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Jean-Marie Frère

Researcher at University of Liège

Publications -  56
Citations -  2464

Jean-Marie Frère is an academic researcher from University of Liège. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 26, co-authored 56 publications receiving 2357 citations. Previous affiliations of Jean-Marie Frère include Pasteur Institute & Catholic University of Leuven.

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Standard Numbering Scheme for Class B β-Lactamases

TL;DR: This work proposes a scheme developed through a collaborative approach that preserves traditional numbering of catalytically important residues, is adaptable to new variants or enzymes yet to be discovered and includes a variation for genetic and epidemiological applications.
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Beta‐lactamases and bacterial resistance to antibiotics

TL;DR: The elucidation of the structures of some β‐lactamases by X‐ray crystallography has provided precious insights into their catalytic mechanisms and revealed unsuspected similarities with the DD‐transpeptidases, the bacterial enzymes which constitute the lethal targets of β‐ lactams.
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On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target

TL;DR: Significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.
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Mercaptophosphonate Compounds as Broad-Spectrum Inhibitors of the Metallo-β-lactamases

TL;DR: The inhibitory effect of mercaptophosphonate derivatives against the three subclasses of MBLs (B1, B2, and B3) is investigated and Interestingly, compound 18 turned out to be a potent broad spectrum MBL inhibitor.
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Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols.

TL;DR: Analysis of structural data and non-denturing mass spectrometric analyses led to the identification of broad spectrum inhibitors, including potent inhibitors of the CphA MBL (Aeromonas hydrophila), suggesting that the development of reasonably broad-spectrum MBL inhibitors should be possible.