in peptidoglycan biosynthesis, as it catalyzes the formation of the terminal D-ala-D-ala dipeptide of the peptidoglycan precursor UDPMurNAc-pentape
Externí odkaz:
https://doaj.org/article/c1d486e583d44c8eac076f7ed3fbdb08
Autor:
Kaja Rožman, Delphine Patin, Stanislav Gobec, Matej Sova, Hélène Barreteau, Veronika Škedelj, Simona Golic Grdadolnik, Iza Ogris, Anamarija Zega, Martina Hrast
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry
Journal of Enzyme Inhibition and Medicinal Chemistry, Informa Healthcare, 2019, 34 (1), pp.1010--1017. ⟨10.1080/14756366.2019.1608981⟩
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 1010-1017 (2019)
Journal of Enzyme Inhibition and Medicinal Chemistry, 2019, 34 (1), pp.1010--1017. ⟨10.1080/14756366.2019.1608981⟩
Journal of Enzyme Inhibition and Medicinal Chemistry, Informa Healthcare, 2019, 34 (1), pp.1010--1017. ⟨10.1080/14756366.2019.1608981⟩
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 1010-1017 (2019)
Journal of Enzyme Inhibition and Medicinal Chemistry, 2019, 34 (1), pp.1010--1017. ⟨10.1080/14756366.2019.1608981⟩
International audience; The Mur ligases form a series of consecutive enzymes that participate in the intracellular steps of bacterial peptidoglycan biosynthesis. They therefore represent interesting targets for antibacterial drug discovery. MurC, D,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1932abd8087edcfa8a7927f6fa884665
https://hal.archives-ouvertes.fr/hal-02171151
https://hal.archives-ouvertes.fr/hal-02171151
Autor:
Peter Molek, Veronika Škedelj, Jure Stojan, Anamarija Zega, Didier Blanot, Jean-Luc Mainardi, Urša Pečar Fonović, Stanislav Gobec, Sophie Magnet
Publikováno v:
Biochimie
Biochimie, Elsevier, 2019, 158, pp.217--223. ⟨10.1016/j.biochi.2019.01.012⟩
Biochimie, 2019, 158, pp.217--223. ⟨10.1016/j.biochi.2019.01.012⟩
Biochimie, Elsevier, 2019, 158, pp.217--223. ⟨10.1016/j.biochi.2019.01.012⟩
Biochimie, 2019, 158, pp.217--223. ⟨10.1016/j.biochi.2019.01.012⟩
International audience; Enterococcus faecium D-aspartate ligase (Aslfm) is a peptide bond-forming enzyme that is involved in the peptidoglycan assembly pathway. It catalyzes the ATP-dependent ligation of the β-carboxylate of D-Asp to the ε-amino gr
Publikováno v:
Journal of Medicinal Chemistry. 54:915-929
Autor:
Jure Stojan, Matjaž Brvar, Ana Kroflič, Victoria J. Savage, Jean-Luc Mainardi, Anamarija Zega, Vincent Dubbée, Alex J. O'Neill, Tom Solmajer, Didier Blanot, Andrej Perdih, Michel Arthur, Jean-Emmanuel Hugonnet, Marija Bešter-Rogač, Sophie Magnet, Veronika Škedelj
Publikováno v:
European journal of medicinal chemistry. 67
The d -aspartate ligase of Enterococcus faecium (Asl fm ) is an attractive target for the development of narrow-spectrum antibacterial agents that are active against multidrug-resistant E. faecium. Although there is currently little available informa
Autor:
Christopher P. Randall, Julieanne M. Bostock, Tihomir Tomašič, Marija Bešter-Rogač, Ian Chopra, Ana Kroflič, Veronika Škedelj, Stanislav Gobec, Martina Hrast, Anamarija Zega, Gregor Anderluh, Vesna Hodnik, Alex J. O'Neill, Emilija Arsovska
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e39922 (2012)
PLoS ONE
PLoS ONE
BACKGROUND: ATP-dependent D-alanine:D-alanine ligase (Ddl) is a part of biochemical machinery involved in peptidoglycan biosynthesis, as it catalyzes the formation of the terminal D-ala-D-ala dipeptide of the peptidoglycan precursor UDPMurNAc-pentape