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Andrea J. Robinson

Researcher at Monash University, Clayton campus

Publications -  113
Citations -  1818

Andrea J. Robinson is an academic researcher from Monash University, Clayton campus. The author has contributed to research in topics: Catalysis & Metathesis. The author has an hindex of 24, co-authored 109 publications receiving 1633 citations. Previous affiliations of Andrea J. Robinson include Wilmington University & Monash University.

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High conversion and productive catalyst turnovers in cross-metathesis reactions of natural oils with 2-butene

TL;DR: In this article, high conversion and selectivity can be obtained for the cross-metathesis of 2-butene with triglycerides and unsaturated fatty acid esters derived from natural oils.
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Microwave-assisted RCM for the synthesis of carbocyclic peptides.

TL;DR: Microwave irradiation dramatically improves the efficiency of ring closing metathesis (RCM) reactions of resin‐attached peptides and the technology is illustrated by the highly selective synthesis of dicarba analogues of α‐conotoxin IMI.
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Solid phase synthesis and structural analysis of novel A-chain dicarba analogs of human relaxin-3 (INSL7) that exhibit full biological activity

TL;DR: The replacement of the A-chain intramolecular disulfide bond of human relaxin-3 (H3 relaxin, INSL7), an insulin-like peptide that has potential applications in the treatment of stress and obesity, with the physiologically stable dicarba bond is described.
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Cross-metathesis of unsaturated natural oils with 2-butene. High conversion and productive catalyst turnovers.

TL;DR: The cross-metathesis of synthetic and natural triglycerides containing unsaturated fatty acids with 2-butene can be achieved with high conversion and excellent productive turnovers.
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Dicarba α-conotoxin Vc1.1 analogues with differential selectivity for nicotinic acetylcholine and GABAB receptors.

TL;DR: The regioselective synthesis of dicarba analogues of α-conotoxin Vc1.1 will enable the elucidation of the biological target responsible for the peptide's potent analgesic activity and can be used to selectively tune the cyclic peptides' innate biological activity for one receptor over another.