PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33999413-10 2022 In U937 cells, the extra-supplied CyPA increased MMP-9 mRNA and enzyme activity, whereas the CyPA inhibitor, cyclosporine A, suppressed the LPS- and co-culture-enhanced MMP-9. Cyclosporine 109-123 peptidylprolyl isomerase A Homo sapiens 93-97 33361281-3 2021 CyPA mediates immunosuppressive action of the cyclic undecapeptide cyclosporine A and is also involved in multiple cellular processes such as protein folding, intracellular trafficking, signal transduction, and transcriptional regulation. Cyclosporine 67-81 peptidylprolyl isomerase A Homo sapiens 0-4 33492451-2 2021 Besides acting as an intracellular receptor for cyclosporine A, CypA plays a vital role in microorganismal infections, cardiovascular diseases, liver diseases, kidney diseases, neurodegeneration, cancer, rheumatoid arthritis, periodontitis, sepsis, asthma, and aging. Cyclosporine 48-62 peptidylprolyl isomerase A Homo sapiens 64-68 33339864-6 2020 From 32 datasets, the top ranked gene was PPIA, encoding cyclophilin A, a druggable target using cyclosporine. Cyclosporine 97-109 peptidylprolyl isomerase A Homo sapiens 42-46 32907979-7 2020 Cyclosporin A treatment, mutating the CYPA-binding loop in the capsid or CYPA-knockout eliminated SIVcpzPts" resistance to PF74 in HeLa cells. Cyclosporine 0-13 peptidylprolyl isomerase A Homo sapiens 38-42 33121398-2 2021 CypA, the intracellular target protein for the immunosuppressant cyclosporine A (CsA), plays important cellular roles through peptidyl-prolyl cis-trans isomerase (PPIase). Cyclosporine 65-79 peptidylprolyl isomerase A Homo sapiens 0-4 33121398-2 2021 CypA, the intracellular target protein for the immunosuppressant cyclosporine A (CsA), plays important cellular roles through peptidyl-prolyl cis-trans isomerase (PPIase). Cyclosporine 81-84 peptidylprolyl isomerase A Homo sapiens 0-4 31634494-8 2020 The interruption of interaction between CypA and N protein by CsA and its derivatives suggest a mechanism how CypA inhibitors suppress viral replication. Cyclosporine 62-65 peptidylprolyl isomerase A Homo sapiens 40-44 32321312-3 2020 In the co-culture, we found that CsA inhibited the expression of cyclophilin A (CyPA), CD147 and the activities of MMPs, which were all induced by P.g-LPS. Cyclosporine 33-36 peptidylprolyl isomerase A Homo sapiens 65-78 32321312-3 2020 In the co-culture, we found that CsA inhibited the expression of cyclophilin A (CyPA), CD147 and the activities of MMPs, which were all induced by P.g-LPS. Cyclosporine 33-36 peptidylprolyl isomerase A Homo sapiens 80-84 32321312-4 2020 We also found that P.g-LPS and recombinant human CyPA increased activation of ERK1/2 and IkappaB (an NF-kappaB inhibitory protein), but CsA and the anti-CD147 antibody significantly inhibited these effects. Cyclosporine 136-139 peptidylprolyl isomerase A Homo sapiens 49-53 32321312-5 2020 Taken together, CsA in the presence of P.g-LPS might suppress MMP activities by blocking the CyPA/CD147 interaction that results in the inhibition of ERK1/2 and NF-kappaB signaling by interfering with the phosphorylation of ERK1/2 and IkappaB. Cyclosporine 16-19 peptidylprolyl isomerase A Homo sapiens 93-97 32434054-5 2020 Cyclophilin A (CyPA), the most important immunophilin and endogenous ligand of cyclosporine A (CsA), is strongly involved in several detrimental cardiovascular processes, such as calcification. Cyclosporine 79-93 peptidylprolyl isomerase A Homo sapiens 0-13 32434054-5 2020 Cyclophilin A (CyPA), the most important immunophilin and endogenous ligand of cyclosporine A (CsA), is strongly involved in several detrimental cardiovascular processes, such as calcification. Cyclosporine 79-93 peptidylprolyl isomerase A Homo sapiens 15-19 32434054-5 2020 Cyclophilin A (CyPA), the most important immunophilin and endogenous ligand of cyclosporine A (CsA), is strongly involved in several detrimental cardiovascular processes, such as calcification. Cyclosporine 95-98 peptidylprolyl isomerase A Homo sapiens 0-13 32434054-5 2020 Cyclophilin A (CyPA), the most important immunophilin and endogenous ligand of cyclosporine A (CsA), is strongly involved in several detrimental cardiovascular processes, such as calcification. Cyclosporine 95-98 peptidylprolyl isomerase A Homo sapiens 15-19 32708451-9 2020 We showed that the in-vitro inhibition of PPIA with ciclosporin A (CsA) resulted in downregulation of PPIA and fibronectin (FN1) expression and significantly reduced their secretion. Cyclosporine 52-65 peptidylprolyl isomerase A Homo sapiens 42-46 32708451-9 2020 We showed that the in-vitro inhibition of PPIA with ciclosporin A (CsA) resulted in downregulation of PPIA and fibronectin (FN1) expression and significantly reduced their secretion. Cyclosporine 52-65 peptidylprolyl isomerase A Homo sapiens 102-106 32708451-9 