Detalhe da pesquisa
1.
Deubiquitinating activity of SARS-CoV-2 papain-like protease does not influence virus replication or innate immune responses in vivo.
PLoS Pathog
; 20(3): e1012100, 2024 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-38527094
2.
Demonstrating the importance of porcine reproductive and respiratory syndrome virus papain-like protease 2 deubiquitinating activity in viral replication by structure-guided mutagenesis.
PLoS Pathog
; 19(12): e1011872, 2023 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-38096325
3.
Ubiquitin variants potently inhibit SARS-CoV-2 PLpro and viral replication via a novel site distal to the protease active site.
PLoS Pathog
; 18(12): e1011065, 2022 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-36548304
4.
Biochemical Insights into Imipenem Collateral Susceptibility Driven by ampC Mutations Conferring Ceftolozane/Tazobactam Resistance in Pseudomonas aeruginosa.
Antimicrob Agents Chemother
; 67(2): e0140922, 2023 02 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-36715512
5.
The endopeptidase of the maize-affecting Marafivirus type member maize rayado fino virus doubles as a deubiquitinase.
J Biol Chem
; 297(2): 100957, 2021 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-34265303
6.
Molecular characterization of the RNA-protein complex directing -2/-1 programmed ribosomal frameshifting during arterivirus replicase expression.
J Biol Chem
; 295(52): 17904-17921, 2020 12 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-33127640
7.
Frontrunners in the race to develop a SARS-CoV-2 vaccine.
Can J Microbiol
; 67(3): 189-212, 2021 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-33264067
8.
Adding Insult to Injury: Mechanistic Basis for How AmpC Mutations Allow Pseudomonas aeruginosa To Accelerate Cephalosporin Hydrolysis and Evade Avibactam.
Antimicrob Agents Chemother
; 64(9)2020 08 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-32660987
9.
Structural and mechanistic analysis of a ß-glycoside phosphorylase identified by screening a metagenomic library.
J Biol Chem
; 293(9): 3451-3467, 2018 03 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-29317495
10.
Molecular Basis for the Potent Inhibition of the Emerging Carbapenemase VCC-1 by Avibactam.
Antimicrob Agents Chemother
; 63(4)2019 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-30782990
11.
Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants.
PLoS Pathog
; 13(5): e1006372, 2017 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-28542609
12.
Synergistic activity of fosfomycin, ß-lactams and peptidoglycan recycling inhibition against Pseudomonas aeruginosa.
J Antimicrob Chemother
; 72(2): 448-454, 2017 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-27999022
13.
Letter to the Editor.
Mol Ther
; 29(1): 3, 2021 01 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-33321097
14.
Transactivation of programmed ribosomal frameshifting by a viral protein.
Proc Natl Acad Sci U S A
; 111(21): E2172-81, 2014 May 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-24825891
15.
The ß-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide.
J Biol Chem
; 290(5): 2630-43, 2015 Jan 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-25480792
16.
Producing glucose 6-phosphate from cellulosic biomass: structural insights into levoglucosan bioconversion.
J Biol Chem
; 290(44): 26638-48, 2015 Oct 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-26354439
17.
Viral OTU deubiquitinases: a structural and functional comparison.
PLoS Pathog
; 10(3): e1003894, 2014 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-24676359
18.
Deubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cells.
Proc Natl Acad Sci U S A
; 110(9): E838-47, 2013 Feb 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-23401522
19.
Conformational itinerary of Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase during its catalytic cycle.
J Biol Chem
; 289(7): 4504-14, 2014 Feb 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-24362022
20.
Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression.
J Biol Chem
; 289(50): 34667-82, 2014 Dec 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-25320088