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Peptidylprolyl IsomeraseCyclophilinsImmunophilinsTacrolimus Binding ProteinsAmino Acid IsomerasesCyclophilin AHSP90 Heat-Shock ProteinsCyclosporineGlucose-6-Phosphate IsomeraseTacrolimusTriose-Phosphate IsomeraseCarrier ProteinsPeriplasmAmino Acid SequenceMolecular Sequence DataAntigens, CD147CyclosporinsMannose-6-Phosphate IsomeraseIsomerasesAldose-Ketose IsomerasesProtein Disulfide-IsomerasesHeat-Shock ProteinsProtein BindingSteroid IsomerasesDodecenoyl-CoA IsomeraseProtein FoldingStreptomyces antibioticusCarbon-Carbon Double Bond IsomerasesKineticsVirus Physiological PhenomenaCarbohydrate EpimerasesCoronavirusChinaTravelDisease OutbreaksCoronavirus InfectionsSARS VirusSevere Acute Respiratory Syndrome
PPIaseCatalyze the cis-trans isomeriNuclear ribonucleoprotein particle-specificProteinCYPAEnzymeEncodesCypDGenePPIasesInhibitorsPeptideFamilyPeptidylprolineActivity2017ComplexesHumanCrystalDomainFunctionsProteinProlyl isomeraseTrans isomeraseCypAProteinsIsomerizationCyclosporinMitochondrialRegulateCytosolResiduesStructuresMolecularInteractionComplexMemberLiver
PPIase5
  • The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. (nih.gov)
  • PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. (prospecbio.com)
  • Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA ) is a typical member of the Cyclophilin family and is involved in protein folding/translocation, signal transduction, inflammation, immune system regulation, apoptosis and virus replication. (chinagene.cn)
  • Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. (usf.edu)
  • Cyclophilin A (CypA), which has peptidyl-prolyl cis-trans isomerase (PPIase) activity, regulates multiple functions of cells by binding to its extracellular receptor CD147. (bvsalud.org)
Catalyze the cis-trans isomeri1
  • Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. (thermofisher.com)
Nuclear ribonucleoprotein particle-specific1
  • Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. (nih.gov)
Protein5
  • Two protein-protein interaction sites on the spliceosome-associated human cyclophilin CypH. (nih.gov)
  • The cyclophilins are a highly conserved ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. (wikipedia.org)
  • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. (cathdb.info)
  • protein_coding" "AAC73139","fkpB","Escherichia coli","FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Ensembl]. (ntu.edu.sg)
  • protein_coding" "AAC73627","ppiB","Escherichia coli","peptidyl-prolyl cis-trans isomerase B (rotamase B) [Ensembl]. (ntu.edu.sg)
CYPA1
  • Cyclophilins A and B (CypA/B) are the two most abundant Cyps in hepatocytes and are therefore potential targets for pan-viral therapeutics. (bvsalud.org)
Enzyme1
  • Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene. (wikipedia.org)
Encodes3
  • This gene encodes a member of the cyclophilin family. (thermofisher.com)
  • SQN encodes the Arabidopsis homolog of cyclophilin 40 (CyP40). (or.jp)
  • Encodes cyclophilin ROC7. (riken.jp)
CypD1
  • Fragment-based screening by SPR enabled the discovery of chemical diverse fragment hits with millimolar binding affinities to the peptidyl-prolyl isomerase Cyclophilin D (CypD). (nih.gov)
Gene1
PPIases1
  • The orientation of proline residues is regulated by cis/trans peptidyl-prolyl isomerases (PPIases). (usf.edu)
Inhibitors1
  • Current inhibitors of peptidylprolyl isomerases show no selectivity between the tightly conserved cyclophilin paralogs and exhibit significant off-target effects, immunosuppression, and toxicity. (rcsb.org)
Peptide1
  • Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. (nih.gov)
Family3
  • They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. (embl.de)
  • In this regard, the cyclophilins are an important family of proteins that have peptidyl-prolyl isomerase activity and play roles in the replication of a number of positive-sense RNA viruses, including hepatotropic viruses such as hepatitis C virus (HCV). (bvsalud.org)
  • Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). (bvsalud.org)
Peptidylproline1
Activity2
  • Liqian Ren, Wei Liu, Wenbo Li, Wenjun Liu, Lei Sun. Peptidylprolyl cis/trans isomerase activity and molecular evolution of vertebrate Cyclophilin A[J]. Hereditas(Beijing), 2016, 38(8): 736-745. (chinagene.cn)
  • FUNCTIONS IN: triose-phosphate isomerase activity, copper ion bi. (riken.jp)
20171
  • and Blair, Laura J., "Human Cyclophilin 40 Unravels Neurotoxic Amyloids" (2017). (usf.edu)
Complexes1
  • Calcineurin is a common target of cyclophilin-cyclosporine A and Fkbp-Fk506 complexes. (chinagene.cn)
Human3
  • A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. (nih.gov)
  • 6] Colgan J, Yuan HE, Franke EK, Luban J. Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization. (chinagene.cn)
  • Human Cyclophilin 40 Unravels Neurotoxic Amyloids" by Jeremy D. Baker, Lindsey B. Shelton et al. (usf.edu)
Crystal1
  • 5A0E: Crystal structure of cyclophilin D in complex with CsA analogue, JW47. (rcsb.org)
Domain3
  • the E-value for the Pro_isomerase domain shown below is 7.1e-13. (embl.de)
  • This entry represents the core beta-barrel cyclophilin-like domain. (embl.de)
  • Peptidylprolyl isomerase domain and WD repeat-containing. (ntu.edu.sg)
Functions1
  • A cyclophilin functions in pre-mRNA splicing. (nih.gov)
Protein19
  • The cyclophilins are a highly conserved ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. (wikipedia.org)
  • [1] These proteins have peptidyl prolyl isomerase activity, which catalyzes the isomerization of peptide bonds from trans form to cis form at proline residues and facilitates protein folding . (wikidoc.org)
  • Cyclophilin A is a cytosolic and highly abundant protein. (wikidoc.org)
  • The protein belongs to a family of isozymes , including cyclophilins B and C, and natural killer cell cyclophilin-related protein. (wikidoc.org)
  • The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. (thermofisher.com)
  • 8. Binding of the cyclophilin 40 ortholog SQUINT to Hsp90 protein is required for SQUINT function in Arabidopsis. (nih.gov)
  • 12. Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock. (nih.gov)
  • 15. Regulation of the Hsp90-binding immunophilin, cyclophilin 40, is mediated by multiple sites for GA-binding protein (GABP). (nih.gov)
  • The ADP/Ca2+-sensitive labelled component was purified to a single band on SDS-PAGE migrating at approximately 22kDa Identical proteins were purified from sheep heart and rat liver mitochondria The 22kDa protein displayed peptidylprolyl cis trans isomerase (PPIase) activity suggesting it belonged to the cyclophilin (CyP) family of proteins. (ucl.ac.uk)
  • Partial amino acid sequencing of the protein revealed sequence similarity with human cyclophilin D (CyPD). (ucl.ac.uk)
  • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. (cathdb.info)
  • The protein has the alias name cyclophilin D which is also the alias name for the related protein Peptidyl-Prolyl Isomerase F. (nih.gov)
  • Cyclophilin A (CypA) is a peptidyl-prolyl isomerase involved in cardiovascular diseases such as atherosclerosis and aortic aneurysms, and rho-associated protein kinase (ROCK) is involved in the pathogenesis of vascular calcification. (tokushima-u.ac.jp)
  • The immunophilins, FK506 binding protein and cyclophilin, are discretely localized in the brain: relationship to calcineurin. (nih.gov)
  • The immunosuppressant drugs cyclosporin A and FK506 bind to small, predominantly soluble proteins cyclophilin and FK506 binding protein, respectively, to mediate their pharmacological actions. (nih.gov)
  • The immunosuppressant actions of these drugs occur through binding of cyclophilin-cyclosporin A and FK506 binding protein-FK506 complexes to the calcium-calmodulin-dependent protein phosphatase, calcineurin, inhibiting phosphatase activity. (nih.gov)
