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Joël Cotton

Researcher at National and Kapodistrian University of Athens

Publications -  7
Citations -  584

Joël Cotton is an academic researcher from National and Kapodistrian University of Athens. The author has contributed to research in topics: Angiotensin-converting enzyme & ACE inhibitor. The author has an hindex of 7, co-authored 7 publications receiving 544 citations. Previous affiliations of Joël Cotton include French Alternative Energies and Atomic Energy Commission.

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RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites

TL;DR: RXP 407, a highly potent and selective inhibitor of the N-terminal active site of wild ACE, may lead to a new generation of ACE inhibitors able to block in vivo only a subset of the different functions regulated by ACE.
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Roles of the Two Active Sites of Somatic Angiotensin-Converting Enzyme in the Cleavage of Angiotensin I and Bradykinin Insights From Selective Inhibitors

TL;DR: In vivo the conversion of Ang I seems to involve the two active sites of ACE, free of inhibitor, and it might be suggested that the gene duplication of ACE in vertebrates may represent a means for regulating the cleavage of angiotensin I differently from that of BK.
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Functional conservation of the active sites of human and Drosophila angiotensin I-converting enzyme.

TL;DR: The relationship of Ance and Acer to the N- and C-domains of human sACE is investigated by genomic sequence analysis and by using domain-selective inhibitors, including RXP 407, a selective inhibitor of the human N-domain.
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Structural determinants of RXPA380, a potent and highly selective inhibitor of the angiotensin-converting enzyme C-domain.

TL;DR: Structural insights provided by this study should enhance understanding of the factors controlling the selectivity of the two domains of somatic ACE and allow the design of new selective ACE inhibitors.