Detalhe da pesquisa
1.
In-cell kinetic stability is an essential trait in metallo-ß-lactamase evolution.
Nat Chem Biol;
19(9): 1116-1126, 2023 09.
Artigo
em Inglês
| MEDLINE
| ID: mdl-37188957
2.
Interactions of hydrolyzed ß-lactams with the L1 metallo-ß-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products.
J Biol Chem;
299(5): 104606, 2023 05.
Artigo
em Inglês
| MEDLINE
| ID: mdl-36924941
3.
Relative inhibitory activities of the broad-spectrum ß-lactamase inhibitor taniborbactam against metallo-ß-lactamases.
Antimicrob Agents Chemother;
68(2): e0099123, 2024 Feb 07.
Artigo
em Inglês
| MEDLINE
| ID: mdl-38047644
4.
Structural basis of metallo-ß-lactamase resistance to taniborbactam.
Antimicrob Agents Chemother;
68(2): e0116823, 2024 Feb 07.
Artigo
em Inglês
| MEDLINE
| ID: mdl-38063400
5.
Structural role of K224 in taniborbactam inhibition of NDM-1.
Antimicrob Agents Chemother;
68(2): e0133223, 2024 Feb 07.
Artigo
em Inglês
| MEDLINE
| ID: mdl-38174924
6.
Deciphering the evolution of metallo-ß-lactamases: A journey from the test tube to the bacterial periplasm.
J Biol Chem;
298(3): 101665, 2022 03.
Artigo
em Inglês
| MEDLINE
| ID: mdl-35120928
7.
Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions.
Mol Biol Evol;
39(10)2022 10 07.
Artigo
em Inglês
| MEDLINE
| ID: mdl-36136729
8.
Metallo-ß-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Chem Rev;
121(13): 7957-8094, 2021 07 14.
Artigo
em Inglês
| MEDLINE
| ID: mdl-34129337
9.
Specific Protein-Membrane Interactions Promote Packaging of Metallo-ß-Lactamases into Outer Membrane Vesicles.
Antimicrob Agents Chemother;
65(10): e0050721, 2021 09 17.
Artigo
em Inglês
| MEDLINE
| ID: mdl-34310214
10.
Mitochondrial cytochrome c oxidase biogenesis: Recent developments.
Semin Cell Dev Biol;
76: 163-178, 2018 04.
Artigo
em Inglês
| MEDLINE
| ID: mdl-28870773
11.
Distinct Mechanisms of Dissemination of NDM-1 Metallo-ß-Lactamase in Acinetobacter Species in Argentina.
Antimicrob Agents Chemother;
64(5)2020 04 21.
Artigo
em Inglês
| MEDLINE
| ID: mdl-32122888
12.
A Standard Numbering Scheme for Class C ß-Lactamases.
Antimicrob Agents Chemother;
64(3)2020 02 21.
Artigo
em Inglês
| MEDLINE
| ID: mdl-31712217
13.
The Real Crisis in Antimicrobial Resistance: Failure to Anticipate and Respond.
Clin Infect Dis;
78(6): 1429-1433, 2024 Jun 14.
Artigo
em Inglês
| MEDLINE
| ID: mdl-38289748
14.
Dramatic Electronic Perturbations of CuA Centers via Subtle Geometric Changes.
J Am Chem Soc;
141(3): 1373-1381, 2019 01 23.
Artigo
em Inglês
| MEDLINE
| ID: mdl-30582893
15.
Formation and Electronic Structure of an Atypical CuA Site.
J Am Chem Soc;
141(11): 4678-4686, 2019 03 20.
Artigo
em Inglês
| MEDLINE
| ID: mdl-30807125
16.
The Reaction Mechanism of Metallo-ß-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.
Antimicrob Agents Chemother;
63(1)2019 01.
Artigo
em Inglês
| MEDLINE
| ID: mdl-30348667
17.
Fine Tuning of Functional Features of the CuA Site by Loop-Directed Mutagenesis.
Inorg Chem;
58(3): 2149-2157, 2019 Feb 04.
Artigo
em Inglês
| MEDLINE
| ID: mdl-30644741
18.
pH-Induced Binding of the Axial Ligand in an Engineered CuA Site Favors the πu State.
Inorg Chem;
58(23): 15687-15691, 2019 Dec 02.
Artigo
em Inglês
| MEDLINE
| ID: mdl-31710470
19.
Cross-class metallo-ß-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
Proc Natl Acad Sci U S A;
113(26): E3745-54, 2016 06 28.
Artigo
em Inglês
| MEDLINE
| ID: mdl-27303030
20.
Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations.
Int J Mol Sci;
20(15)2019 Aug 05.
Artigo
em Inglês
| MEDLINE
| ID: mdl-31387303