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NMR Backbone Assign...
NMR Backbone Assignment of VIM-2 and Identification of the Active Enantiomer of a Potential Inhibitor
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- Wieske, Lianne H. E. (author)
- Uppsala universitet,Institutionen för kemi - BMC
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- Bogaerts, Jonathan (author)
- Department of Chemistry, University of Antwerp, Antwerp 2020, Belgium
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- Leding, Albin A. M. (author)
- Uppsala universitet,Institutionen för kemi - BMC
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- Wilcox, Scott (author)
- Uppsala universitet,Institutionen för kemi - BMC
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- Andersson Rasmussen, Anna (author)
- Uppsala universitet,Institutionen för kemi - BMC
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- Leszczak, Kinga (author)
- Department of Chemistry, UiT The Arctic University of Norway, Tromsø 9037, Norway
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- Turunen, Lotta (author)
- Uppsala universitet,Institutionen för kemi - BMC
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- Herrebout, Wouter A. (author)
- Department of Chemistry, University of Antwerp, Antwerp 2020, Belgium
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- Hubert, Madlen (author)
- Uppsala universitet,Institutionen för kemi - BMC,Department of Chemistry − BMC, Uppsala University, Uppsala SE-751 23, Sweden
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- Bayer, Annette (author)
- Department of Chemistry, UiT The Arctic University of Norway, Tromsø 9037, Norway
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- Erdélyi, Máté (author)
- Uppsala universitet,Organisk kemi,Department of Chemistry − BMC, Uppsala University, Uppsala SE-751 23, Sweden
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(creator_code:org_t)
- 2022-01-28
- 2022
- English.
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In: ACS Medicinal Chemistry Letters. - : American Chemical Society (ACS). - 1948-5875. ; 13:2, s. 257-261
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Abstract
Subject headings
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- Carbapenem resistance caused by metallo-β-lactamases is a serious global challenge that, if not tackled efficiently, is expected to lead to millions of deaths in the coming decades. Verona-integron encoded metallo-β-lactamase 2 (VIM-2) is a bacterial enzyme that has been reported from multidrug-resistant nosocomial isolates of Pseudomonas aeruginosa and other Gram-negative pathogens. As it hydrolyzes most β-lactams efficiently, including carbapenems, it is a major threat to current antimicrobial chemotherapies. So far, there is no clinically applicable inhibitor for this enzyme. In this work, the backbone NMR resonance assignment of VIM-2 is disclosed, opening up NMR investigations of this clinically important enzyme and its potential inhibitors for solutions, enabling a rational improvement of inhibitor candidates. Making use of the assignment, we identified the active enantiomer of a VIM-2 inhibitor candidate as well as its possible binding site and Kd, utilizing NMR chemical shift titration experiments.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Wieske, Lianne H ...
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Bogaerts, Jonath ...
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Leding, Albin A. ...
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Wilcox, Scott
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Andersson Rasmus ...
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Leszczak, Kinga
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show more...
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Turunen, Lotta
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Herrebout, Woute ...
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Hubert, Madlen
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Bayer, Annette
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Erdélyi, Máté
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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ACS Medicinal Ch ...
- By the university
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Uppsala University