Matches in SemOpenAlex for { <https://semopenalex.org/work/W4386779965> ?p ?o ?g. }
Showing items 1 to 53 of
53
with 100 items per page.
- W4386779965 abstract "The formation of dihydrouridine from uridine substrate is catalysed by the human tRNA-dihydrouridine synthase (hDus2) enzyme. The abundance of dihydrouridine, possibly accumulated due to the aberrant function of hDus2, is linked with carcinogenesis. In this study, we focused on hDus2 enzyme, in hopes of discovering novel molecule with affinity for its tRNA binding site. Using the computational method, we performed virtual screening of a natural compound library (NPACT) with Autodock Vina, followed by validation using Smina and Idock. The top hits ZINC08219592, ZINC44387960, and ZINC95098958 were further investigated for their ADME properties to assess their potential as drug candidates. Additionally, the electronic structure properties of the lead molecules were investigated using Density Functional Theory (DFT). Our findings suggest that the identified natural molecules may act as potential hDus2 binders, opening new possibilities for the development of targeted anticancer drugs. This study provides a foundation for further research and the potential advancement of cancer therapeutics targeting on hDus2." @default.
- W4386779965 created "2023-09-16" @default.
- W4386779965 date "2023-01-01" @default.
- W4386779965 modified "2023-09-27" @default.
- W4386779965 title "In In-silico Identification of Potential Inhibitors of Human Dihydrouridine Synthase 2 for Cancer Therapy" @default.
- W4386779965 doi "https://doi.org/10.56042/ijpap.v61i9.3495" @default.
- W4386779965 hasPublicationYear "2023" @default.
- W4386779965 type Work @default.
- W4386779965 citedByCount "0" @default.
- W4386779965 crossrefType "journal-article" @default.
- W4386779965 hasBestOaLocation W43867799651 @default.
- W4386779965 hasConcept C104317684 @default.
- W4386779965 hasConcept C159110408 @default.
- W4386779965 hasConcept C161624437 @default.
- W4386779965 hasConcept C181199279 @default.
- W4386779965 hasConcept C185592680 @default.
- W4386779965 hasConcept C202751555 @default.
- W4386779965 hasConcept C2775905019 @default.
- W4386779965 hasConcept C41685203 @default.
- W4386779965 hasConcept C55493867 @default.
- W4386779965 hasConcept C69366308 @default.
- W4386779965 hasConcept C70721500 @default.
- W4386779965 hasConcept C71924100 @default.
- W4386779965 hasConcept C86803240 @default.
- W4386779965 hasConceptScore W4386779965C104317684 @default.
- W4386779965 hasConceptScore W4386779965C159110408 @default.
- W4386779965 hasConceptScore W4386779965C161624437 @default.
- W4386779965 hasConceptScore W4386779965C181199279 @default.
- W4386779965 hasConceptScore W4386779965C185592680 @default.
- W4386779965 hasConceptScore W4386779965C202751555 @default.
- W4386779965 hasConceptScore W4386779965C2775905019 @default.
- W4386779965 hasConceptScore W4386779965C41685203 @default.
- W4386779965 hasConceptScore W4386779965C55493867 @default.
- W4386779965 hasConceptScore W4386779965C69366308 @default.
- W4386779965 hasConceptScore W4386779965C70721500 @default.
- W4386779965 hasConceptScore W4386779965C71924100 @default.
- W4386779965 hasConceptScore W4386779965C86803240 @default.
- W4386779965 hasLocation W43867799651 @default.
- W4386779965 hasOpenAccess W4386779965 @default.
- W4386779965 hasPrimaryLocation W43867799651 @default.
- W4386779965 hasRelatedWork W2064956914 @default.
- W4386779965 hasRelatedWork W2288137038 @default.
- W4386779965 hasRelatedWork W2398288423 @default.
- W4386779965 hasRelatedWork W2905695153 @default.
- W4386779965 hasRelatedWork W2964783067 @default.
- W4386779965 hasRelatedWork W3113194108 @default.
- W4386779965 hasRelatedWork W3124243165 @default.
- W4386779965 hasRelatedWork W3197716319 @default.
- W4386779965 hasRelatedWork W4206955939 @default.
- W4386779965 hasRelatedWork W4319350709 @default.
- W4386779965 isParatext "false" @default.
- W4386779965 isRetracted "false" @default.
- W4386779965 workType "article" @default.