  • Utilizing immunohistochemistry, in situ hybridization and autoradiography, we have localized protein and messenger RNA for FK506 binding protein, cyclophilin and calcineurin. (nih.gov)
  • We observe a striking co-localization of FK506 binding protein and calcineurin in most brain regions and a close similarity between calcineurin and cyclophilin. (nih.gov)
  • FK506 binding protein and cyclophilin localizations largely correspond to those of calcineurin, although cyclophilin is enriched in some brain areas that lack calcineurin. (nih.gov)
Prolyl isomerase3
  • Fragment-based screening by SPR enabled the discovery of chemical diverse fragment hits with millimolar binding affinities to the peptidyl-prolyl isomerase Cyclophilin D (CypD). (nih.gov)
  • 4. The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. (nih.gov)
  • 7. The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. (nih.gov)
Trans isomerase4
  • Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene. (wikipedia.org)
  • 19. Role of Cysteine Residues in Regulation of Peptidyl-prolyl cis-trans Isomerase Activity of Wheat Cyclophilin TaCYPA-1. (nih.gov)
  • they contain a highly conserved peptidylprolyl cis/trans isomerase domain. (kyobobook.co.kr)
  • A peptidyl-prolyl cis-trans isomerase and member of the cyclophilin family. (nih.gov)
CypA1
  • In this study, we found that RSV infection significantly increased the expression of cyclophilin A (cypA) in clinical patients, mice, and epithelial cells. (nih.gov)
Proteins4
  • Cyclophilins are a family of proteins from vertebrates and other organisms that bind to ciclosporin (cyclosporin A), an immunosuppressant which is usually used to suppress rejection after internal organ transplants . (wikidoc.org)
  • 10. S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. (nih.gov)
  • 11. Identification of cyclophilin-40-interacting proteins reveals potential cellular function of cyclophilin-40. (nih.gov)
  • The dramatic similarities in localization of FK506 binding proteins and cyclophilins with calcineurin suggest related functions. (nih.gov)
Isomerization1
  • 9. The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin. (nih.gov)
Cyclosporin5
  • Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium / calmodulin -dependent phosphatase , calcineurin , the inhibition of which is thought to suppress organ rejection by halting the production of the pro-inflammatory molecules TNF alpha and interleukin 2 . (wikidoc.org)
  • Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening. (wikidoc.org)
  • Cyclophilin inhibitors, such as cyclosporin , are being developed to treat neurodegenerative diseases . (wikidoc.org)
  • The crystal structure of a complex between recombinant human cyclophilin A (Cyp) and cyclosporin A (CsA) has been determined from a novel orthorhombic crystal form that contains only one monomer of complex per asymmetric unit rather than five in the previously determined tetragonal structure. (nih.gov)
  • The molecular replacement solution and X-ray refinement to 2.8 A of a decameric complex of human cyclophilin A with the immunosuppressive drug cyclosporin A. (nih.gov)
Mitochondrial1
  • Cyclophilin D, which is located in the matrix of mitochondria , is only a modulatory, but may or may not be a structural component of the mitochondrial permeability transition pore . (wikidoc.org)
Regulate1
Cytosol1
Residues1
  • 3. A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90. (nih.gov)
Structures1
  • 6. Two structures of cyclophilin 40: folding and fidelity in the TPR domains. (nih.gov)
Molecular2
  • 1. Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties. (nih.gov)
  • A cytoplasmic cyclophilin with molecular chaperoning properties. (nih.gov)
Interaction1
  • 5. Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70. (nih.gov)
Complex1
Member1
Liver1
  • [11] Cyclophilin inhibition may also be a therapy for liver diseases. (wikidoc.org)