Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis (2020)
- Authors:
- Ribeiro, João A.
- Hammer, Alexander

- Zuniga, Gerardo A. Libreros

- Pacheco, Sair Maximo Chavez

- Tyrakis, Petros

- Oliveira, Gabriel S. de
- Kirkman, Timothy

- Bakali, Jamal El

- Rocco, Silvana A.

- Sforça, Mauricio L.

- Parise Filho, Roberto

- Coyne, Anthony G.

- Blundell, Tom L.

- Abell, Chris

- Dias, Marcio Vinicius Bertacine

- USP affiliated authors: PARISE FILHO, ROBERTO - FCF ; DIAS, MARCIO VINÍCIUS BERTACINE - ICB
- Unidades: FCF; ICB
- DOI: 10.1021/acsinfecdis.0c00263
- Subjects: MYCOBACTERIUM TUBERCULOSIS; ÁCIDO FÓLICO; MICROBIOLOGIA; INIBIDORES DE ENZIMAS; ATIVAÇÃO ENZIMÁTICA
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 2020
- Source:
- Título: ACS Infectious Diseases
- ISSN: 2373-8227
- Volume/Número/Paginação/Ano: v. 6, p. 2192−2201 : + Supplementary materials (p. S1-S16), 2020
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
RIBEIRO, João A. et al. Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis. ACS Infectious Diseases, v. 6, p. 2192−2201 : + Supplementary materials ( S1-S16), 2020Tradução . . Disponível em: https://doi.org/10.1021/acsinfecdis.0c00263. Acesso em: 10 fev. 2026. -
APA
Ribeiro, J. A., Hammer, A., Zuniga, G. A. L., Pacheco, S. M. C., Tyrakis, P., Oliveira, G. S. de, et al. (2020). Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis. ACS Infectious Diseases, 6, 2192−2201 : + Supplementary materials ( S1-S16). doi:10.1021/acsinfecdis.0c00263 -
NLM
Ribeiro JA, Hammer A, Zuniga GAL, Pacheco SMC, Tyrakis P, Oliveira GS de, Kirkman T, Bakali JE, Rocco SA, Sforça ML, Parise Filho R, Coyne AG, Blundell TL, Abell C, Dias MVB. Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis [Internet]. ACS Infectious Diseases. 2020 ; 6 2192−2201 : + Supplementary materials ( S1-S16).[citado 2026 fev. 10 ] Available from: https://doi.org/10.1021/acsinfecdis.0c00263 -
Vancouver
Ribeiro JA, Hammer A, Zuniga GAL, Pacheco SMC, Tyrakis P, Oliveira GS de, Kirkman T, Bakali JE, Rocco SA, Sforça ML, Parise Filho R, Coyne AG, Blundell TL, Abell C, Dias MVB. Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis [Internet]. ACS Infectious Diseases. 2020 ; 6 2192−2201 : + Supplementary materials ( S1-S16).[citado 2026 fev. 10 ] Available from: https://doi.org/10.1021/acsinfecdis.0c00263 - Optimization of new dihydrofolate reductase inhibitors of mycobacterium tuberculosis (mtDHFR): molecular docking, synthesis, evaluation of enzyme inhibition and antimycobacterial activity
- Design, synthesis and biological activity of novel substituted 3-benzoic acid derivatives as MtDHFR inhibitors
- Mycobacterium tuberculosis dihydrofolate reductase inhibitors: State of Art Past 20 Years
- Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis
- Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis
- Mechanistic insights into dideoxygenation in gentamicin biosynthesis
- Cloning, expression, purification and biophysical analysis of two putative halogenases from the glycopeptide A47,934 gene cluster of Streptomyces toyocaensis
- Enzymology of pyran ring A formation in salinomycin biosynthesis
- Abordagem estrutural sobre biossínteses, alvos, estratégias de desenvolvimento e resistência a antimicrobianos
- Mycobacterial OtsA structures unveil substrate preference mechanism and allosteric regulation by 2-oxoglutarate and 2-phosphoglycerate
Informações sobre o DOI: 10.1021/acsinfecdis.0c00263 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
