Detalhe da pesquisa
1.
AI-Accelerated Design of Targeted Covalent Inhibitors for SARS-CoV-2.
J Chem Inf Model
; 63(5): 1438-1453, 2023 03 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-36808989
2.
Unusual zwitterionic catalytic site of SARS-CoV-2 main protease revealed by neutron crystallography.
J Biol Chem
; 295(50): 17365-17373, 2020 12 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-33060199
3.
Potent and selective covalent inhibition of the papain-like protease from SARS-CoV-2.
Nat Commun
; 14(1): 1733, 2023 03 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-36977673
4.
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease: room-temperature X-ray and neutron crystallography, binding thermodynamics, and antiviral activity.
Res Sq
; 2022 Feb 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-35169792
5.
The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature.
bioRxiv
; 2022 Feb 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-35169801
6.
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease.
Nat Commun
; 13(1): 2268, 2022 04 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-35477935
7.
The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature.
Sci Adv
; 8(21): eabo5083, 2022 May 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-35622909
8.
Potent and Selective Covalent Inhibition of the Papain-like Protease from SARS-CoV-2.
Res Sq
; 2022 Jul 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-35898342
9.
Potent and Selective Covalent Inhibition of the Papain-like Protease from SARS-CoV-2.
Res Sq
; 2022 Jul 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-34642689
10.
Direct Observation of Protonation State Modulation in SARS-CoV-2 Main Protease upon Inhibitor Binding with Neutron Crystallography.
J Med Chem
; 64(8): 4991-5000, 2021 04 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-33755450
11.
Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like Protease with Human Interferon-Stimulated Gene 15 Protein.
J Phys Chem Lett
; 12(23): 5608-5615, 2021 Jun 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-34110168
12.
Structural, Electronic, and Electrostatic Determinants for Inhibitor Binding to Subsites S1 and S2 in SARS-CoV-2 Main Protease.
J Med Chem
; 64(23): 17366-17383, 2021 12 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-34705466
13.
Room-temperature neutron and X-ray data collection of 3CL Mpro from SARS-CoV-2.
Acta Crystallogr F Struct Biol Commun
; 76(Pt 10): 483-487, 2020 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-33006576
14.
Malleability of the SARS-CoV-2 3CL Mpro Active-Site Cavity Facilitates Binding of Clinical Antivirals.
Structure
; 28(12): 1313-1320.e3, 2020 12 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-33152262
15.
Room-temperature X-ray crystallography reveals the oxidation and reactivity of cysteine residues in SARS-CoV-2 3CL Mpro: insights into enzyme mechanism and drug design.
IUCrJ
; 7(Pt 6)2020 Sep 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-33063790
16.
Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography.
Nat Commun
; 11(1): 3202, 2020 06 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-32581217