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Adel Amer

Researcher at Alexandria University

Publications -  70
Citations -  689

Adel Amer is an academic researcher from Alexandria University. The author has contributed to research in topics: Bicyclic molecule & Quinoxaline. The author has an hindex of 14, co-authored 69 publications receiving 608 citations. Previous affiliations of Adel Amer include Taibah University & United Arab Emirates University.

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Synthesis of 3-benzyl-2-substituted quinoxalines as novel monoamine oxidase A inhibitors.

TL;DR: A new series of 3-benzyl-2-substituted quinoxalines synthesized by means of microwave enhancement of nucleophilic substitution reaction involving the corresponding 2-chloroquinoxaline analogs and substituted amines or hydrazine showed more selective inhibitory activity toward MAO-A thanMAO-B.
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Exploring new selective 3-benzylquinoxaline-based MAO-A inhibitors: design, synthesis, biological evaluation and docking studies.

TL;DR: Most of the compounds showed a selective MAO-A inhibitory activity in the nanomolar or low micromolar range and were synthesized and evaluated in vitro as inhibitors of the two monoamine oxidase isoforms.
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Synthesis of new series of quinoxaline based MAO-inhibitors and docking studies

TL;DR: The inhibition profile was found to be competitive for compounds 3k, 3m, 5f and 5n with MAO-A selectivity and interactions with many residues previously reported to have an effect on the inhibition of the enzyme were revealed.
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Synthesis and evaluation of quinazoline amino acid derivatives as mono amine oxidase (MAO) inhibitors.

TL;DR: The microwave irradiation afforded the product in less reaction time, higher yield and purity, and selective MAO-A inhibition activity superior to that of the standard clorgyline was determined.
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Synthesis and structure elucidation of novel fused 1,2,4-triazine derivatives as potent inhibitors targeting CYP1A1 activity.

TL;DR: Analysis of triazolotriazine derivatives docking showed that these compounds bind only at the interface of substrate recognition site 2 (SRS2) and (S RS6) at the outer surface of the protein.