34817-61-3Relevant articles and documents
6,7-DIHYDRO-4H-PYRAZOLO[1,5-A]PYRAZINE AND 6,7-DIHYDRO-4H-TRIAZOLO[1,5-A]PYRAZINE COMPOUNDS FOR THE TREATMENT OF INFECTIOUS DISEASES
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Page/Page column 37; 38, (2018/03/28)
The present invention relates to compounds of the formula (I), or pharmaceutically acceptable salts, enantiomer or diastereomer thereof, wherein R1 to R4 and Q are as described above. The compounds may be useful for the treatment or prophylaxis of hepatitis B virus infection.
Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition
Gersch, Malte,Kolb, Roman,Alte, Ferdinand,Groll, Michael,Sieber, Stephan A.
supporting information, p. 1360 - 1366 (2014/02/14)
Over 100 protease inhibitors are currently used in the clinics, and most of them use blockage of the active site for their mode of inhibition. Among the protease drug targets are several enzymes for which the correct multimeric assembly is crucial to thei
Structure-reactivity relationships in the inactivation of elastase by β-sultams
Hinchliffe, Paul S.,Wood, J. Matthew,Davis, Andrew M.,Austin, Rupert P.,Beckett, R. Paul,Page, Michael I.
, p. 67 - 80 (2007/10/03)
N-Acyl-β-sultams are time dependent irreversible active site directed inhibitors of elastase. The rate of inactivation is first order with respect to β-sultam concentration and the second order rate constants show a similar dependence on pH to that for the hydrolysis of a peptide substrate. Inactivation is due to the formation of a stable 1:1 enzyme inhibitor complex as a result of the active site serine being sulfonylated by the β-sultam. Ring opening of the β-sultam occurs by S-N fission in contrast to the C-N fission observed in the acylation of elastase by N-acylsulfonamides. Structure-activity effects are compared between sulfonylation of the enzyme and alkaline hydrolysis. Variation in 4-alkyl and N-substituted β-sultams causes differences in the rates of inactivation by 4 orders of magnitude.
