Page last updated: 2024-08-07 15:44:11
Procathepsin L
A procathepsin L that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07711]
Synonyms
EC 3.4.22.15;
Cathepsin L1;
Major excreted protein;
MEP
Research
Bioassay Publications (38)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (2.63) | 18.2507 |
| 2000's | 14 (36.84) | 29.6817 |
| 2010's | 17 (44.74) | 24.3611 |
| 2020's | 6 (15.79) | 2.80 |
Compounds (99)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| camostat | Homo sapiens (human) | IC50 | 0.0180 | 1 | 1 |
| camostat | Homo sapiens (human) | Ki | 3.4394 | 1 | 6 |
| carmofur | Homo sapiens (human) | IC50 | 1.8200 | 1 | 1 |
| celecoxib | Homo sapiens (human) | IC50 | 0.5600 | 1 | 1 |
| chloroquine | Homo sapiens (human) | IC50 | 5.4700 | 1 | 1 |
| chlorpromazine | Homo sapiens (human) | IC50 | 11.2400 | 1 | 2 |
| disulfiram | Homo sapiens (human) | IC50 | 9.3500 | 1 | 1 |
| ebselen | Homo sapiens (human) | IC50 | 0.6700 | 1 | 1 |
| emodin | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| fluphenazine | Homo sapiens (human) | IC50 | 11.8000 | 1 | 2 |
| indomethacin | Homo sapiens (human) | IC50 | 11.8000 | 1 | 1 |
| niclosamide | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| nimesulide | Homo sapiens (human) | IC50 | 1.9200 | 1 | 1 |
| promethazine | Homo sapiens (human) | IC50 | 13.6450 | 1 | 2 |
| ethyl acetate | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| allicin | Homo sapiens (human) | Ki | 9.3000 | 1 | 1 |
| aloxistatin | Homo sapiens (human) | IC50 | 2.4100 | 1 | 1 |
| leupeptin | Homo sapiens (human) | IC50 | 0.0046 | 2 | 2 |
| calpeptin | Homo sapiens (human) | IC50 | 0.0720 | 1 | 1 |
| Pyrrolidine-1-carbonitrile | Homo sapiens (human) | IC50 | 2.7924 | 2 | 2 |
| e 64 | Homo sapiens (human) | IC50 | 0.0279 | 5 | 5 |
| e 64 | Homo sapiens (human) | Ki | 0.0300 | 1 | 1 |
| benzyloxycarbonylphenylalanylphenylalanine diazomethyl ketone | Homo sapiens (human) | IC50 | 0.0500 | 1 | 1 |
| 2-phenyl-4-oxohydroquinoline | Homo sapiens (human) | IC50 | 2.6000 | 1 | 1 |
| tanshinone ii a | Homo sapiens (human) | IC50 | 0.8000 | 1 | 1 |
| 1-methylpropyl-2-imidazolyl disulfide | Homo sapiens (human) | IC50 | 21.0000 | 1 | 2 |
| 1-(2-Naphthylmethyl)-2,3-dioxo-indoline-5-carboxamide | Homo sapiens (human) | IC50 | 0.3700 | 1 | 1 |
| hirsutanone | Homo sapiens (human) | IC50 | 4.1000 | 1 | 1 |
| S-[5-(trifluoromethyl)-4H-1,2,4-triazol-3-yl] 5-(phenylethynyl)furan-2-carbothioate | Homo sapiens (human) | IC50 | 3.0000 | 1 | 1 |
| telaprevir | Homo sapiens (human) | IC50 | 3.5000 | 1 | 1 |
| N-(4-Butan-2-ylphenyl)-N-[2-(cyclopentylamino)-2-oxo-1-pyridin-3-ylethyl]furan-2-carboxamide | Homo sapiens (human) | IC50 | 18.1000 | 1 | 2 |
| amentoflavone | Homo sapiens (human) | IC50 | 8.3000 | 1 | 1 |
| savinin | Homo sapiens (human) | IC50 | 25.0000 | 1 | 1 |
| pepstatin | Homo sapiens (human) | IC50 | 0.8000 | 1 | 1 |
| broussochalcone a | Homo sapiens (human) | IC50 | 25.6500 | 1 | 2 |
| rupintrivir | Homo sapiens (human) | IC50 | 410.0000 | 1 | 2 |
| rupintrivir | Homo sapiens (human) | Ki | 10.0000 | 1 | 2 |
| relacatib | Homo sapiens (human) | IC50 | 0.0020 | 1 | 1 |
| relacatib | Homo sapiens (human) | Ki | 0.0033 | 2 | 7 |
| 5-Chloro-3-pyridinyl 2-furoate | Homo sapiens (human) | IC50 | 0.0600 | 1 | 1 |
| ca 074 | Homo sapiens (human) | IC50 | 67.6967 | 3 | 3 |
| k11002 | Homo sapiens (human) | Ki | 1.0000 | 1 | 1 |
| l 006235 | Homo sapiens (human) | IC50 | 3.5886 | 4 | 5 |
| l 006235 | Homo sapiens (human) | Ki | 6.0000 | 1 | 1 |
| l-873724 | Homo sapiens (human) | IC50 | 1.1228 | 7 | 13 |
| odanacatib | Homo sapiens (human) | IC50 | 3.9190 | 2 | 2 |
| odanacatib | Homo sapiens (human) | Ki | 1.2589 | 1 | 1 |
| balicatib | Homo sapiens (human) | IC50 | 1.1804 | 4 | 5 |
| balicatib | Homo sapiens (human) | Ki | 7.2543 | 3 | 3 |
| s-benzyl phenylmethanethiosulfinate | Homo sapiens (human) | Ki | 31.7000 | 1 | 1 |
| n-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide | Homo sapiens (human) | IC50 | 0.7600 | 1 | 1 |
| calpain inhibitor iii | Homo sapiens (human) | IC50 | 0.6366 | 2 | 2 |
| np 031112 | Homo sapiens (human) | IC50 | 1.5500 | 1 | 1 |
| PF-00835231 | Homo sapiens (human) | IC50 | 0.3992 | 2 | 4 |
| Benzotriazol-1-yl 1H-indole-5-carboxylate | Homo sapiens (human) | Ki | 0.0075 | 1 | 1 |
| 5-Chloropyridin-3-yl 5-(4-chlorophenyl)furan-2-carboxylate | Homo sapiens (human) | IC50 | 0.0630 | 1 | 1 |
| (5-Chloropyridin-3-yl) 1H-indole-5-carboxylate | Homo sapiens (human) | IC50 | 0.3100 | 1 | 1 |
| 5-Chloropyridin-3-yl 1H-indole-2-carboxylate | Homo sapiens (human) | IC50 | 0.0650 | 1 | 1 |
| sid 26681509 | Homo sapiens (human) | IC50 | 0.0560 | 2 | 2 |
