Page last updated: 2024-08-07 13:08:53
Cathepsin S
A cathepsin S that is encoded in the genome of human. [PRO:DNx, UniProtKB:P25774]
Synonyms
EC 3.4.22.27
Research
Bioassay Publications (21)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 11 (52.38) | 29.6817 |
| 2010's | 9 (42.86) | 24.3611 |
| 2020's | 1 (4.76) | 2.80 |
Compounds (18)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| l 006235 | Homo sapiens (human) | EC50 | 0.7900 | 1 | 1 |
| balicatib | Homo sapiens (human) | EC50 | 2.9000 | 1 | 1 |
Drugs with Other Measurements
Azetidines and spiro azetidines as novel P2 units in hepatitis C virus NS3 protease inhibitors.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 23, Issue:23, 2013
MK-7009, a potent and selective inhibitor of hepatitis C virus NS3/4A protease.Antimicrobial agents and chemotherapy, , Volume: 54, Issue:1, 2010
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 18, Issue:3, 2008
Structure activity relationships of 5-, 6-, and 7-methyl-substituted azepan-3-one cathepsin K inhibitors.Journal of medicinal chemistry, , Mar-09, Volume: 49, Issue:5, 2006
Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
Trifluoroethylamines as amide isosteres in inhibitors of cathepsin K.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 15, Issue:21, 2005
Lysosomotropism of basic cathepsin K inhibitors contributes to increased cellular potencies against off-target cathepsins and reduced functional selectivity.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 18, Issue:3, 2008
The identification of potent, selective, and bioavailable cathepsin S inhibitors.Bioorganic & medicinal chemistry letters, , Sep-01, Volume: 17, Issue:17, 2007
Identification of a potent and selective non-basic cathepsin K inhibitor.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 16, Issue:7, 2006
Discovery of selective covalent cathepsin K inhibitors containing novel 4-cyanopyrimidine warhead based on quantum chemical calculations and binding mode analysis.Bioorganic & medicinal chemistry, , Nov-15, Volume: 74, 2022
(1R,2R)-N-(1-cyanocyclopropyl)-2-(6-methoxy-1,3,4,5-tetrahydropyrido[4,3-b]indole-2-carbonyl)cyclohexanecarboxamide (AZD4996): a potent and highly selective cathepsin K inhibitor for the treatment of osteoarthritis.Journal of medicinal chemistry, , Jul-26, Volume: 55, Issue:14, 2012
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 18, Issue:3, 2008
Development of N-(Functionalized benzoyl)-homocycloleucyl-glycinonitriles as Potent Cathepsin K Inhibitors.Journal of medicinal chemistry, , Sep-10, Volume: 58, Issue:17, 2015
3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins.ACS medicinal chemistry letters, , Oct-09, Volume: 5, Issue:10, 2014
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 18, Issue:3, 2008
Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
Lysosomotropism of basic cathepsin K inhibitors contributes to increased cellular potencies against off-target cathepsins and reduced functional selectivity.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
Azetidines and spiro azetidines as novel P2 units in hepatitis C virus NS3 protease inhibitors.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 23, Issue:23, 2013
MK-7009, a potent and selective inhibitor of hepatitis C virus NS3/4A protease.Antimicrobial agents and chemotherapy, , Volume: 54, Issue:1, 2010
Azetidines and spiro azetidines as novel P2 units in hepatitis C virus NS3 protease inhibitors.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 23, Issue:23, 2013
MK-7009, a potent and selective inhibitor of hepatitis C virus NS3/4A protease.Antimicrobial agents and chemotherapy, , Volume: 54, Issue:1, 2010
Enables
This protein enables 7 target(s):
| Target | Category | Definition |
|---|
| fibronectin binding | molecular function | Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. [GOC:hjd] |
| cysteine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE] |
| serine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| collagen binding | molecular function | Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). [GOC:ai, ISBN:0198506732] |
| laminin binding | molecular function | Binding to a laminin, a major glycoprotein constituent of the basement membrane of cells. [GOC:ecd] |
| proteoglycan binding | molecular function | Binding to a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans. [ISBN:0198506732] |
| cysteine-type endopeptidase activator activity involved in apoptotic process | molecular function | Binds to and increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process. [GOC:mah, GOC:mtg_apoptosis] |
Located In
This protein is located in 11 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
| late endosome | cellular component | A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center. [NIF_Subcellular:nlx_subcell_20090702, PMID:11964142, PMID:2557062] |
| endolysosome lumen | cellular component | The volume enclosed by the membrane of an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome. [GOC:pde] |
| lysosomal lumen | cellular component | The volume enclosed within the lysosomal membrane. [GOC:jl, PMID:15213228] |
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
| phagocytic vesicle | cellular component | A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis. [GOC:go_curators, ISBN:0198506732] |
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
| tertiary granule lumen | cellular component | Any membrane-enclosed lumen that is part of a tertiary granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
| ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
Involved In
This protein is involved in 18 target(s):
| Target | Category | Definition |
|---|
| toll-like receptor signaling pathway | biological process | The series of molecular signals initiated by a ligand binding to a toll-like receptor of a target cell. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate an innate immune response. [GO_REF:0000022, GOC:add, ISBN:0781735149, PMID:12467241, PMID:12524386, PMID:12855817, PMID:15585605, PMID:15728447] |
| adaptive immune response | biological process | An immune response mediated by cells expressing specific receptors for antigens produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). [GO_REF:0000022, GOC:add, ISBN:0781735149] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| apoptotic process | biological process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263] |
| response to acidic pH | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution. [GOC:go_curators, GOC:tb, Wikipedia:PH] |
| protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. [GOC:curators, GOC:jl, GOC:jsg] |
| antigen processing and presentation | biological process | The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. [GO_REF:0000022, GOC:add, ISBN:0781735149, PMID:15771591, PMID:15928678] |
| antigen processing and presentation of exogenous peptide antigen via MHC class II | biological process | The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class II protein complex. The peptide antigen is typically, but not always, processed from a whole protein. [GOC:add, ISBN:0781735149, PMID:15771591] |
| extracellular matrix disassembly | biological process | A process that results in the breakdown of the extracellular matrix. [GOC:jid] |
| collagen catabolic process | biological process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. [GOC:mah, ISBN:0815316194] |
| basement membrane disassembly | biological process | The controlled breakdown of the basement membrane in the context of a normal process such as imaginal disc eversion. [GOC:sart, PMID:17301221] |
| antigen processing and presentation of peptide antigen | biological process | The process in which an antigen-presenting cell expresses peptide antigen in association with an MHC protein complex on its cell surface, including proteolysis and transport steps for the peptide antigen both prior to and following assembly with the MHC protein complex. The peptide antigen is typically, but not always, processed from an endogenous or exogenous protein. [GOC:add, ISBN:0781735149, PMID:15771591] |
| proteolysis involved in protein catabolic process | biological process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. [GOC:ai, GOC:dph, GOC:tb] |
| cellular response to thyroid hormone stimulus | biological process | A change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a thyroid hormone stimulus. [GOC:sjw, PMID:9916872] |
| positive regulation of cation channel activity | biological process | Any process that activates or increases the frequency, rate or extent of cation channel activity. [GOC:BHF] |
| positive regulation of peptidase activity | biological process | Any process that increases the frequency, rate or extent of peptidase activity, the hydrolysis of peptide bonds within proteins. [GOC:dph, GOC:tb] |
| immune response | biological process | Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. [GO_REF:0000022, GOC:add] |
| positive regulation of apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis] |