2020 We showed that the in-vitro inhibition of PPIA with ciclosporin A (CsA) resulted in downregulation of PPIA and fibronectin (FN1) expression and significantly reduced their secretion. Cyclosporine 67-70 peptidylprolyl isomerase A Homo sapiens 42-46 32708451-9 2020 We showed that the in-vitro inhibition of PPIA with ciclosporin A (CsA) resulted in downregulation of PPIA and fibronectin (FN1) expression and significantly reduced their secretion. Cyclosporine 67-70 peptidylprolyl isomerase A Homo sapiens 102-106 31634494-8 2020 The interruption of interaction between CypA and N protein by CsA and its derivatives suggest a mechanism how CypA inhibitors suppress viral replication. Cyclosporine 62-65 peptidylprolyl isomerase A Homo sapiens 110-114 30198892-8 2018 This first structure of the CypA-ALV complex shows that the binding of ALV is highly similar to that of CsA. Cyclosporine 104-107 peptidylprolyl isomerase A Homo sapiens 28-32 30814280-5 2019 Adaptation of N57A HIV-1LAI selected for a second CA mutation, G94D, which rescued the N57A infectivity defect in HIV-1LAI but not HIV-1NL4-3 The rescue of N57A by G94D in HIV-1LAI is abrogated by CsA treatment in some cell types, demonstrating that this rescue is CypA dependent. Cyclosporine 197-200 peptidylprolyl isomerase A Homo sapiens 265-269 31413881-3 2019 New approaches based on CypA are currently being developed for the treatment of limb ischemia, neutralization of the side effects of Cyclosporine A (CsA) therapy, etc. Cyclosporine 133-147 peptidylprolyl isomerase A Homo sapiens 24-28 31413881-3 2019 New approaches based on CypA are currently being developed for the treatment of limb ischemia, neutralization of the side effects of Cyclosporine A (CsA) therapy, etc. Cyclosporine 149-152 peptidylprolyl isomerase A Homo sapiens 24-28 30359668-3 2018 To overcome these limitations, we invented a new strategy to carry CsA by fusing its cognate human receptor, cyclophilin A (CypA), to a 73 kDa elastin-like polypeptide (ELP) termed A192 using recombinant protein expression. Cyclosporine 67-70 peptidylprolyl isomerase A Homo sapiens 109-122 30359668-3 2018 To overcome these limitations, we invented a new strategy to carry CsA by fusing its cognate human receptor, cyclophilin A (CypA), to a 73 kDa elastin-like polypeptide (ELP) termed A192 using recombinant protein expression. Cyclosporine 67-70 peptidylprolyl isomerase A Homo sapiens 124-128 29643244-7 2018 Treatment of SUN1-expressing cells with cyclosporine (CsA) significantly reduced the sensitivity of the virus to SUN1, and an HIV-1 mutant containing CA-G89A, which does not interact with cyclophilin A (CypA), was resistant to SUN1 overexpression. Cyclosporine 54-57 peptidylprolyl isomerase A Homo sapiens 203-207 27033630-2 2017 Besides acting as a cellular receptor for immunosuppressive drug cyclosporine A (CsA), CypA is involved in various cellular activities. Cyclosporine 65-79 peptidylprolyl isomerase A Homo sapiens 87-91 28062572-1 2017 Cyclophilin A (CypA), a well-recognized receptor for anti-inflammatory drug cyclosporine A (CsA) is a ubiquitous and multifunctional protein. Cyclosporine 76-90 peptidylprolyl isomerase A Homo sapiens 0-13 28062572-1 2017 Cyclophilin A (CypA), a well-recognized receptor for anti-inflammatory drug cyclosporine A (CsA) is a ubiquitous and multifunctional protein. Cyclosporine 76-90 peptidylprolyl isomerase A Homo sapiens 15-19 28062572-1 2017 Cyclophilin A (CypA), a well-recognized receptor for anti-inflammatory drug cyclosporine A (CsA) is a ubiquitous and multifunctional protein. Cyclosporine 92-95 peptidylprolyl isomerase A Homo sapiens 0-13 28062572-1 2017 Cyclophilin A (CypA), a well-recognized receptor for anti-inflammatory drug cyclosporine A (CsA) is a ubiquitous and multifunctional protein. Cyclosporine 92-95 peptidylprolyl isomerase A Homo sapiens 15-19 28790108-3 2017 Cyclophilin A (CypA) is a cytosolic protein that belongs to the peptidyl-prolyl isomerase (PPIase) family and the major intracellular target of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 171-184 peptidylprolyl isomerase A Homo sapiens 0-13 28790108-3 2017 Cyclophilin A (CypA) is a cytosolic protein that belongs to the peptidyl-prolyl isomerase (PPIase) family and the major intracellular target of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 171-184 peptidylprolyl isomerase A Homo sapiens 15-19 28790108-3 2017 Cyclophilin A (CypA) is a cytosolic protein that belongs to the peptidyl-prolyl isomerase (PPIase) family and the major intracellular target of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 186-189 peptidylprolyl isomerase A Homo sapiens 0-13 28790108-3 2017 Cyclophilin A (CypA) is a cytosolic protein that belongs to the peptidyl-prolyl isomerase (PPIase) family and the major intracellular target of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 