Glycosaminoglycans Facilitate Procathepsin B Activation through Disruption of Propeptide-Mature Enzyme Interactions*
- Dejan Caglič, J. Pungercar, G. Pejler, V. Turk, B. Turk
- Biology, ChemistryJournal of Biological Chemistry
- 9 November 2007
It is demonstrated that polyanionic polysaccharides, glycosaminoglycans (GAGs), can accelerate the autocatalytic removal of the propeptide and subsequent activation of cathepsin B.
Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation.
- D. Cavallo-Medved, D. Rudy, G. Blum, M. Bogyo, Dejan Caglič, Bonnie F. Sloane
- Biology, ChemistryExperimental Cell Research
- 15 April 2009
Autocatalytic processing of procathepsin B is triggered by proenzyme activity
- J. Pungercar, Dejan Caglič, B. Turk
- Biology, ChemistryThe FEBS Journal
- 1 February 2009
A model for autocatalytic activation of cysteine cathepsins is proposed, involving propeptide dissociation from the active‐site cleft as the first step during zymogen activation.
Expression and activity profiling of selected cysteine cathepsins and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis
- Urška Požgan, Dejan Caglič, B. Rozman, H. Nagase, V. Turk, B. Turk
- Medicine, BiologyBiological chemistry
- 1 May 2010
It is reported that both cysteine cathepsins B and S and matrix metalloproteases-1, -3 and -13 are detected in patient synovial fluid samples with significantly higher levels detected in rheumatoid arthritis patients.
Functional in vivo imaging of cysteine cathepsin activity in murine model of inflammation.
- Dejan Caglič, A. Globisch, K. Wendt
- Biology, ChemistryBioorganic & Medicinal Chemistry
- 1 February 2011
The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
- Dejan Caglič, U. Repnik, B. Turk
- Biology, MedicineBiological chemistry
- 1 February 2013
Its stability at neutral pH and potent proteolytic activity on extracellular matrix components mean that cathepsin S may contribute significantly to cartilage degradation and may thus be considered a potential drug target in joint diseases.
Reexamining hydroxamate inhibitors of botulinum neurotoxin serotype A: extending towards the β-exosite.
- Garry R. Smith, Dejan Caglič, T. Dickerson
- BiologyBioorganic & Medicinal Chemistry Letters
- 1 June 2012
Identification of Clinically Viable Quinolinol Inhibitors of Botulinum Neurotoxin A Light Chain
- Dejan Caglič, Michelle C. Krutein, T. Dickerson
- Chemistry, BiologyJournal of Medicinal Chemistry
- 5 January 2014
The data show the potential of quinolinol compounds as BoNT therapeutics due to their good in vitro potencies and favorable ADME properties, and Evaluation of the most potent compounds in an ADME panel showed that these compounds possess poor solubility at pH 6.8, but display excellent solubilities at low pH, suggesting that oral dosing may be possible.
Selective and sensitive monitoring of caspase-1 activity by a novel bioluminescent activity-based probe.
- Maik Kindermann, H. Roschitzki-Voser, K. Wendt
- BiologyChemistry and Biology
- 24 September 2010
High-Throughput Screening Uncovers Novel Botulinum Neurotoxin Inhibitor Chemotypes.
- K. Bompiani, Dejan Caglič, T. Dickerson
- Biology, ChemistryACS Combinatorial Science
- 20 July 2016
High-throughput screening of 97088 compounds identified numerous small molecules that activate or inhibit metalloprotease activity, and four major classes of inhibitory compounds identified are described, detail their structure-activity relationships, and assess their relative inhibitory potency.
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