Proteins > Peptidyl-prolyl cis-trans isomerase A
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Peptidyl-prolyl cis-trans isomerase A
A peptidyl-prolyl cis-trans isomerase A that is encoded in the genome of human. [PRO:DNx, UniProtKB:P62937]
Synonyms
PPIase A;
EC 5.2.1.8;
Cyclophilin A;
Cyclosporin A-binding protein;
Rotamase A
Research
Bioassay Publications (25)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (8.00) | 18.2507 |
2000's | 7 (28.00) | 29.6817 |
2010's | 14 (56.00) | 24.3611 |
2020's | 2 (8.00) | 2.80 |
Compounds (10)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Interplay among Conformation, Intramolecular Hydrogen Bonds, and Chameleonicity in the Membrane Permeability and Cyclophilin A Binding of Macrocyclic Peptide Cyclosporin O Derivatives.Journal of medicinal chemistry, , 06-24, Volume: 64, Issue:12, 2021
Discovery of a Potent and Orally Bioavailable Cyclophilin Inhibitor Derived from the Sanglifehrin Macrocycle.Journal of medicinal chemistry, , 11-08, Volume: 61, Issue:21, 2018
Discovery of Potent Cyclophilin Inhibitors Based on the Structural Simplification of Sanglifehrin A.Journal of medicinal chemistry, , 02-09, Volume: 60, Issue:3, 2017
Design and synthesis of peptide-based macrocyclic cyclophilin inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 26, Issue:21, 2016
Structure-Based Discovery of Novel Cyclophilin A Inhibitors for the Treatment of Hepatitis C Virus Infections.Journal of medicinal chemistry, , Dec-24, Volume: 58, Issue:24, 2015
Identification, synthesis and pharmacological evaluation of novel anti-EV71 agents via cyclophilin A inhibition.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 25, Issue:24, 2015
Anti-inflammatory effects of extracellular cyclosporins are exclusively mediated by CD147.Journal of medicinal chemistry, , Sep-26, Volume: 56, Issue:18, 2013
Oligopeptide cyclophilin inhibitors: a reassessment.European journal of medicinal chemistry, , Volume: 46, Issue:11, 2011
Discovery of a potent peptidic cyclophilin A inhibitor Trp-Gly-Pro.European journal of medicinal chemistry, , Volume: 46, Issue:5, 2011
Ranking high affinity ligands of low solubility by NMR spectroscopy.ACS medicinal chemistry letters, , Jun-09, Volume: 2, Issue:6, 2011
SCY-635, a novel nonimmunosuppressive analog of cyclosporine that exhibits potent inhibition of hepatitis C virus RNA replication in vitro.Antimicrobial agents and chemotherapy, , Volume: 54, Issue:2, 2010
Facile synthesis of a fluorescent cyclosporin a analogue to study cyclophilin 40 and cyclophilin 18 ligands.ACS medicinal chemistry letters, , Dec-09, Volume: 1, Issue:9, 2010
Synthesis and biological evaluation of [D-lysine]8cyclosporin A analogs as potential anti-HCV agents.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 20, Issue:22, 2010
Discovering potent small molecule inhibitors of cyclophilin A using de novo drug design approach.Journal of medicinal chemistry, , Sep-10, Volume: 52, Issue:17, 2009
Augmented photoswitching modulates immune signaling.Nature chemical biology, , Volume: 5, Issue:10, 2009
Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent.Antimicrobial agents and chemotherapy, , Volume: 52, Issue:4, 2008
Simultaneous identification of multiple receptors of natural product using an optimized cDNA phage display cloning.Bioorganic & medicinal chemistry letters, , Jul-15, Volume: 18, Issue:14, 2008
Synthesis and neurotrophic activity of nonimmunosuppressant cyclosporin A derivatives.Bioorganic & medicinal chemistry letters, , Sep-06, Volume: 14, Issue:17, 2004
Synthesis of non-immunosuppressive cyclophilin-Binding cyclosporin A derivatives as potential anti-HIV-1 drugs.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 13, Issue:24, 2003
Structure-activity studies of ground- and transition-state analogue inhibitors of cyclophilin.Journal of medicinal chemistry, , Aug-02, Volume: 44, Issue:16, 2001
The role of water molecules in the structure-based design of (5-hydroxynorvaline)-2-cyclosporin: synthesis, biological activity, and crystallographic analysis with cyclophilin A.Journal of medicinal chemistry, , Aug-18, Volume: 38, Issue:17, 1995
Improved binding affinity for cyclophilin A by a cyclosporin derivative singly modified at its effector domain.Journal of medicinal chemistry, , Oct-28, Volume: 37, Issue:22, 1994
Potent nonimmunosuppressive cyclophilin inhibitors with improved pharmaceutical properties and decreased transporter inhibition.Journal of medicinal chemistry, , Oct-23, Volume: 57, Issue:20, 2014
Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent.Antimicrobial agents and chemotherapy, , Volume: 52, Issue:4, 2008
Potent nonimmunosuppressive cyclophilin inhibitors with improved pharmaceutical properties and decreased transporter inhibition.Journal of medicinal chemistry, , Oct-23, Volume: 57, Issue:20, 2014
SCY-635, a novel nonimmunosuppressive analog of cyclosporine that exhibits potent inhibition of hepatitis C virus RNA replication in vitro.Antimicrobial agents and chemotherapy, , Volume: 54, Issue:2, 2010
Synthesis and biological evaluation of [D-lysine]8cyclosporin A analogs as potential anti-HCV agents.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 20, Issue:22, 2010
Synthesis of non-immunosuppressive cyclophilin-Binding cyclosporin A derivatives as potential anti-HIV-1 drugs.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 13, Issue:24, 2003
Potent nonimmunosuppressive cyclophilin inhibitors with improved pharmaceutical properties and decreased transporter inhibition.Journal of medicinal chemistry, , Oct-23, Volume: 57, Issue:20, 2014
Ranking high affinity ligands of low solubility by NMR spectroscopy.ACS medicinal chemistry letters, , Jun-09, Volume: 2, Issue:6, 2011
Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent.Antimicrobial agents and chemotherapy, , Volume: 52, Issue:4, 2008
Enables
This protein enables 8 target(s):
