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Explore antimicrobial resistance genes from the literature
extended-spectrum class A beta-lactamase BEL-1
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| blaBEL-1 | Card DatabaseReference Gene CatalogResFinder DatabaseReslit | 7 | TICARCILLIN, CEPHALOSPORIN +15 |
| Belgium, Spain|China|Taiwan |
| 2005, 2016, 2025 |
| DQ089809.1 |
| AAZ04368.1 |
| blaBEL-2 | Card DatabaseReference Gene CatalogResFinder DatabaseReslit | 5 | TICARCILLIN, CEPHALOSPORIN +14 | Pseudomonas aeruginosa +1 | Belgium | 2010 | FJ666063.1 | ACV69996.1 |
| blaBEL-3 | Card DatabaseReference Gene CatalogResFinder DatabaseReslit | 5 | TICARCILLIN, CEPHALOSPORIN +13 | Pseudomonas aeruginosa | Spain | 2010 | GQ202694.1 | ACT09140.1 |
| blaBEL-4 | Card DatabaseReference Gene CatalogResFinder Database | 4 | TICARCILLIN, CEPHALOSPORIN +10 | Pseudomonas aeruginosa | - | - | KX388629.1 | ANM44757.1 |
| blaBEL-5 | Reference Gene Catalog | 1 | CEPHALOSPORIN | Pseudomonas aeruginosa | - | - | PV474612.1 | XRI57711.1 |
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.
The study identifies BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, which hydrolyzes expanded-spectrum cephalosporins and aztreonam. BEL-1 is encoded in a class 1 integron In120 in Pseudomonas aeruginosa.
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa.
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa.
The study identifies BEL-2, a novel extended-spectrum beta-lactamase in Pseudomonas aeruginosa, which exhibits increased activity towards expanded-spectrum cephalosporins compared to BEL-1.
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa.
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa.
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa.
Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
The study identifies blaOXA-144 and blaBEL-3 as new acquired β-lactamases contributing to resistance in carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains.
Crystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum beta-lactamase and Its Complexes with Moxalactam and Imipenem.
The study describes the crystal structure of the BEL-1 extended-spectrum beta-lactamase from Pseudomonas aeruginosa and its complexes with moxalactam and imipenem, highlighting the structural features that contribute to its resistance properties.
Broad spectrum of β-lactamase coverage and potent antimicrobial activity of xeruborbactam in combination with meropenem against carbapenemase-producing Enterobacterales, including strains resistant to new β-lactam/β-lactamase inhibitor combinations.
Xeruborbactam in combination with meropenem shows potent activity against carbapenemase-producing Enterobacterales, including strains resistant to other β-lactam/β-lactamase inhibitor combinations. Specific β-lactamases like blaIMP-23 and blaSPM-1 were identified as resistant to xeruborbactam.
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