186-189 peptidylprolyl isomerase A Homo sapiens 15-19 28729360-2 2017 In addition to its role as a host-cell receptor for cyclosporine A, CypA has diverse functions in inflammatory conditions and diseases. Cyclosporine 52-66 peptidylprolyl isomerase A Homo sapiens 68-72 27033630-2 2017 Besides acting as a cellular receptor for immunosuppressive drug cyclosporine A (CsA), CypA is involved in various cellular activities. Cyclosporine 81-84 peptidylprolyl isomerase A Homo sapiens 87-91 26994210-4 2016 The prototypic inhibitor CsA (cyclosporin A) of both cyclophilins as well as the new water-soluble MM258 derivative prevented this suppression. Cyclosporine 30-43 peptidylprolyl isomerase A Homo sapiens 53-65 27642560-4 2016 Experiments with CyPA-specific siRNA, or with cyclosporine A, an inhibitor of CyPA, confirmed that H2O2-mediated upregulation of HCMV replication is specifically mediated by upregulation of CyPA expression. Cyclosporine 46-60 peptidylprolyl isomerase A Homo sapiens 78-82 27642560-4 2016 Experiments with CyPA-specific siRNA, or with cyclosporine A, an inhibitor of CyPA, confirmed that H2O2-mediated upregulation of HCMV replication is specifically mediated by upregulation of CyPA expression. Cyclosporine 46-60 peptidylprolyl isomerase A Homo sapiens 78-82 27279606-7 2016 Interestingly, the infectivity of wild-type or P90A virus could be rescued from the MX2-independent IFN-alpha-induced blocks in THP-1 cells by treatment with cyclosporine (Cs) or its nonimmunosuppressive analogue SDZ-NIM811, indicating that Cs-sensitive host cell cyclophilins other than CypA contribute to the activity of IFN-alpha-induced blocks. Cyclosporine 158-170 peptidylprolyl isomerase A Homo sapiens 288-292 26994210-4 2016 The prototypic inhibitor CsA (cyclosporin A) of both cyclophilins as well as the new water-soluble MM258 derivative prevented this suppression. Cyclosporine 25-28 peptidylprolyl isomerase A Homo sapiens 53-65 26792730-4 2016 Utilizing human Jurkat T cells, we demonstrate that CrkII-SH3N binding of C3G is inhibited by cyclosporin A (CsA) plus FK506 that inhibit the cyclophilin A (CypA) and FK506 binding protein (FKBP) peptidyl-prolyl cis-trans isomerases (PPIases; also termed immunophilins), respectively. Cyclosporine 94-107 peptidylprolyl isomerase A Homo sapiens 142-155 27041481-2 2016 Cyclophilin A (Cyp A) is a target protein implicated in the mechanism of action of immunosuppressive compounds such as Cyclosporine A (CsA). Cyclosporine 135-138 peptidylprolyl isomerase A Homo sapiens 0-13 27041481-2 2016 Cyclophilin A (Cyp A) is a target protein implicated in the mechanism of action of immunosuppressive compounds such as Cyclosporine A (CsA). Cyclosporine 135-138 peptidylprolyl isomerase A Homo sapiens 15-20 27041481-6 2016 The same than CsA, Gracilin H, A and Tetrahydroaplysulphurin-1 were able to inhibit phosphatase activity once the complex between Cyp A-CsA/Spongionella compounds was formed. Cyclosporine 14-17 peptidylprolyl isomerase A Homo sapiens 130-135 27041481-6 2016 The same than CsA, Gracilin H, A and Tetrahydroaplysulphurin-1 were able to inhibit phosphatase activity once the complex between Cyp A-CsA/Spongionella compounds was formed. Cyclosporine 136-139 peptidylprolyl isomerase A Homo sapiens 130-135 26792730-4 2016 Utilizing human Jurkat T cells, we demonstrate that CrkII-SH3N binding of C3G is inhibited by cyclosporin A (CsA) plus FK506 that inhibit the cyclophilin A (CypA) and FK506 binding protein (FKBP) peptidyl-prolyl cis-trans isomerases (PPIases; also termed immunophilins), respectively. Cyclosporine 94-107 peptidylprolyl isomerase A Homo sapiens 157-161 26792730-4 2016 Utilizing human Jurkat T cells, we demonstrate that CrkII-SH3N binding of C3G is inhibited by cyclosporin A (CsA) plus FK506 that inhibit the cyclophilin A (CypA) and FK506 binding protein (FKBP) peptidyl-prolyl cis-trans isomerases (PPIases; also termed immunophilins), respectively. Cyclosporine 109-112 peptidylprolyl isomerase A Homo sapiens 142-155 26792730-4 2016 Utilizing human Jurkat T cells, we demonstrate that CrkII-SH3N binding of C3G is inhibited by cyclosporin A (CsA) plus FK506 that inhibit the cyclophilin A (CypA) and FK506 binding protein (FKBP) peptidyl-prolyl cis-trans isomerases (PPIases; also termed immunophilins), respectively. Cyclosporine 109-112 peptidylprolyl isomerase A Homo sapiens 157-161 26752561-9 2016 Moreover, inhibition of PPIA with cyclosporine A blocked cell growth of the cell lines, the effect size was associated with the PPIA expression levels. Cyclosporine 34-48 peptidylprolyl isomerase A Homo sapiens 24-28 26752561-9 2016 Moreover, inhibition of PPIA with cyclosporine A blocked cell growth of the cell lines, the effect size was associated with the PPIA expression levels. Cyclosporine 34-48 peptidylprolyl isomerase A Homo sapiens 128-132 25738284-2 2015 CypA is the major cellular target for the immunosuppressive drug cyclosporin A and mediates its actions. Cyclosporine 65-78 peptidylprolyl isomerase A Homo sapiens 0-4 26264861-2 2016 CsA has been shown to be a safe and highly effective immunosuppressive drug that binds with the protein Cyclophilin A (CypA) at active sites. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 104-117 26264861-2 2016 CsA has been shown to be a safe and highly effective immunosuppressive drug that binds with the protein Cyclophilin A (CypA) at active sites. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 119-123 26264861-4 2016 In this project, we elucidate the binding of CsA to CypA at the molecular level by computing their electron structures and revealing their interactions. Cyclosporine 45-48 peptidylprolyl isomerase A Homo sapiens 52-56 26264861-6 2016 We have identified the wave function of CypA, the biological active residues and active atoms of CypA and CsA, the interaction site between CypA and CsA, and the hydrogen bonds in the ligand CsA binding site. Cyclosporine 106-109 peptidylprolyl isomerase A Homo sapiens 40-44 26030368-1 2015 Cyclophilins are peptidyl cis-trans prolyl isomerases (PPIases), whose activity is typically inhibited by cyclosporine A (CsA), a potent immunosuppressor. Cyclosporine 106-120 peptidylprolyl isomerase A Homo sapiens 0-12 26030368-1 2015 Cyclophilins are peptidyl cis-trans prolyl isomerases (PPIases), whose activity is typically inhibited by cyclosporine A (CsA), a potent immunosuppressor. Cyclosporine 122-125 peptidylprolyl isomerase A Homo sapiens 0-12 26030368-5 2015 Although highly homologous, CY and the archetypal cyclophilin A (CyPA) present distinct catalytic and CsA-binding activities owing to unique structural features between these cylophilins. Cyclosporine 102-105 peptidylprolyl isomerase A Homo sapiens 50-63 26030368-5 2015 Although highly homologous, CY and the archetypal cyclophilin A (CyPA) present distinct catalytic and CsA-binding activities owing to unique structural features between these cylophilins. Cyclosporine 102-105 peptidylprolyl isomerase A Homo sapiens 65-69 25743766-5 2015 CyPA was initially discovered as the intracellular receptor of the immunosuppressive drug cyclosporine 30 years ago. Cyclosporine 90-102 peptidylprolyl isomerase A Homo sapiens 0-4 24200080-4 2014 Cyclophilin A (CypA) and other members of this family are inhibited by cyclosporin A (CsA) which sensitized diverse drug-resistant tumor cell lines in vitro to cisplatin. Cyclosporine 71-84 peptidylprolyl isomerase A Homo sapiens 0-13 25048953-6 2014 Cyclic peptides, which bind and inhibit cyclophilins without having immunosuppressive properties, have been generated by chemical modifications of cyclosporin A. Cyclosporine 147-160 peptidylprolyl isomerase A Homo sapiens 40-52 24479545-3 2014 Disruption of CypA binding to CA, either by genetic means or by the competitive inhibitor cyclosporine A (CsA), reduces the efficiency of HIV-1 transduction in some cells but not in others. Cyclosporine 90-104 peptidylprolyl isomerase A Homo sapiens 14-18 24479545-3 2014 Disruption of CypA binding to CA, either by genetic means or by the competitive inhibitor cyclosporine A (CsA), reduces the efficiency of HIV-1 transduction in some cells but not in others. Cyclosporine 106-109 peptidylprolyl isomerase A Homo sapiens 14-18 24663101-2 2014 Interference with cyclophilin A binding, either by mutations in the HIV-1 capsid protein (CA) or by the drug cyclosporine A (CsA), inhibits HIV-1 replication in cell culture. Cyclosporine 109-123 peptidylprolyl isomerase A Homo sapiens 18-31 24663101-2 2014 Interference with cyclophilin A binding, either by mutations in the HIV-1 capsid protein (CA) or by the drug cyclosporine A (CsA), inhibits HIV-1 replication in cell culture. Cyclosporine 125-128 peptidylprolyl isomerase A Homo sapiens 18-31 24200080-4 2014 Cyclophilin A (CypA) and other members of this family are inhibited by cyclosporin A (CsA) which sensitized diverse drug-resistant tumor cell lines in vitro to cisplatin. Cyclosporine 71-84 peptidylprolyl isomerase A Homo sapiens 15-19 24200080-4 2014 Cyclophilin A (CypA) and other members of this family are inhibited by cyclosporin A (CsA) which sensitized diverse drug-resistant tumor cell lines in vitro to cisplatin. Cyclosporine 86-89 peptidylprolyl isomerase A Homo sapiens 0-13 24200080-4 2014 Cyclophilin A (CypA) and other members of this family are inhibited by cyclosporin A (CsA) which sensitized diverse drug-resistant tumor cell lines in vitro to cisplatin. Cyclosporine 86-89 peptidylprolyl isomerase A Homo sapiens 15-19 24227937-4 2013 CypA, a cytosolic binding protein of the immunosuppressive drug cyclosporine A, is overexpressed in many cancer types and often associated with malignant