Zobrazeno 1 - 3
of 3
pro vyhledávání: '"C. J. Cunliffe"'
Publikováno v:
Journal of Medicinal Chemistry. 35:2652-2658
N-Oxaloglycine (3) is an alpha-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917c4aae631c48946cb15da38dc16978
https://doi.org/10.1021/jm00092a016
https://doi.org/10.1021/jm00092a016
Publikováno v:
The Biochemical journal. 240(2)
An assay for prolyl 4-hydroxylase (EC 1.14.11.2) is described which measures succinic acid produced during the decarboxylation of 2-oxoglutaric acid in the presence of poly(L-Pro-Gly-L-Pro). [1-14C]Succinic acid was separated from its precursor 2-oxo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4d3cd054a89cbcb2a84428f6a842cf8
https://pubmed.ncbi.nlm.nih.gov/3028379
https://pubmed.ncbi.nlm.nih.gov/3028379
Autor:
T J Franklin, C J Cunliffe
Publikováno v:
The Biochemical journal. 239(2)
Prolyl 4-hydroxylase (EC 1.14.11.2) is an essential enzyme in the post-translational modification of collagen. Inhibitors of this enzyme are of potential interest for the treatment of diseases involving excessive deposition of collagen. We have found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::331d539b0d00f87074a4486c21a796b0
https://pubmed.ncbi.nlm.nih.gov/3028370
https://pubmed.ncbi.nlm.nih.gov/3028370