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Journal Article
Molecular Microbiology, ISSN 0950-382X, 10/2015, Volume 98, Issue 1, p. 142
  Caspases are a family of cysteine-dependent proteases known to be involved in the process of programmed cell death in metazoans. Recently, cyanobacteria were... 
Enzymes | E coli | Bacterial proteins | Amino acids | Cells | Apoptosis
Journal Article
Molecular Microbiology, ISSN 0950-382X, 10/2015, Volume 98, Issue 1, pp. 142 - 150
Journal Article
Molecular Microbiology, ISSN 0950-382X, 10/2015, Volume 98, Issue 1, pp. 142 - 150
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 10/2019, Volume 675, p. 108121
Human dipeptidyl-peptidase I (DPPI) is a tetrameric enzyme from the family of papain-like cysteine peptidases. It is ubiquitously expressed and plays important... 
Chlorogenic acid | Cathepsin C | Allosteric regulation | Phthalanilic acid | Caffeic acid
Journal Article
FEBS Journal, ISSN 1742-464X, 11/2015, Volume 282, Issue 22, pp. 4328 - 4340
Journal Article
BioMolecular Concepts, ISSN 1868-5021, 06/2013, Volume 4, Issue 3, pp. 287 - 308
Papain-like cysteine peptidases are a diverse family of peptidases found in most known organisms. In eukaryotes, they are divided into multiple evolutionary... 
cysteine cathepsins | lysosomal enzymes | proteolysis | Cysteine cathepsins | Proteolysis | Lysosomal enzymes
Journal Article
Biochemical Journal, ISSN 0264-6021, 07/2010, Volume 429, Issue 2, pp. 379 - 389
Journal Article
PloS one, 2014, Volume 9, Issue 9, p. e106642
Targeting allosteric sites is gaining increasing recognition as a strategy for modulating the activity of enzymes, especially in drug design. Here we... 
Cathepsin K - metabolism | Osteoporosis - enzymology | Allosteric Regulation | Cathepsin K - chemistry | Humans | Enzyme Stability
Journal Article
Acta Chimica Slovenica, ISSN 1318-0207, 2017, Volume 64, Issue 4, pp. 782 - 789
Eight novel 5-(N-Boc-N-benzyl-2-aminoethyl)-7-oxo-4,7-dihydropyrazolo[1,5-a] pyrimidin-3-carboxamides were prepared in three steps from methyl... 
Pyrazolo[1,5-a]pyrimidines | Cathepsin inhibition | Synthesis | Cyclization | synthesis | Pyrazolo[1,5-a] pyrimidines | POTENT | DRUG DISCOVERY | BIOLOGICAL EVALUATION | CHEMISTRY | cathepsin inhibition | IDENTIFICATION | cyclization | CHEMISTRY, MULTIDISCIPLINARY | pyrazolo[1,5-a]pyrimidines
Journal Article
Journal Article
Protein Expression and Purification, ISSN 1046-5928, 05/2019, Volume 157, pp. 21 - 27
Cathepsin C is a tetrameric lysosomal protease that acts as a dipeptidyl-peptidase due to the presence of the exclusion domain that is unique among papain-like... 
Elastolysis | Oligomeric proteins | Gelatinolysis | Proteolysis | Exclusion domain | CELLS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CYSTEINE CATHEPSINS | IDENTIFICATION | INHIBITION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PAPILLON-LEFEVRE-SYNDROME | MUTATIONS | Ethylenediaminetetraacetic acid | Hydrolysis | Cysteine | Elastin | Cathepsins | Papain | Cystine
Journal Article
Biomolecular concepts, 06/2013, Volume 4, Issue 3, p. 287
Papain-like cysteine peptidases are a diverse family of peptidases found in most known organisms. In eukaryotes, they are divided into multiple evolutionary... 
Catalytic Domain | Animals | Protein Structure, Secondary | Peptide Hydrolases - physiology | Humans | Peptide Hydrolases - classification | Models, Molecular | Phylogeny | Evolution, Molecular | Papain - chemistry
Journal Article