transformation. Cyclosporine 64-78 peptidylprolyl isomerase A Homo sapiens 0-4 23152499-7 2012 We show that cyclosporine A added to a sample containing NS5B(Delta21), NS5A-D2, and CypA specifically inhibits the interaction between CypA and NS5A-D2 without altering the one between NS5A-D2 and NS5B(Delta21). Cyclosporine 13-27 peptidylprolyl isomerase A Homo sapiens 85-89 23846495-11 2013 Finally, cyclosporine A and CyPA-peptidyl-prolyl cis-trans isomerase mutant, R55A, inhibited AngII-stimulated CyPA and p47phox association in VSMC, suggesting that peptidyl-prolyl cis-trans isomerase activity was required for their interaction. Cyclosporine 9-23 peptidylprolyl isomerase A Homo sapiens 110-114 23849880-4 2013 A drug template for CypA inhibition is cyclosporine A (CsA), a cyclic undecapeptide that simultaneously binds to both CypA and the Ca(2+)-dependent phosphatase calcineurin (CN), and can attenuate immune responses. Cyclosporine 39-53 peptidylprolyl isomerase A Homo sapiens 20-24 23849880-4 2013 A drug template for CypA inhibition is cyclosporine A (CsA), a cyclic undecapeptide that simultaneously binds to both CypA and the Ca(2+)-dependent phosphatase calcineurin (CN), and can attenuate immune responses. Cyclosporine 39-53 peptidylprolyl isomerase A Homo sapiens 118-122 23849880-4 2013 A drug template for CypA inhibition is cyclosporine A (CsA), a cyclic undecapeptide that simultaneously binds to both CypA and the Ca(2+)-dependent phosphatase calcineurin (CN), and can attenuate immune responses. Cyclosporine 55-58 peptidylprolyl isomerase A Homo sapiens 20-24 23849880-4 2013 A drug template for CypA inhibition is cyclosporine A (CsA), a cyclic undecapeptide that simultaneously binds to both CypA and the Ca(2+)-dependent phosphatase calcineurin (CN), and can attenuate immune responses. Cyclosporine 55-58 peptidylprolyl isomerase A Homo sapiens 118-122 23849880-5 2013 Synthetic modifications of the CsA scaffold allows for selective binding to CypA and CN separately, thus providing access to novel, non-immunosuppressive antiviral agents. Cyclosporine 31-34 peptidylprolyl isomerase A Homo sapiens 76-80 23152531-8 2013 Furthermore, upon fractionation of intracellular membranes in density gradients, CypA was found to cosediment with membranous EAV replication structures, which could be prevented by CsA treatment. Cyclosporine 182-185 peptidylprolyl isomerase A Homo sapiens 81-85 23665451-5 2013 In this study, we evaluated whether the chiHIV vector efficiently transduces human cells, and the transduction efficiency might increase by a CypA inhibitor (cyclosporine) and a proteasome inhibitor (MG132). Cyclosporine 158-170 peptidylprolyl isomerase A Homo sapiens 142-146 23224887-3 2013 Similar effect on functional expression of NCX1 protein can be obtained also without CsA treatment by knockdown of cell cyclophilin A (CypA), one of the cellular receptor of CsA. Cyclosporine 174-177 peptidylprolyl isomerase A Homo sapiens 120-133 23224887-3 2013 Similar effect on functional expression of NCX1 protein can be obtained also without CsA treatment by knockdown of cell cyclophilin A (CypA), one of the cellular receptor of CsA. Cyclosporine 174-177 peptidylprolyl isomerase A Homo sapiens 135-139 23224887-4 2013 This suggests that CypA has a role in acquisition of function competence of NCX1 protein.Unlike CsA treatment, which affects the functional expression of all three mammalian NCX proteins similarly, FK506 and rapamycin treatment modulates only the functional expression of NCX2 and NCX3 proteins. Cyclosporine 96-99 peptidylprolyl isomerase A Homo sapiens 19-23 22902549-9 2013 Cyp inhibitors such as cyclosporine A (CsA) or non-immunosuppressive derivates such as alisporivir and SCY-635, prevent IRF9-CypA complex formation. Cyclosporine 23-37 peptidylprolyl isomerase A Homo sapiens 125-129 22902549-9 2013 Cyp inhibitors such as cyclosporine A (CsA) or non-immunosuppressive derivates such as alisporivir and SCY-635, prevent IRF9-CypA complex formation. Cyclosporine 39-42 peptidylprolyl isomerase A Homo sapiens 125-129 23152499-7 2012 We show that cyclosporine A added to a sample containing NS5B(Delta21), NS5A-D2, and CypA specifically inhibits the interaction between CypA and NS5A-D2 without altering the one between NS5A-D2 and NS5B(Delta21). Cyclosporine 13-27 peptidylprolyl isomerase A Homo sapiens 136-140 23342381-5 2012 The CypA binding pattern of truncated NS5A genotypes correlated with the susceptibility of these replicons to CsA. Cyclosporine 110-113 peptidylprolyl isomerase A Homo sapiens 4-8 22846842-8 2012 In addition, CsA compromised the UVB-induced checkpoint function by upregulating the molecular chaperone protein cyclophilin A (CypA). Cyclosporine 13-16 peptidylprolyl isomerase A Homo sapiens 113-126 22906739-4 2012 The binding affinity of compound 1a to CypA has been confirmed