CF
Antimalarials
/ chemistry
Binding Sites
Catalytic Domain
Dihydroorotate Dehydrogenase
Enzyme Inhibitors
/ chemistry
Molecular Dynamics Simulation
Oxidoreductases Acting on CH-CH Group Donors
/ chemistry
Plasmodium falciparum
/ enzymology
Protozoan Proteins
/ chemistry
Purines
/ chemistry
Pyridines
/ chemistry
Quantum Theory
Thermodynamics
Plasmodium falciparum
dihydroorotate dehydrogenase
malaria
molecular dynamics simulations
Journal
Chemistry & biodiversity
ISSN: 1612-1880
Titre abrégé: Chem Biodivers
Pays: Switzerland
ID NLM: 101197449
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
30
06
2019
accepted:
07
10
2019
pubmed:
8
10
2019
medline:
7
1
2020
entrez:
8
10
2019
Statut:
ppublish
Résumé
The quest for reliable dihydroorotate dehydrogenase (DHODH) inhibitors has engendered the discovery of potential therapeutic compounds at different stages of clinical trials. Although promising, high attrition rates and unfavorable bioactivities have limited their drug developmental progress. A recent structural modification of DSM265, a triazolopyrimidine-based inhibitor, yielded DSM421, derived by the substitution of the SF
Identifiants
pubmed: 31589372
doi: 10.1002/cbdv.201900365
doi:
Substances chimiques
Antimalarials
0
Dihydroorotate Dehydrogenase
0
Enzyme Inhibitors
0
Protozoan Proteins
0
Purines
0
Pyridines
0
triazolopyrimidinone
273-40-5
Oxidoreductases Acting on CH-CH Group Donors
EC 1.3.-
pyridine
NH9L3PP67S
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1900365Subventions
Organisme : College of Health Sciences
Organisme : University of KwaZulu-Natal
Organisme : Center for High-Performance Computing
Informations de copyright
© 2019 Wiley-VHCA AG, Zurich, Switzerland.
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