Molecular dynamics simulations suggest SARS-CoV-2 3CLpro mutations in Beta and Omicron variants do not alter binding affinities for cleavage sites of non-structural proteins (2023)
- Authors:
- USP affiliated authors: CARVALHO, CRISTIANE RODRIGUES GUZZO - ICB ; AMORIM, VITOR MARTINS DE FREITAS - ICB ; SOUZA, ANACLETO SILVA DE - ICB
- Unidade: ICB
- DOI: 10.3390/covid3040044
- Subjects: MICROBIOLOGIA; COVID-19; MUTAÇÃO GENÉTICA; ENZIMAS PROTEOLÍTICAS; REPLICAÇÃO VIRAL; TRANSCRIÇÃO GÊNICA; INFECÇÕES POR VÍRUS DE RNA
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
ABNT
AMORIM, Vitor Martins de3 Freitas et al. Molecular dynamics simulations suggest SARS-CoV-2 3CLpro mutations in Beta and Omicron variants do not alter binding affinities for cleavage sites of non-structural proteins. COVID, v. 3, n. 4, p. 622-636, 2023Tradução . . Disponível em: https://doi.org/10.3390/covid3040044. Acesso em: 29 dez. 2025. -
APA
Amorim, V. M. de3 F., Souza, R. F. de, Souza, A. S. de, & Guzzo, C. R. (2023). Molecular dynamics simulations suggest SARS-CoV-2 3CLpro mutations in Beta and Omicron variants do not alter binding affinities for cleavage sites of non-structural proteins. COVID, 3( 4), 622-636. doi:10.3390/covid3040044 -
NLM
Amorim VM de3 F, Souza RF de, Souza AS de, Guzzo CR. Molecular dynamics simulations suggest SARS-CoV-2 3CLpro mutations in Beta and Omicron variants do not alter binding affinities for cleavage sites of non-structural proteins [Internet]. COVID. 2023 ; 3( 4): 622-636.[citado 2025 dez. 29 ] Available from: https://doi.org/10.3390/covid3040044 -
Vancouver
Amorim VM de3 F, Souza RF de, Souza AS de, Guzzo CR. Molecular dynamics simulations suggest SARS-CoV-2 3CLpro mutations in Beta and Omicron variants do not alter binding affinities for cleavage sites of non-structural proteins [Internet]. COVID. 2023 ; 3( 4): 622-636.[citado 2025 dez. 29 ] Available from: https://doi.org/10.3390/covid3040044 - Molecular dynamics simulations of the spike trimeric ectodomain of the SARS-CoV-2 Omicron variant: structural relationships with infectivity, evasion to immune system and transmissibility
- Cooperative and structural relationships of the trimeric Spike with infectivity and antibody escape of the strains Delta (B.1.617.2) and Omicron (BA.2, BA.5, and BQ.1)
- Molecular dynamics analysis of fast-spreading severe acute respiratory syndrome coronavirus 2 variants and their effects on the interaction with human angiotensin-converting enzyme 2
- Antagonistic trends between binding affinity and drug-Likeness in SARS-CoV-2 Mpro inhibitors revealed by machine learning
- Quantitative structure-activity relationships, molecular docking and molecular dynamics simulations reveal drug repurposing candidates as potent SARS-CoV-2 main protease inhibitors
- Severe acute respiratory syndrome Coronavirus 2 variants of concern: a perspective for emerging more transmissible and vaccine-resistant strains
- 3-Chymotrypsin-like Protease (3CLpro) of SARS-CoV-2: validation as a molecular target, proposal of a novel catalytic mechanism, and inhibitors in preclinical and clinical trials
- Relações quantitativas entre a estrutura e atividade para uma série de antichagásicos derivados do fenarimol
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths
- Estudos em quimioinformática baseados na estrutura do ligante e do receptor de candidatos a agentes antichagásicos
Informações sobre o DOI: 10.3390/covid3040044 (Fonte: oaDOI API)
Download do texto completo
| Tipo | Nome | Link | |
|---|---|---|---|
 |
Molecular Dynamics Simula... | Direct link |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
