Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Andreas Haldimann"'
Autor:
Dor Russ, Fabian Glaser, Einat Shaer Tamar, Idan Yelin, Michael Baym, Eric D. Kelsic, Claudia Zampaloni, Andreas Haldimann, Roy Kishony
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Beta-lactam antibiotics and beta-lactamase inhibitors compete for the same binding site on beta-lactamases; thus, mutations that increase beta-lactamase activity likely increase also susceptibility to the inhibitor. Here, Russ et al. identify rare mu
Externí odkaz:
https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b34
Autor:
Michael H. Baym, Claudia Zampaloni, Roy Kishony, Andreas Haldimann, Fabian Glaser, Idan Yelin, Dor Russ, Eric D. Kelsic, Einat Shaer Tamar
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications
Nature Communications
Beta-lactamase inhibitors are increasingly used to counteract antibiotic resistance mediated by beta-lactamase enzymes. These inhibitors compete with the beta-lactam antibiotic for the same binding site on the beta-lactamase, thus generating an evolu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b0d9aff47b7d0289c60b3d57610c7c3
https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b34
https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b34
Autor:
Claudia Zampaloni, Rusudan Okujava, Isabelle Walter, Caterina Bissantz, Elisabet I. Nielsen, Tianlai Shi, Andreas Haldimann, Anders N. Kristoffersson
Publikováno v:
Journal of Antimicrobial Chemotherapy.
Background Diazabicyclooctanes (DBOs) are an increasingly important group of non β-lactam β-lactamase inhibitors, employed clinically in combinations such as ceftazidime/avibactam. The dose finding of such combinations is complicated using the trad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4efa4db951fbe72593dff9f89291a35e
https://doi.org/10.1093/jac/dkz440
https://doi.org/10.1093/jac/dkz440
Autor:
Fabian Glaser, Claudia Zampaloni, Einat Shaer Tamar, Dor Russ, Roy Kishony, Idan Yelin, Andreas Haldimann
Beta-lactamase inhibitors are increasingly used to counteract microbial resistance to beta-lactam antibiotics mediated by beta-lactamase enzymes. These inhibitors compete with the beta-lactam drug for the same binding site of the beta-lactamase, ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b1bc61245061dc309d77fb869d0ed3d
Autor:
Melissa D. Barnes, Laura J. Rojas, Barry N. Kreiswirth, Michael R. Jacobs, Robert A. Bonomo, Caryn E. Good, Magdalena A. Taracila, Saralee Bajaksouzian, Krisztina M. Papp-Wallace, Andreas Haldimann, David van Duin
Publikováno v:
Antimicrobial agents and chemotherapy. 63(8)
Carbapenem-resistant Enterobacteriaceae (CRE) are resistant to most antibiotics, making CRE infections extremely difficult to treat with available agents. Klebsiella pneumoniae carbapenemases (KPC-2 and KPC-3) are predominant carbapenemases in CRE in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98e7badfa8bbcaf12613944e9d807a88
https://pubmed.ncbi.nlm.nih.gov/31182530
https://pubmed.ncbi.nlm.nih.gov/31182530
Publikováno v:
The Journal of antimicrobial chemotherapy. 74(4)
Background Diazabicyclooctanes (DBOs) are promising β-lactamase inhibitors. Some, including nacubactam (OP0595/RG6080), also bind PBP2 and have an enhancer effect, allowing activity against Enterobacteriaceae with MBLs, which DBOs do not inhibit. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bad9d476bbd64ea1fcb303be5368a4f2
https://pubmed.ncbi.nlm.nih.gov/30590470
https://pubmed.ncbi.nlm.nih.gov/30590470
Autor:
Ian Morrissey, Rusudan Okujava, Sophie Magnet, Claudia Zampaloni, Nimmi Kothari, Ian Harding, Andreas Haldimann, Kenneth Bradley, Fernando Garcia-Alcalde
Publikováno v:
Open Forum Infectious Diseases
Background Nacubactam (NAC, OP0595, RG6080) is a novel member of the diazabicyclooctane inhibitor family with a dual mode of action, acting as a β-lactamase inhibitor and an antibacterial agent by means of PBP2 inactivation. NAC restores and extends
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6398d02896407d62192294adda3a5b61
http://europepmc.org/articles/PMC6252560
http://europepmc.org/articles/PMC6252560
Autor:
Stephen Hawser, José M. Entenza, Philippe Moreillon, Marlyse Giddey, Andreas Haldimann, Sergio Lociuro
Publikováno v:
Antimicrobial Agents and Chemotherapy. 53:3635-3641
Iclaprim is a novel diaminopyrimidine antibiotic that is active against methicillin-resistant Staphylococcus aureus (MRSA). However, it is known that the activity of diaminopyrimidines against S. aureus is antagonized by thymidine through uptake and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cd255efff4bf5c97fbf136915f9431a
https://doi.org/10.1128/aac.00325-09
https://doi.org/10.1128/aac.00325-09
Autor:
Henk Schulz, Monica Bandera, Laurent Weiss, Christian Oefner, Sergio Lociuro, Heike Laue, Glenn E. Dale, Sandro Parisi, Seema Mukhija, Andreas Haldimann
Publikováno v:
Journal of Antimicrobial Chemotherapy. 63:687-698
Objectives Iclaprim is a novel 2,4-diaminopyrimidine that exhibits potent, rapid bactericidal activity against major Gram-positive pathogens, including methicillin-susceptible Staphylococcus aureus and methicillin-resistant S. aureus, and is currentl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::360cbedbac9234e0e180a3b32c35fbdc
https://doi.org/10.1093/jac/dkp024
https://doi.org/10.1093/jac/dkp024
Publikováno v:
Journal of Bacteriology. 185:2793-2801
An enzymatic pathway for synthesis of 5-phospho- d -ribosyl α-1-diphosphate (PRPP) without the participation of PRPP synthase was analyzed in Escherichia coli . This pathway was revealed by selection for suppression of the NAD requirement of strains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::341b10641e7fa7b5b4aa7926cbc82ae9
https://doi.org/10.1128/jb.185.9.2793-2801.2003
https://doi.org/10.1128/jb.185.9.2793-2801.2003