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Paolo Grieco

Researcher at University of Naples Federico II

Publications -  220
Citations -  4452

Paolo Grieco is an academic researcher from University of Naples Federico II. The author has contributed to research in topics: Receptor & Melanocortin. The author has an hindex of 35, co-authored 202 publications receiving 3857 citations. Previous affiliations of Paolo Grieco include Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico & University of Arizona.

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D-amino acid scan of γ-melanocyte-stimulating hormone : Importance of Trp8 on human MC3 receptor selectivity

TL;DR: In general, the trend is that D-amino acid substitutions of the aromatic residues 1, 6, 8, and 11 and the basic residue Arg(10), but not Arg(7), result in an increase in MC3R selectivity over the MC4R and MC5R and only agonist activity is observed.
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Urantide: an ultrapotent urotensin II antagonist peptide in the rat aorta.

TL;DR: To the knowledge, urantide is the most potent UT receptor antagonist so far described, and might represent a useful tool for exploring the (patho)physiological role of hU‐II in the mammalian cardiovascular system.
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Preparation of 'side-chain-to-side-chain' cyclic peptides by Allyl and Alloc strategy: potential for library synthesis.

TL;DR: It is demonstrated that properly controlled palladium-mediated deprotection of Allyl/Alloc protecting groups can be used to prepare cyclic peptides on the resin using an automated peptide synthesizer and cyclic glucagon analogue containing 24 amino acid residues.
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A new, potent urotensin II receptor peptide agonist containing a Pen residue at the disulfide bridge.

TL;DR: Conformational analysis of solution NMR data indicated that the putative biologically active conformation of U-II is stabilized by introduction of a Pen residue, which is the most potent U- II receptor agonist reported to date.
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A different molecular mechanism underlying antimicrobial and hemolytic actions of temporins A and L.

TL;DR: A different molecular mechanism underlying the antimicrobial and hemolytic activities of the two peptides temporin A and L is proposed and new analogues of TA and TL are designed and found interesting differences in their efficacy against microbial species and human erythrocytes.