Selected Publication:
SHR
Neuro
Cancer
Cardio
Lipid
Metab
Microb
Sánchez-Murcia, PA; de Castro, S; García-Aparicio, C; Jiménez, MA; Corona, A; Tramontano, E; Sluis-Cremer, N; Menéndez-Arias, L; Velázquez, S; Gago, F; Camarasa, MJ.
Peptides Mimicking the β7/β8 Loop of HIV-1 Reverse Transcriptase p51 as "Hotspot-Targeted" Dimerization Inhibitors.
ACS Med Chem Lett. 2020; 11(5):811-817
Doi: 10.1021/acsmedchemlett.9b00623
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Leading authors Med Uni Graz
-
Sánchez Murcia Pedro Alejandro
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
-
A conformationally constrained short peptide designed to target a protein-protein interaction hotspot in HIV-1 reverse transcriptase (RT) disrupts p66-p51 interactions and paves the way to the development of novel RT dimerization inhibitors.
Copyright © 2020 American Chemical Society.
- Find related publications in this database (Keywords)
-
Constrained peptides
-
dimerization hotspot
-
dimerization inhibitors
-
HIV reverse transcriptase