| mk-7009 | Homo sapiens (human) | IC50 | 10,000.0000 | 1 | 1 |
| GRL-0617 | Homo sapiens (human) | IC50 | 0.6000 | 1 | 1 |
| (5-Chloropyridin-3-yl) 1H-indole-4-carboxylate | Homo sapiens (human) | IC50 | 0.0300 | 1 | 1 |
| gallinamide a | Homo sapiens (human) | IC50 | 0.0154 | 4 | 4 |
| gallinamide a | Homo sapiens (human) | Ki | 0.0080 | 1 | 1 |
| 6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.1175 | 1 | 1 |
| 6-(3,5-difluoroanilino)-9-(2,2-difluoroethyl)-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 7.9433 | 1 | 1 |
| 9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.5623 | 1 | 1 |
| KOM70144 | Homo sapiens (human) | IC50 | 0.5600 | 1 | 1 |
| N-[(1R)-2-(tert-butylamino)-2-oxo-1-(3-pyridinyl)ethyl]-N-(4-tert-butylphenyl)-2-furancarboxamide | Homo sapiens (human) | IC50 | 1.5000 | 1 | 1 |
| N-[(2S)-3-cyclohexyl-1-oxo-1-({(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)propan-2-yl]-1H-indole-2-carboxamide | Homo sapiens (human) | IC50 | 0.0194 | 2 | 3 |
| 3-fluoro-Nalpha-(1H-indol-2-ylcarbonyl)-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide | Homo sapiens (human) | IC50 | 0.0400 | 1 | 1 |
Drugs with Activation Measurements
Discovery of novel cyanamide-based inhibitors of cathepsin C.ACS medicinal chemistry letters, , Feb-10, Volume: 2, Issue:2, 2011
Novel, nonpeptidic cyanamides as potent and reversible inhibitors of human cathepsins K and L.Journal of medicinal chemistry, , Jan-04, Volume: 44, Issue:1, 2001
[no title available]RSC medicinal chemistry, , Feb-23, Volume: 13, Issue:2, 2022
Development of Novel Peptide-Based Michael Acceptors Targeting Rhodesain and Falcipain-2 for the Treatment of Neglected Tropical Diseases (NTDs).Journal of medicinal chemistry, , 08-24, Volume: 60, Issue:16, 2017
Structures and bioactivities of dihydrochalcones from Metrodorea stipularis.Journal of natural products, , Nov-26, Volume: 77, Issue:11, 2014
Novel 2H-isoquinolin-3-ones as antiplasmodial falcipain-2 inhibitors.Bioorganic & medicinal chemistry, , Sep-15, Volume: 17, Issue:18, 2009
Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing.The Journal of biological chemistry, , Jul-20, Volume: 282, Issue:29, 2007
Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption.Journal of medicinal chemistry, , Oct-22, Volume: 41, Issue:22, 1998
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
Neuroprotective effect of synthetic chalcone derivatives as competitive dual inhibitors against μ-calpain and cathepsin B through the downregulation of tau phosphorylation and insoluble Aβ peptide formation.European journal of medicinal chemistry, , Oct-04, Volume: 121, 2016
Synthesis and investigation of dihydroxychalcones as calpain and cathepsin inhibitors.Bioorganic chemistry, , Volume: 51, 2013
Identification of 3-acetyl-2-aminoquinolin-4-one as a novel, nonpeptidic scaffold for specific calpain inhibitory activity.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 2009
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
Trifluoroethylamines as amide isosteres in inhibitors of cathepsin K.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 15, Issue:21, 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
Synthesis and structure-activity relationship of nitrile-based cruzain inhibitors incorporating a trifluoroethylamine-based P2 amide replacement.Bioorganic & medicinal chemistry, , 11-15, Volume: 27, Issue:22, 2019
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
Neuroprotective effect of synthetic chalcone derivatives as competitive dual inhibitors against μ-calpain and cathepsin B through the downregulation of tau phosphorylation and insoluble Aβ peptide formation.European journal of medicinal chemistry, , Oct-04, Volume: 121, 2016
Identification of 3-acetyl-2-aminoquinolin-4-one as a novel, nonpeptidic scaffold for specific calpain inhibitory activity.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 2009
Discovery and Crystallographic Studies of Trisubstituted Piperazine Derivatives as Non-Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity and Low Toxicity.Journal of medicinal chemistry, , 10-13, Volume: 65, Issue:19, 2022
Discovery of Di- and Trihaloacetamides as Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity.Journal of the American Chemical Society, , 12-15, Volume: 143, Issue:49, 2021
Identification and synthesis of a unique thiocarbazate cathepsin L inhibitor.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 18, Issue:1, 2008
Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype.Bioorganic & medicinal chemistry letters, , Jun-15, Volume: 18, Issue:12, 2008