by Fortebio"s Octet RED system and the increased phosphorylation of ERK in H446 cells is observed by treatment with both compound 1a and CsA. Cyclosporine 200-203 peptidylprolyl isomerase A Homo sapiens 39-43 22846842-12 2012 Our findings identified deregulation of XPC and CypA as key targets of CsA, and UVB damage and PI3K/AKT activation as two principal drivers for CsA-sensitized skin tumorigenesis, further supporting an immunosuppression-independent mechanism of CsA action on skin tumorigenesis. Cyclosporine 71-74 peptidylprolyl isomerase A Homo sapiens 48-52 22846842-8 2012 In addition, CsA compromised the UVB-induced checkpoint function by upregulating the molecular chaperone protein cyclophilin A (CypA). Cyclosporine 13-16 peptidylprolyl isomerase A Homo sapiens 128-132 22846842-10 2012 CsA-induced phosphoinositide 3-kinase(PI3K)/AKT activation was required for both XPC suppression and CypA upregulation. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 101-105 22814107-1 2012 Cyclophilin A (CyPA) is a peptidyl-prolyl cis/trans isomerase originally identified as the target of the immunosuppressive drug cyclosporine A. Cyclosporine 128-142 peptidylprolyl isomerase A Homo sapiens 0-13 22814107-1 2012 Cyclophilin A (CyPA) is a peptidyl-prolyl cis/trans isomerase originally identified as the target of the immunosuppressive drug cyclosporine A. Cyclosporine 128-142 peptidylprolyl isomerase A Homo sapiens 15-19 21728990-1 2011 Cyclophilin A (CyPA) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA) which possesses peptidyl-prodyl cis/trans isomerase (PPIase) activity. Cyclosporine 71-84 peptidylprolyl isomerase A Homo sapiens 0-13 22615963-9 2012 Finally, CsA could enhance the binding between CypA and M1. Cyclosporine 9-12 peptidylprolyl isomerase A Homo sapiens 47-51 22615963-10 2012 The above results suggested that CsA inhibited the replication of influenza A virus through CypA-dependent and -independent pathways. Cyclosporine 33-36 peptidylprolyl isomerase A Homo sapiens 92-96 22316150-6 2012 In the absence of a functional CypA, e.g., by the addition of an inhibitor such as cyclosporine A (CsA), HIV-1 has reduced infectivity. Cyclosporine 83-97 peptidylprolyl isomerase A Homo sapiens 31-35 22316150-6 2012 In the absence of a functional CypA, e.g., by the addition of an inhibitor such as cyclosporine A (CsA), HIV-1 has reduced infectivity. Cyclosporine 99-102 peptidylprolyl isomerase A Homo sapiens 31-35 21728990-1 2011 Cyclophilin A (CyPA) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA) which possesses peptidyl-prodyl cis/trans isomerase (PPIase) activity. Cyclosporine 71-84 peptidylprolyl isomerase A Homo sapiens 15-19 21728990-1 2011 Cyclophilin A (CyPA) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA) which possesses peptidyl-prodyl cis/trans isomerase (PPIase) activity. Cyclosporine 86-89 peptidylprolyl isomerase A Homo sapiens 0-13 21728990-1 2011 Cyclophilin A (CyPA) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA) which possesses peptidyl-prodyl cis/trans isomerase (PPIase) activity. Cyclosporine 86-89 peptidylprolyl isomerase A Homo sapiens 15-19 22046132-8 2011 Conversely, inhibition of cyclophilins by cyclosporine A (CspA) blocked the replication of CoVs of all genera, including SARS-CoV, human CoV-229E and -NL-63, feline CoV, as well as avian infectious bronchitis virus. Cyclosporine 42-56 peptidylprolyl isomerase A Homo sapiens 26-38 21963115-1 2011 Potent cyclophilin A (CypA) inhibitors such as non-immunosuppressive cyclosporin A (CsA) derivatives have been already used in clinical trials in patients with viral infections. Cyclosporine 69-82 peptidylprolyl isomerase A Homo sapiens 7-20 21963115-1 2011 Potent cyclophilin A (CypA) inhibitors such as non-immunosuppressive cyclosporin A (CsA) derivatives have been already used in clinical trials in patients with viral infections. Cyclosporine 69-82 peptidylprolyl isomerase A Homo sapiens 22-26 21963115-1 2011 Potent cyclophilin A (CypA) inhibitors such as non-immunosuppressive cyclosporin A (CsA) derivatives have been already used in clinical trials in patients with viral infections. Cyclosporine 84-87 peptidylprolyl isomerase A Homo sapiens 7-20 21963115-1 2011 Potent cyclophilin A (CypA) inhibitors such as non-immunosuppressive cyclosporin A (CsA) derivatives have been already used in clinical trials in patients with viral infections. Cyclosporine 84-87 peptidylprolyl isomerase A Homo sapiens 22-26 21963115-6 2011 However, in the context of the CsA framework a net charge of -7 clustered at the amino acid side chain of position 1 resulted in slightly improved CypA inhibition. Cyclosporine 31-34 peptidylprolyl isomerase A Homo sapiens 147-151 22046132-8 2011 Conversely, inhibition of cyclophilins by cyclosporine A (CspA) blocked the replication of CoVs of all genera, including SARS-CoV, human