Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Gyles E. Cozier"'
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
Autor:
Rachael C. Andrews, Benedict May, Federico J. Hernández, Gyles E. Cozier, Piers A. Townsend, Oliver B. Sutcliffe, Tom S. F. Haines, Tom P. Freeman, Jennifer Scott, Stephen M. Husbands, Ian S. Blagbrough, Richard W. Bowman, Simon E. Lewis, Matthew N. Grayson, Rachel Crespo-Otero, David R. Carbery, Christopher R. Pudney
Publikováno v:
Andrews, R, May, B, Hernández, F J, Townsend, P, Cozier, G, Sutcliffe, O B, Haines, T S F, Freeman, T, Scott, J, Husbands, S, Blagbrough, I, Bowman, R, Lewis, S, Grayson, M, Crespo-Otero, R, Carbery, D & Pudney, C 2023, ' Photochemical Fingerprinting Is a Sensitive Probe for the Detection of Synthetic Cannabinoid Receptor Agonists; Toward Robust Point-of-Care Detection ', Analytical Chemistry, vol. 95, no. 2, pp. 703-713 . https://doi.org/10.1021/acs.analchem.2c02529
With synthetic cannabinoid receptor agonist (SCRA) use still prevalent across Europe and structurally advanced generations emerging, it is imperative that drug detection methods advance in parallel. SCRAs are a chemically diverse and evolving group,
Autor:
Gyles E. Cozier, Emma C. Newby, Sylva L. U. Schwager, R. Elwyn Isaac, Edward D. Sturrock, K. Ravi Acharya
Publikováno v:
The FEBS journalReferences. 289(21)
Human angiotensin I-converting enzyme (ACE) has two isoforms, somatic ACE (sACE) and testis ACE (tACE). The functions of sACE are widespread, with its involvement in blood pressure regulation most extensively studied. sACE is composed of an N-domain
Autor:
null Gyles E. Cozier, null Emma C. Newby, null Sylva L. U. Schwager, null R. Elwyn Isaac, null Edward D. Sturrock, null K. Ravi Acharya
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74439a198717789b50896599edf31b12
https://doi.org/10.1111/febs.16543/v2/response1
https://doi.org/10.1111/febs.16543/v2/response1
Publikováno v:
The Febs Journal
Angiotensin‐1‐converting enzyme (ACE) is a key enzyme in the renin–angiotensin–aldosterone and kinin systems where it cleaves angiotensin I and bradykinin peptides, respectively. However, ACE also participates in numerous other physiological
Publikováno v:
Clinical Science
Clinical Science (London, England : 1979)
Clinical Science (London, England : 1979)
Angiotensin converting enzyme (ACE) is well-known for its role in blood pressure regulation via the renin–angiotensin aldosterone system (RAAS) but also functions in fertility, immunity, haematopoiesis and diseases such as obesity, fibrosis and Alz
Publikováno v:
Journal of Medicinal Chemistry
Neprilysin (NEP) and angiotensin-converting enzyme (ACE) are two key zinc-dependent metallopeptidases in the natriuretic peptide and kinin systems and renin-angiotensin-aldosterone system, respectively. They play an important role in blood pressure r
Publikováno v:
Cozier, G, Lubbe, L, Sturrock, E & Acharya, R 2020, ' ACE-domain selectivity extends beyond direct interacting residues at the active site ', Biochemical Journal, vol. 477, no. 7, pp. 1241-1259 . https://doi.org/10.1042/BCJ20200060
Biochemical Journal
Biochemical Journal
Angiotensin-converting enzyme (ACE) is best known for its formation of the vasopressor angiotensin II that controls blood pressure but is also involved in other physiological functions through the hydrolysis of a variety of peptide substrates. The en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce9c544569721bb601420dc617dfb8f9
https://purehost.bath.ac.uk/ws/files/204588204/Cozier_et_al_Accepted_version_19_Mar_2020.pdf
https://purehost.bath.ac.uk/ws/files/204588204/Cozier_et_al_Accepted_version_19_Mar_2020.pdf
Autor:
Lauren B. Arendse, Lizelle Lubbe, Sylva L. U. Schwager, Afolake T. Arowolo, Emma Ruth Belcher, Gyles E. Cozier, Edward D. Sturrock, K. Ravi Acharya
Publikováno v:
The Biochemical journal. 476(10)
Angiotensin-converting enzyme (ACE) is a zinc metalloprotease best known for its role in blood pressure regulation. ACE consists of two homologous catalytic domains, the N- and C-domain, that display distinct but overlapping catalytic functions in vi
Publikováno v:
Journal of Hypertension. 39:e386