Výsledky vyhledávání - "Sylva L. Schwager"

Probing the Requirements for Dual Angiotensin-Converting Enzyme C-Domain Selective/Neprilysin Inhibition

Autor: Lauren B. Arendse, Gyles E. Cozier, Charles J. Eyermann, Gregory S. Basarab, Sylva L. Schwager, Kelly Chibale, K. Ravi Acharya, Edward D. Sturrock

Publikováno v: Arendse, L B, Cozier, G, Eyermann, C, Basarab, G, Schwager, S L U, Chibale, K, Acharya, R & Sturrock, E D 2022, ' Probing the requirements for dual angiotensin-converting enzyme C-domain selective/neprilysin inhibition ', Journal of Medicinal Chemistry, vol. 65, no. 4, pp. 3371-3387 . https://doi.org/10.1021/acs.jmedchem.1c01924

Selective inhibition of the angiotensin-converting enzyme C-domain (cACE) and neprilysin (NEP), leaving the ACE N-domain (nACE) free to degrade bradykinin and other peptides, has the potential to provide the potent antihypertensive and cardioprotecti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58cd177ad72f4cc61dfcddd02a716f09
https://doi.org/10.1021/acs.jmedchem.1c01924

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Akademický článek

A novel angiotensin I-converting enzyme mutation (S333W) impairs N-domain enzymatic cleavage of the anti-fibrotic peptide, AcSDKP.

Autor: Sergei M Danilov, Michael S Wade, Sylva L Schwager, Ross G Douglas, Andrew B Nesterovitch, Isolda A Popova, Kyle D Hogarth, Nakul Bhardwaj, David E Schwartz, Edward D Sturrock, Joe G N Garcia

Publikováno v: PLoS ONE, Vol 9, Iss 2, p e88001 (2014)

BACKGROUND: Angiotensin I-converting enzyme (ACE) has two functional N- and C-domain active centers that display differences in the metabolism of biologically-active peptides including the hemoregulatory tetrapeptide, Ac-SDKP, hydrolysed preferential

Externí odkaz: https://doaj.org/article/ffe120ace2814c07ab74584edaa8d8c5

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Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design

Autor: Gyles E, Cozier, Lauren B, Arendse, Sylva L, Schwager, Edward D, Sturrock, K Ravi, Acharya

Publikováno v: Journal of medicinal chemistry. 61(22)

Omapatrilat was designed as a vasopeptidase inhibitor with dual activity against the zinc metallopeptidases angiotensin-1 converting enzyme (ACE) and neprilysin (NEP). ACE has two homologous catalytic domains (nACE and cACE), which exhibit different

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f3542969d16928c146c6d977a8773a0d
https://pubmed.ncbi.nlm.nih.gov/30372620

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Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity

Autor: Gyles E, Cozier, Sylva L, Schwager, Rajni K, Sharma, Kelly, Chibale, Edward D, Sturrock, K Ravi, Acharya

Publikováno v: The Febs Journal

Angiotensin‐1‐converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities. Based on kinetic studies it was previously reported that sampatril

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7678c1617aea72f4a4979b9a13be455c
https://pubmed.ncbi.nlm.nih.gov/29476645

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Kinetic and structural characterization of amyloid-β peptide hydrolysis by human angiotensin-1-converting enzyme

Autor: Kate M, Larmuth, Geoffrey, Masuyer, Ross G, Douglas, Sylva L, Schwager, K Ravi, Acharya, Edward D, Sturrock

Publikováno v: The Febs Journal

Angiotensin‐1‐converting enzyme (ACE), a zinc metallopeptidase, consists of two homologous catalytic domains (N and C) with different substrate specificities. Here we report kinetic parameters of five different forms of human ACE with various amy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ae944c88a42a79119e6ac168f7dcd8dc
https://pubmed.ncbi.nlm.nih.gov/26748546

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