Potent Anti-SARS-CoV-2 Activity by the Natural Product Gallinamide A and Analogues via Inhibition of Cathepsin L.Journal of medicinal chemistry, , 02-24, Volume: 65, Issue:4, 2022
[no title available]Journal of medicinal chemistry, , 10-24, Volume: 62, Issue:20, 2019
The marine cyanobacterial metabolite gallinamide A is a potent and selective inhibitor of human cathepsin L.Journal of natural products, , Jan-24, Volume: 77, Issue:1, 2014
Enables
This protein enables 9 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] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| 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] |
| cysteine-type peptidase activity | molecular function | Catalysis of the hydrolysis of 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] |
| histone binding | molecular function | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. [GOC:jl, PMID:16209651, PMID:30212449, PMID:9305837] |
| proteoglycan binding | molecular function | Binding to a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans. [ISBN:0198506732] |
| serpin family protein binding | molecular function | Binding to a member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors. [GOC:mr, InterPro:IPR000215, PMID:16737556] |
| 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 15 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] |
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
| 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] |
| multivesicular body | cellular component | A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm. [PMID:11566881, PMID:16533950] |
| Golgi apparatus | cellular component | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| apical plasma membrane | cellular component | The region of the plasma membrane located at the apical end of the cell. [GOC:curators] |
| 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] |
| chromaffin granule | cellular component | Specialized secretory vesicle found in the cells of adrenal glands and various other organs, which is concerned with the synthesis, storage, metabolism, and secretion of epinephrine and norepinephrine. [GOC:jl, PMID:19158310, PMID:1961743] |
| 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] |
| 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] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| endocytic vesicle lumen | cellular component | The volume enclosed by the membrane of an endocytic vesicle. [GOC:pde] |
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 21 target(s):
| Target | Category | Definition |
|---|
| 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] |
| protein autoprocessing | biological process | Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein. [GOC:ai, PMID:9335337] |
| fusion of virus membrane with host plasma membrane | biological process | Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. [GOC:bf, GOC:jl] |
| receptor-mediated endocytosis of virus by host cell | biological process | Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. [GOC:bf, GOC:jl, ISBN:0781702534] |
| 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] |
| 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] |
| zymogen activation | biological process | The proteolytic processing of an inactive enzyme to an active form. [GOC:hjd] |
| enkephalin processing | biological process | The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide. [GOC:BHF, GOC:mah, GOC:rl, PMID:8262946] |
| fusion of virus membrane with host endosome membrane | biological process | Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. [GOC:bf, UniProtKB-KW:KW-1170, VZ:992] |
| CD4-positive, alpha-beta T cell lineage commitment | biological process | The process in which an immature T cell becomes committed to becoming a CD4-positive, alpha-beta T cell. [ISBN:0781735149] |
| symbiont entry into host cell | biological process | The process by which a symbiont breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the symbiont or its genome is released into the host cell. [GOC:jl] |
| 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] |
| elastin catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of elastin. Elastin is a glycoprotein which is randomly coiled and crosslinked to form elastic fibers that are found in connective tissue. [GOC:BHF, GOC:dph, GOC:tb] |
| macrophage apoptotic process | biological process | Any apoptotic process in a macrophage, a mononuclear phagocyte present in a variety of tissues. [CL:0000235, GOC:BHF, GOC:mah, GOC:mtg_apoptosis] |
| 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 apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| 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] |