Please use this identifier to cite or link to this item:
http://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/13346
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Murugesan, Sankaranarayanan | - |
dc.date.accessioned | 2023-12-11T10:48:29Z | - |
dc.date.available | 2023-12-11T10:48:29Z | - |
dc.date.issued | 2021-01 | - |
dc.identifier.uri | https://www.future-science.com/doi/10.4155/fmc-2020-0257 | - |
dc.identifier.uri | http://dspace.bits-pilani.ac.in:8080/xmlui/handle/123456789/13346 | - |
dc.description.abstract | Reverse transcriptase and integrase are key enzymes that play a pivotal role in HIV-1 viral maturation and replication. Reverse transcriptase consists of two active sites: RNA-dependent DNA polymerase and RNase H. The catalytic domains of integrase and RNase H share striking similarity, comprising two aspartates and one glutamate residue, also known as the catalytic DDE triad, and a Mg2+ pair. The simultaneous inhibition of reverse transcriptase and integrase can be a rational drug discovery approach for combating the emerging drug resistance problem. In the present review, the dual inhibition of RNase H and integrase is systematically discussed, including rationality of design, journey of development, advancement and future perspective | en_US |
dc.language.iso | en | en_US |
dc.publisher | Future Science Group | en_US |
dc.subject | Pharmacy | en_US |
dc.subject | Dual inhibition | en_US |
dc.subject | Reverse transcriptase (RT) | en_US |
dc.subject | Integrase | en_US |
dc.subject | Molecular hybridization | en_US |
dc.subject | Resistancereverse transcriptase | en_US |
dc.title | Search for new therapeutics against HIV-1 via dual inhibition of RNase H and integrase: current status and future challenges | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Pharmacy |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.