CoV-229E and -NL-63, feline CoV, as well as avian infectious bronchitis virus. Cyclosporine 58-62 peptidylprolyl isomerase A Homo sapiens 26-38 20602248-5 2010 Here, we discuss structural and functional aspects of the human cyclophilins and their interaction with various intra-cellular targets that can be under the control of CsA or its complexes with diverse cyclophilins that are selectively expressed in different cellular compartments. Cyclosporine 168-171 peptidylprolyl isomerase A Homo sapiens 64-76 21396746-2 2011 After testing these three synthetic peptides, we found that the peptide Trp-Gly-Pro (WGP) showed comparable inhibitory ability as positive control cyclosporine A (CsA) on CypA-mediated PPIase activity with IC50 values of 33.11 nM and 10.25 nM, respectively. Cyclosporine 147-161 peptidylprolyl isomerase A Homo sapiens 171-175 21396746-2 2011 After testing these three synthetic peptides, we found that the peptide Trp-Gly-Pro (WGP) showed comparable inhibitory ability as positive control cyclosporine A (CsA) on CypA-mediated PPIase activity with IC50 values of 33.11 nM and 10.25 nM, respectively. Cyclosporine 163-166 peptidylprolyl isomerase A Homo sapiens 171-175 24900335-1 2011 Cyclosporine A (CsA) and its chemical analogues EthVal4Cs, MeVal4Cs, and Me(d-Ala)3EthVal4Cs (Alisporivir) all interact with cyclophilin A (CypA). Cyclosporine 0-14 peptidylprolyl isomerase A Homo sapiens 125-138 24900335-1 2011 Cyclosporine A (CsA) and its chemical analogues EthVal4Cs, MeVal4Cs, and Me(d-Ala)3EthVal4Cs (Alisporivir) all interact with cyclophilin A (CypA). Cyclosporine 0-14 peptidylprolyl isomerase A Homo sapiens 140-144 24900335-1 2011 Cyclosporine A (CsA) and its chemical analogues EthVal4Cs, MeVal4Cs, and Me(d-Ala)3EthVal4Cs (Alisporivir) all interact with cyclophilin A (CypA). Cyclosporine 16-19 peptidylprolyl isomerase A Homo sapiens 125-138 24900335-1 2011 Cyclosporine A (CsA) and its chemical analogues EthVal4Cs, MeVal4Cs, and Me(d-Ala)3EthVal4Cs (Alisporivir) all interact with cyclophilin A (CypA). Cyclosporine 16-19 peptidylprolyl isomerase A Homo sapiens 140-144 21593166-4 2011 CypA inhibitors such as cyclosporine (CsA) have been shown to inhibit hepatitis C virus (HCV) replication. Cyclosporine 24-36 peptidylprolyl isomerase A Homo sapiens 0-4 21593166-4 2011 CypA inhibitors such as cyclosporine (CsA) have been shown to inhibit hepatitis C virus (HCV) replication. Cyclosporine 38-41 peptidylprolyl isomerase A Homo sapiens 0-4 21489988-9 2011 CypA indeed interacts with NS5A-D3, and this interaction is completely abolished by cyclosporin A. Cyclosporine 84-97 peptidylprolyl isomerase A Homo sapiens 0-4 20602248-5 2010 Here, we discuss structural and functional aspects of the human cyclophilins and their interaction with various intra-cellular targets that can be under the control of CsA or its complexes with diverse cyclophilins that are selectively expressed in different cellular compartments. Cyclosporine 168-171 peptidylprolyl isomerase A Homo sapiens 202-214 20451281-8 2010 Remarkably, CsA prevents the CypA-NS5A interaction in a dose-dependent manner. Cyclosporine 12-15 peptidylprolyl isomerase A Homo sapiens 29-33 20945139-1 2010 The fungal cyclic peptide cyclosporin A (CsA) and fungal macrolide compound sanglifehrin A (SFA) have been developed as immunosuppressive drugs and both bind to cyclophilin A (CypA). Cyclosporine 41-44 peptidylprolyl isomerase A Homo sapiens 161-174 20945139-1 2010 The fungal cyclic peptide cyclosporin A (CsA) and fungal macrolide compound sanglifehrin A (SFA) have been developed as immunosuppressive drugs and both bind to cyclophilin A (CypA). Cyclosporine 41-44 peptidylprolyl isomerase A Homo sapiens 176-180 21994697-4 2010 Importantly, Cyclosporine A derivatives that lack immunosuppressive function efficiently block the CyPA-NS5A interaction and inhibit HCV in cell culture, an animal model, and human trials. Cyclosporine 13-27 peptidylprolyl isomerase A Homo sapiens 99-103 20681522-10 2010 In this work, we show that knockdown of cell CypA using targeting siRNA (without any CsA treatment) results in a reduction in the level of NCX1 surface expression, a decrease in the level of Na(+)-dependent Ca(2+) uptake, and no change in the total amount of cell NCX1 protein in NCX1.5-transfected HEK 293 cells and nontransfected H9c2 cells that express NCX1.1 naturally. Cyclosporine 85-88 peptidylprolyl isomerase A Homo sapiens 45-49 20681522-13 2010 Overexpression of CypA or its R55A mutant, which exhibits a substantially reduced PPIase activity, alleviated the reduction of NCX1 surface expression caused by CsA treatment, suggesting that the PPIase domain was probably not mandatory for NCX1 functional expression. Cyclosporine 161-164 peptidylprolyl isomerase A Homo sapiens 18-22 20451281-9 2010 Importantly, the CypA-NS5A interaction