H
Hajar Sirous
Researcher at Isfahan University of Medical Sciences
Publications - 16
Citations - 159
Hajar Sirous is an academic researcher from Isfahan University of Medical Sciences. The author has contributed to research in topics: Medicine & Chemistry. The author has an hindex of 6, co-authored 10 publications receiving 88 citations.
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Journal ArticleDOI
An integrated in silico screening strategy for identifying promising disruptors of p53-MDM2 interaction.
TL;DR: Three top-ranked hit molecules were found to have acceptable pharmacokinetics properties along with superior in silico inhibitory ability towards the p53-MDM2 interaction compared to known inhibitors.
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Identification of Novel 3-Hydroxy-pyran-4-One Derivatives as Potent HIV-1 Integrase Inhibitors Using in silico Structure-Based Combinatorial Library Design Approach.
Hajar Sirous,Giulia Chemi,Sandra Gemma,Stefania Butini,Zeger Debyser,Frauke Christ,Lotfollah Saghaie,Simone Brogi,Afshin Fassihi,Giuseppe Campiani,Margherita Brindisi +10 more
TL;DR: HPCAR-28 represents the most promising compound as potential anti-HIV agent, showing inhibitory activity against HIV IN in the low nanomolar range, comparable to that found for Raltegravir, and relevant potency in inhibiting HIV- 1 replication and HIV-1 IN strand transfer activity.
Journal ArticleDOI
Synthesis, Molecular Modelling and Biological Studies of 3-hydroxypyrane- 4-one and 3-hydroxy-pyridine-4-one Derivatives as HIV-1 Integrase Inhibitors.
Hajar Sirous,Afshin Fassihi,Simone Brogi,Giuseppe Campiani,Frauke Christ,Zeger Debyser,Sandra Gemma,Stefania Butini,Giulia Chemi,Alessandro Grillo,Rezvan Zabihollahi,Mohammad R. Aghasadeghi,Lotfollah Saghaie,Hamid Reza Memarian +13 more
TL;DR: Halogenated derivatives, HPb and HPd, displayed the most promising anti-HIV profile, paving the way to the optimization of the presented scaffolds for developing new effective antiviral agents.
Journal ArticleDOI
In vitro and in silico studies of the inhibitory effects of some novel kojic acid derivatives on tyrosinase enzyme.
TL;DR: One compound appeared to have the highest inhibition on tyrosinase activity, which has an NO2 group which binds to both of Cu2+ ions located inside the active site of the enzyme.
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Amyloid β fibril disruption by oleuropein aglycone: long-time molecular dynamics simulation to gain insight into the mechanism of action of this polyphenol from extra virgin olive oil
TL;DR: A comprehensive computational investigation of the mechanism of action of OA as an Aβ fibril disruptor at the molecular level showed that OA is able to move in depth within the Aβfibrils targeting a key motif in Aβ peptide, known to be relevant for stabilizing the assembled fibrils.