Novel Mechanism of Cathepsin B Inhibition by Antibiotic Nitroxoline and Related Compounds.
Summary of "Novel Mechanism of Cathepsin B Inhibition by Antibiotic Nitroxoline and Related Compounds."
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Affiliation
Faculty of Pharmacy, University of Ljubljana, Aškerčeva 7, 1000 Ljubljana (Slovenia), Fax: (+386) 1-42-58-031.
Journal Details
This article was published in the following journal.
Name: ChemMedChem
ISSN: 1860-7187
Pages:
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/21598397
- DOI: http://dx.doi.org/10.1002/cmdc.201100098
Medical and Biotech [MESH] Definitions
Protein Synthesis Inhibitors
Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.
Cathepsin W
A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.
Cathepsin E
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
Cathepsin F
A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
Cathepsin B
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
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