Title : Synthesis and structure-activity relationships of peptidyl alpha-keto heterocycles as novel inhibitors of prolyl endopeptidase.

Pub. Date : 1994 Oct 14

PMID : 7932578






10 Functional Relationships(s)
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Protein Name
Organism
1 The preparation and in vitro prolyl endopeptidase (PEP) inhibitory activity of a series of alpha-keto heterocyclic compounds is described. alpha-keto heterocyclic compounds prolyl endopeptidase Homo sapiens
2 The preparation and in vitro prolyl endopeptidase (PEP) inhibitory activity of a series of alpha-keto heterocyclic compounds is described. alpha-keto heterocyclic compounds prolyl endopeptidase Homo sapiens
3 Many of the compounds including those substituted with thiazole, benzothiazole, benzoxazole, imidazole, and pyridine groups exhibit IC50 potencies of PEP inhibition at nanomolar levels. Thiazoles prolyl endopeptidase Homo sapiens
4 Many of the compounds including those substituted with thiazole, benzothiazole, benzoxazole, imidazole, and pyridine groups exhibit IC50 potencies of PEP inhibition at nanomolar levels. benzothiazole prolyl endopeptidase Homo sapiens
5 Many of the compounds including those substituted with thiazole, benzothiazole, benzoxazole, imidazole, and pyridine groups exhibit IC50 potencies of PEP inhibition at nanomolar levels. Benzoxazoles prolyl endopeptidase Homo sapiens
6 Many of the compounds including those substituted with thiazole, benzothiazole, benzoxazole, imidazole, and pyridine groups exhibit IC50 potencies of PEP inhibition at nanomolar levels. imidazole prolyl endopeptidase Homo sapiens
7 Many of the compounds including those substituted with thiazole, benzothiazole, benzoxazole, imidazole, and pyridine groups exhibit IC50 potencies of PEP inhibition at nanomolar levels. pyridine prolyl endopeptidase Homo sapiens
8 This heterocyclic nitrogen atom would provide a critical hydrogen-bond interaction with the histidine residue of the catalytic triad in PEP. Nitrogen prolyl endopeptidase Homo sapiens
9 This heterocyclic nitrogen atom would provide a critical hydrogen-bond interaction with the histidine residue of the catalytic triad in PEP. Hydrogen prolyl endopeptidase Homo sapiens
10 This heterocyclic nitrogen atom would provide a critical hydrogen-bond interaction with the histidine residue of the catalytic triad in PEP. Histidine prolyl endopeptidase Homo sapiens