Karina Calvopina
Overview
Explore the profile of Karina Calvopina including associated specialties, affiliations and a list of published articles.
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22
Citations
278
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Recent Articles
1.
Hinchliffe P, Calvopina K, Rabe P, Mojica M, Schofield C, Dmitrienko G, et al.
J Biol Chem
. 2024 Oct;
300(10):107819.
PMID: 39383701
No abstract available.
2.
de Munnik M, Lang P, Calvopina K, Rabe P, Brem J, Schofield C
Commun Biol
. 2024 Sep;
7(1):1173.
PMID: 39294212
The essential L,D-transpeptidase of Mycobacterium tuberculosis (Ldt) catalyses the formation of 3 3 cross-links in cell wall peptidoglycan and is a target for development of antituberculosis therapeutics. Efforts to inhibit...
3.
Hinchliffe P, Calvopina K, Rabe P, Mojica M, Schofield C, Dmitrienko G, et al.
J Biol Chem
. 2023 Mar;
299(5):104606.
PMID: 36924941
L1 is a dizinc subclass B3 metallo-β-lactamase (MBL) that hydrolyzes most β-lactam antibiotics and is a key resistance determinant in the Gram-negative pathogen Stenotrophomonas maltophilia, an important cause of nosocomial...
4.
Lucic A, Malla T, Calvopina K, Tooke C, Brem J, McDonough M, et al.
Antibiotics (Basel)
. 2022 Mar;
11(3).
PMID: 35326858
Carbapenems are important antibacterials and are both substrates and inhibitors of some β-lactamases. We report studies on the reaction of the unusual carbapenem biapenem, with the subclass B1 metallo-β-lactamases VIM-1...
5.
Brem J, Panduwawala T, Ulf Hansen J, Hewitt J, Liepins E, Donets P, et al.
Nat Chem
. 2021 Dec;
14(1):15-24.
PMID: 34903857
Carbapenems are vital antibiotics, but their efficacy is increasingly compromised by metallo-β-lactamases (MBLs). Here we report the discovery and optimization of potent broad-spectrum MBL inhibitors. A high-throughput screen for NDM-1...
6.
Soor H, Diaz D, Tsui K, Calvopina K, Bielinski M, Tantillo D, et al.
J Org Chem
. 2021 Dec;
87(1):94-102.
PMID: 34898194
Amidoboronic acid-containing peptidomimetics are an important class of scaffolds in chemistry and drug discovery. Despite increasing interest in boron-based enzyme inhibitors, constrained amidoboronic acids have received little attention due to...
7.
Farley A, Ermolovich Y, Calvopina K, Rabe P, Panduwawala T, Brem J, et al.
ACS Infect Dis
. 2021 Oct;
7(11):3124.
PMID: 34606235
No abstract available.
8.
Farley A, Ermolovich Y, Calvopina K, Rabe P, Panduwawala T, Brem J, et al.
ACS Infect Dis
. 2021 May;
7(6):1809-1817.
PMID: 34003651
Metallo-β-lactamases (MBLs) can efficiently catalyze the hydrolysis of all classes of β-lactam antibiotics except monobactams. While serine-β-lactamase (SBL) inhibitors (e.g., clavulanic acid, avibactam) are established for clinical use, no such...
9.
Lucic A, Hinchliffe P, Malla T, Tooke C, Brem J, Calvopina K, et al.
Eur J Med Chem
. 2021 Feb;
215:113257.
PMID: 33618159
Penems have demonstrated potential as antibacterials and β-lactamase inhibitors; however, their clinical use has been limited, especially in comparison with the structurally related carbapenems. Faropenem is an orally active antibiotic...
10.
Dulyayangkul P, Calvopina K, Heesom K, Avison M
Antimicrob Agents Chemother
. 2020 Nov;
65(1).
PMID: 33139281
Fluoroquinolone resistance in is multifactorial, but the most significant factor is overproduction of efflux pumps, particularly SmeDEF, following mutation. Here, we report that mutations in the glycosyl transferase gene in...