scholarly article | Q13442814 |
P50 | author | Andrzej Joachimiak | Q28028611 |
Mateusz Wilamowski | Q59696007 | ||
Youngchang Kim | Q92028036 | ||
P2093 | author name string | Natalia Maltseva | |
Christine Tesar | |||
Michael Endres | |||
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Structural basis for the role of Asp-120 in metallo-beta-lactamases | Q27647482 | ||
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia | Q27649023 | ||
Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols | Q27650886 | ||
The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site | Q27656866 | ||
Crystal Structures of Penicillin-Binding Protein 3 from Pseudomonas aeruginosa: Comparison of Native and Antibiotic-Bound Forms | Q27665349 | ||
Structural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor Mercaptoacetate | Q27674549 | ||
The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution | Q27766004 | ||
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Challenges in the Development of a Thiol-Based Broad-Spectrum Inhibitor for Metallo-β-Lactamases | Q48239716 | ||
Crystal Structure of Pseudomonas aeruginosa SPM-1 Provides Insights into Variable Zinc Affinity of Metallo-β-lactamases | Q53103213 | ||
Characterization of purified New Delhi metallo-β-lactamase-1. | Q53210242 | ||
Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates. | Q53706201 | ||
Active-Site Conformational Fluctuations Promote the Enzymatic Activity of NDM-1 | Q57789714 | ||
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Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity | Q89126750 | ||
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NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism | Q30539117 | ||
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Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers | Q34498607 | ||
Postgenomic scan of metallo-beta-lactamase homologues in rhizobacteria: identification and characterization of BJP-1, a subclass B3 ortholog from Bradyrhizobium japonicum | Q34680616 | ||
Occurrence of Antibiotic Resistance Genes and Bacterial Markers in a Tropical River Receiving Hospital and Urban Wastewaters | Q35933905 | ||
Metallo-beta-lactamases: two binding sites for one catalytic metal ion? | Q35959544 | ||
Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily | Q36863408 | ||
Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes | Q37065167 | ||
Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site | Q37287914 | ||
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Catalytic role of the metal ion in the metallo-beta-lactamase GOB. | Q39541312 | ||
Structural and Biochemical Characterization of Rm3, a Subclass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study. | Q39588086 | ||
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Crystal structure and kinetic analysis of the class B3 di-zinc metallo-β-lactamase LRA-12 from an Alaskan soil metagenome. | Q41153799 | ||
Covalent inhibition of New Delhi metallo-β-lactamase-1 (NDM-1) by cefaclor | Q41706618 | ||
Characterization of the kinetic and thermodynamic landscape of RNA folding using a novel application of isothermal titration calorimetry | Q41851043 | ||
An overview of the kinetic parameters of class B beta-lactamases | Q42797036 | ||
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Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens. | Q46286684 | ||
Antibiotic recognition by binuclear metallo-beta-lactamases revealed by X-ray crystallography | Q46746983 | ||
The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis | Q47263304 | ||
The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site. | Q48080395 | ||
1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases | Q48143694 | ||
Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594. | Q48231746 | ||
P433 | issue | 3 | |
P921 | main subject | Stenotrophomonas maltophilia | Q142705 |
emerging pathogen | Q108429945 | ||
P304 | page(s) | 723-743 | |
P577 | publication date | 2019-12-24 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity | |
P478 | volume | 29 |
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