- Abstract:
- Crystallographic analyses of the VIM-5 metallo-β-lactamase (MBL) with isoquinoline inhibitors reveal non zinc ion binding modes. Comparison with other MBL-inhibitor structures directed addition of a zinc-binding thiol enabling identification of potent B1 MBL inhibitors. The inhibitors potentiate meropenem activity against clinical isolates harboring MBLs.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 708.3KB)
-
- Publisher copy:
- 10.1039/c7cc02394d
-
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- Publisher:
- Royal Society of Chemistry Publisher's website
- Journal:
- Chemical Communications Journal website
- Volume:
- 53
- Issue:
- 43
- Pages:
- 5806-5809
- Publication date:
- 2017-04-25
- Acceptance date:
- 2017-04-25
- DOI:
- EISSN:
-
1364-548X
- ISSN:
-
1359-7345
- Pubs id:
-
pubs:692202
- URN:
-
uri:299072f3-9b26-4398-8673-243a4336b9d7
- UUID:
-
uuid:299072f3-9b26-4398-8673-243a4336b9d7
- Local pid:
- pubs:692202
- Paper number:
- 43
- Language:
- English
- Copyright holder:
- Li et al.
- Copyright date:
- 2017
- Notes:
-
This is the accepted manuscript version of the article. The final version is available online from the Royal Society of Chemistry at: https://doi.org/10.1039/c7cc02394d
Journal article
Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition
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