Epoxysuccinyl dipeptides as selective inhibitors of cathepsin B

BJ Gour-Salin, P Lachance, C Plouffe… - Journal of medicinal …, 1993 - ACS Publications
(R= EtO or i-BuNH) and with the C-terminal amino acid proline either blocked (R'= OBzl) or
free (R'= OH). These compounds were vised to investigate the recently reported selectivity of …

Exploration of the P1 SAR of aldehyde cathepsin K inhibitors

JG Catalano, DN Deaton, ES Furfine… - Bioorganic & medicinal …, 2004 - Elsevier
The synthesis and biological activity of a series of aldehyde inhibitors of cathepsin K are
reported. Exploration of the properties of the S1 subsite with a series of α-amino aldehyde …

Rational design of potent and selective NH-linked aryl/heteroaryl cathepsin K inhibitors

J Robichaud, C Bayly, R Oballa, P Prasit… - Bioorganic & medicinal …, 2004 - Elsevier
Prior reports from our laboratories have identified the nonpeptidic inhibitor 2 as a potent and
selective Cathepsin K (Cat K) inhibitor. Modelling studies suggested that the introduction of …

Discovery of selective and nonpeptidic cathepsin S inhibitors

O Irie, T Ehara, A Iwasaki, F Yokokawa, J Sakaki… - Bioorganic & medicinal …, 2008 - Elsevier
Nonpeptidic, selective, and potent cathepsin S inhibitors were derived from an in-house
pyrrolopyrimidine cathepsin K inhibitor by modification of the P2 and P3 moieties. The …

Natural products as cathepsin inhibitors

A Vidal-Albalat, FV González - Studies in Natural Products Chemistry, 2016 - Elsevier
Cathepsins are proteases found in all animals as well as other organisms. There are
approximately a dozen members of this family, which are distinguished by their structure …

The synthesis, kinetic characterization and application of a novel biotinylated affinity label for cathepsin B

B Walker, BM Cullen, G Kay, IM Halliday… - Biochemical …, 1992 - portlandpress.com
In this study we report on the synthesis, kinetic characterization and application of a novel
biotinylated and active-site-directed inactivator of cathepsin B. Thus the …

Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft

I Štern, N Schaschke, L Moroder, D Turk - Biochemical Journal, 2004 - portlandpress.com
The crystal structure of the inhibitor NS-134 in complex with bovine cathepsin B reveals that
functional groups attached to both sides of the epoxysuccinyl reactive group bind to the part …

Cathepsin B and L inhibitors: a patent review (2010-present)

YY Li, J Fang, GZ Ao - Expert opinion on therapeutic patents, 2017 - Taylor & Francis
Introduction: Cathepsins play an important role in protein degradation and processing.
Aberrant cathepsin B or L is closely associated with many serious diseases such as cancer …

[引用][C] Cathepsin S

H Kirschke - Handbook of proteolytic enzymes, 2013 - Elsevier

The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme

B Cigić, SW Dahl, RH Pain - Biochemistry, 2000 - ACS Publications
The 13.5 kDa N-terminal part of the propeptide remains associated with mature cathepsin C
after proteolytic activation and excision of the activation peptide. This residual pro-part …