Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Acyldepsipeptide antibiotics"'
Autor:
Jason K. Sello, Shashank Gupta, Robert T. Sauer, Emma L. Handy, Corey L. Compton, William R. Bishai, Karl R. Schmitz
Publikováno v:
ACS Chemical Biology. 18:724-733
Proteolytic complexes in Mycobacterium tuberculosis (Mtb), the deadliest bacterial pathogen, are major foci in tuberculosis drug development programs. The Clp proteases, which are essential for Mtb viability, are high priority targets. These protease
Autor:
Marie-Theres Vielberg, Peter Sass, Dhana Thomy, Michael Groll, Heike Brötz-Oesterhelt, Helena Carla Castro, Jan Straetener, Rebeca Pereira, Christian Mayer, Kirsten Famulla, Imran Malik
Publikováno v:
Chembiochem
Acyldepsipeptide (ADEP) is an exploratory antibiotic with a novel mechanism of action. ClpP, the proteolytic core of the caseinolytic protease, is deregulated towards unrestrained proteolysis. Here, we report on the mechanism of ADEP resistance in Fi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e7bafe0344f07a33b8c87f5fd0f4c58
https://mediatum.ub.tum.de/doc/1575885/document.pdf
https://mediatum.ub.tum.de/doc/1575885/document.pdf
Autor:
Robert H. Vass, Peter Chien
Publikováno v:
Molecular Microbiology. 101:183-185
Infection by Mycobacterium tuberculosis (Mtb) has had a devastating effect on the world population. Acyldepsipeptide antibiotics (ADEPs) are known to kill some bacteria by over activating the bacterial ClpP peptidase. ADEP antibiotics also target Mtb
Autor:
Heike Brötz-Oesterhelt, Imran Malik
Publikováno v:
Natural product reports. 34(7)
Covering: up to 2017The bacterial Clp protease is a highly conserved and structurally versatile machine. It has gained a lot of recognition during the last decade as a novel antibacterial drug target with an unprecedented mechanism of action. Due to
Publikováno v:
Journal of the American Chemical Society
The cyclic acyldepsipeptide (ADEP) antibiotics are a new class of antibacterial agents that kill bacteria via a mechanism that is distinct from all clinically used drugs. These molecules bind and dysregulate the activity of the ClpP peptidase. The po
Autor:
Heike Brötz-Oesterhelt, Peter Sass
Publikováno v:
International Journal of Medical Microbiology. 304:23-30
Bacterial Clp proteases are important for protein turnover and homeostasis in order to maintain vital cellular functions particularly under stress conditions. Apart from their crucial role in general protein quality control by degrading abnormally fo
Autor:
Fernando Gil, Daniel Paredes-Sabja
Publikováno v:
Future microbiology. 11
Alternative antimicrobial therapies based on acyldepsipeptides may hold promising results, based on the fact that they have shown to efficiently eradicate persister cells, stationary cells and cell in biofilm structures of several pathogenic bacteria
Autor:
Imran Malik, Helga Ruebsamen-Schaeff, Heike Brötz-Oesterhelt, Peter Sass, Berthold Hinzen, Marina Alber, Kirsten Famulla, Rainer Kalscheuer, Alfred L. Goldberg, Olga Kandror, Tatos Akopian
Publikováno v:
Molecular microbiology. 101(2)
The Clp protease complex in Mycobacterium tuberculosis is unusual in its composition, functional importance, and activation mechanism. While most bacterial species contain a single ClpP protein that is dispensable for normal growth, mycobacteria have
Autor:
Hans-Georg Sahl, Guido Schiffer, Kirsten Famulla, Michaele Josten, Peter Sass, Leendert W. Hamoen, Heike Brötz-Oesterhelt
Publikováno v:
Proceedings of the National Academy of Sciences. 108:17474-17479
The worldwide spread of antibiotic-resistant bacteria has lent urgency to the search for antibiotics with new modes of action that are devoid of preexisting cross-resistances. We previously described a unique class of acyldepsipeptides (ADEPs) that e
Publikováno v:
Bioorganic & Medicinal Chemistry. 18:7193-7202
A class of cyclic acyldepsipeptide antibiotics collectively known as the enopeptins has recently attracted much attention because of their activity against multidrug-resistant bacteria, including methicillin-resistant Staphylococcus aureus and vancom