Target | Category | Definition |
RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
peptidyl-prolyl cis-trans isomerase activity | molecular function | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). [EC:5.2.1.8] |
integrin binding | molecular function | Binding to an integrin. [GOC:ceb] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
cyclosporin A binding | molecular function | Binding to cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids. [GOC:mb] |
virion binding | molecular function | Binding to a virion, either by binding to components of the capsid or the viral envelope. [GOC:ai] |
unfolded protein binding | molecular function | Binding to an unfolded protein. [GOC:ai] |
heparan sulfate binding | molecular function | Binding to heparan sulfate. [GO_REF:0000067, GOC:TermGenie, PMID:8567685] |
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] |
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] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
focal adhesion | cellular component | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002] |
membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
vesicle | cellular component | Any small, fluid-filled, spherical organelle enclosed by membrane. [GOC:mah, GOC:pz, GOC:vesicles] |
secretory granule lumen | cellular component | The volume enclosed by the membrane of a secretory granule. [GOC:rph] |
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] |
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 1 target(s):
Target | Category | Definition |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
protein-containing complex | cellular component | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah] |
Involved In
This protein is involved in 28 target(s):
Target | Category | Definition |
protein peptidyl-prolyl isomerization | biological process | The modification of a protein by cis-trans isomerization of a proline residue. [GOC:krc, PMID:16959570] |
negative regulation of protein phosphorylation | biological process | Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein. [GOC:hjd] |
positive regulation of protein phosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein. [GOC:hjd] |
protein folding | biological process | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. [GOC:go_curators, GOC:rb] |
negative regulation of protein kinase activity | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity. [GOC:go_curators] |
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] |
viral release from host cell | biological process | The dissemination of mature viral particles from a host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. [GOC:jl] |
platelet activation | biological process | A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. [http://www.graylab.ac.uk/omd/] |
neuron differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a neuron. [GOC:mah] |
neutrophil chemotaxis | biological process | The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. [GOC:jl, ISBN:0198506732] |
leukocyte chemotaxis | biological process | The movement of a leukocyte in response to an external stimulus. [GOC:add, GOC:jl] |
activation of protein kinase B activity | biological process | Any process that initiates the activity of the inactive enzyme protein kinase B. [GOC:pg] |
negative regulation of stress-activated MAPK cascade | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade. [GOC:mah] |
lipid droplet organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle. [GOC:dph, GOC:jl, GOC:mah, PMID:18093937, PMID:18250201] |
cellular response to oxidative stress | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:mah] |
positive regulation of protein dephosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein. [GOC:bf] |
endothelial cell activation | biological process | The change in morphology and behavior of an endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. [GOC:mgi_curators, ISBN:0781735149, PMID:12851652, PMID:14581484] |
positive regulation of MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. [GOC:go_curators] |
regulation of viral genome replication | biological process | Any process that modulates the frequency, rate or extent of viral genome replication. [GOC:ai] |
positive regulation of viral genome replication | biological process | Any process that activates or increases the frequency, rate or extent of viral genome replication. [GOC:ai] |
positive regulation of protein secretion | biological process | Any process that activates or increases the frequency, rate or extent of the controlled release of a protein from a cell. [GOC:ai] |
positive regulation of NF-kappaB transcription factor activity | biological process | Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. [GOC:dph, GOC:tb, PMID:15087454, PMID:15170030] |
cell adhesion molecule production | biological process | The appearance of a cell adhesion molecule due to biosynthesis or secretion. [GOC:BHF, GOC:rl] |
negative regulation of protein K48-linked ubiquitination | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of K48-linked ubiquitination, a protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. [GOC:BHF, GOC:rph, PMID:23460740] |
platelet aggregation | biological process | The adhesion of one platelet to one or more other platelets via adhesion molecules. [GOC:BHF, GOC:vk] |
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of an oxidative stress-induced intrinsic apoptotic signaling pathway. [GOC:BHF, GOC:mtg_apoptosis, GOC:TermGenie, PMID:11672522] |
negative regulation of viral life cycle | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of viral life cycle. [GO_REF:0000058, GOC:TermGenie, PMID:18005716] |
regulation of apoptotic signaling pathway | biological process | Any process that modulates the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis] |