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
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.
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Page/Page column 37; 38
(2018/03/28)
Carbazole-containing sulfonamides and sulfamides: Discovery of cryptochrome modulators as antidiabetic agents
A series of novel carbazole-containing sulfonamides and sulfamides were synthesized. A structure-activity relationship study of these compounds led to the identification of potent cryptochrome modulators. Based on the results of efficacy studies in diet-induced obese (DIO) mice, and the desired pharmacokinetic parameters, compound 41 was selected for further profiling.
Humphries, Paul S.,Bersot, Ross,Kincaid, John,Mabery, Eric,McCluskie, Kerryn,Park, Timothy,Renner, Travis,Riegler, Erin,Steinfeld, Tod,Turtle, Eric D.,Wei, Zhi-Liang,Willis, Erik
p. 757 - 760
(2016/05/24)
Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition
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
Gersch, Malte,Kolb, Roman,Alte, Ferdinand,Groll, Michael,Sieber, Stephan A.
supporting information
p. 1360 - 1366
(2014/02/14)
β-Sultams exhibit discrete binding preferences for diverse bacterial enzymes with nucleophilic residues
β-Sultams are potent electrophiles that modify nucleophilic residues in selected enzyme active sites. We here identify and characterize some of the specific bacterial targets and show a unique inhibition of the azoreductase family.
Kolb, Roman,Bach, Nina C.,Sieber, Stephan A.
supporting information
p. 427 - 429
(2014/01/06)
Structure-reactivity relationships in the inactivation of elastase by β-sultams
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.
Hinchliffe, Paul S.,Wood, J. Matthew,Davis, Andrew M.,Austin, Rupert P.,Beckett, R. Paul,Page, Michael I.
p. 67 - 80
(2007/10/03)
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