is conserved among genotypes and is interrupted by CsA. Cyclosporine 90-93 peptidylprolyl isomerase A Homo sapiens 17-21 20451281-10 2010 Surprisingly, the NS5A mutant protein, which arose in CsA-resistant HCV variants, behaves similarly to wild-type NS5A in terms of both CypA binding and CsA-mediated release from CypA. Cyclosporine 152-155 peptidylprolyl isomerase A Homo sapiens 178-182 20364129-2 2010 CypA suppresses T-cell activation through cyclosporine complexation and is required for effective HIV-1 replication in host cells. Cyclosporine 42-54 peptidylprolyl isomerase A Homo sapiens 0-4 20132841-7 2010 Importantly, the NS5A-CypA interactions were sensitive to CsA in a dose-responsive manner and an isomerase mutant of CypA interacted with NS5A less efficiently than wild-type CypA. Cyclosporine 58-61 peptidylprolyl isomerase A Homo sapiens 22-26 20132841-7 2010 Importantly, the NS5A-CypA interactions were sensitive to CsA in a dose-responsive manner and an isomerase mutant of CypA interacted with NS5A less efficiently than wild-type CypA. Cyclosporine 58-61 peptidylprolyl isomerase A Homo sapiens 117-121 20132841-7 2010 Importantly, the NS5A-CypA interactions were sensitive to CsA in a dose-responsive manner and an isomerase mutant of CypA interacted with NS5A less efficiently than wild-type CypA. Cyclosporine 58-61 peptidylprolyl isomerase A Homo sapiens 117-121 20132841-8 2010 These findings correlate the anti-HCV properties of CsA with an ability of the compound to disrupt NS5A-CypA interactions in vitro and in vivo, whilst providing the basis for development of assay platforms suitable to screen compound libraries for novel inhibitors of the NS5A-CypA interaction. Cyclosporine 52-55 peptidylprolyl isomerase A Homo sapiens 104-108 20132841-8 2010 These findings correlate the anti-HCV properties of CsA with an ability of the compound to disrupt NS5A-CypA interactions in vitro and in vivo, whilst providing the basis for development of assay platforms suitable to screen compound libraries for novel inhibitors of the NS5A-CypA interaction. Cyclosporine 52-55 peptidylprolyl isomerase A Homo sapiens 277-281 20132841-2 2010 CsA inhibits isomerase activity of cellular-encoded cyclophilin proteins, of which cyclophilin A (CypA) in particular is required for HCV replication. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 98-102 20364129-4 2010 We determined atomic-resolution structures of acetylated CypA and its complexes with cyclosporine and HIV-1 capsid. Cyclosporine 85-97 peptidylprolyl isomerase A Homo sapiens 57-61 20364129-6 2010 Furthermore, CypA acetylation antagonized the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. Cyclosporine 75-87 peptidylprolyl isomerase A Homo sapiens 13-17 20364129-6 2010 Furthermore, CypA acetylation antagonized the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. Cyclosporine 126-138 peptidylprolyl isomerase A Homo sapiens 13-17 19865066-1 2009 Cyclophilin A (CypA) is a cytosolic binding protein of the immunosuppressive drug cyclosporin A. Cyclosporine 82-95 peptidylprolyl isomerase A Homo sapiens 15-19 19656870-2 2009 In Jurkat T lymphocytes, disrupting CypA-CA interaction either by cyclosporine (Cs) treatment or by alteration (e.g., P90A) of the CA inhibits HIV-1 infection. Cyclosporine 66-78 peptidylprolyl isomerase A Homo sapiens 36-40 19656870-2 2009 In Jurkat T lymphocytes, disrupting CypA-CA interaction either by cyclosporine (Cs) treatment or by alteration (e.g., P90A) of the CA inhibits HIV-1 infection. Cyclosporine 80-82 peptidylprolyl isomerase A Homo sapiens 36-40 19656870-6 2009 Reducing the binding of CypA to the A92E mutant capsid, either by Cs treatment or by an additional P90A change in the CA protein, increased the amount of particulate capsids and viral infectivity in HeLa cells. Cyclosporine 66-68 peptidylprolyl isomerase A Homo sapiens 24-28 20089655-7 2010 The inflammatory response and serum ALT/AST level were reduced when the chemotactic effect of CypA was inhibited by cyclosporine and anti-CD147 antibody. Cyclosporine 116-128 peptidylprolyl isomerase A Homo sapiens 94-98 20204291-3 2010 Cyclophilin A (CypA), a target of immunosuppressive drugs cyclosporin A (CsA) and sanglifehrin A (SFA), is an intracellular protein that has peptidyl-prolyl cis-trans isomerase (PPIase) enzymatic activity. Cyclosporine 58-71 peptidylprolyl isomerase A Homo sapiens 0-13 20204291-3 2010 Cyclophilin A (CypA), a target of immunosuppressive drugs cyclosporin A (CsA) and sanglifehrin A (SFA), is an intracellular protein that has peptidyl-prolyl cis-trans isomerase (PPIase) enzymatic activity. Cyclosporine 58-71 peptidylprolyl isomerase A Homo sapiens 15-19 20204291-3 2010 Cyclophilin A (CypA), a target of immunosuppressive drugs cyclosporin A (CsA) and sanglifehrin A (SFA), is an intracellular protein that has peptidyl-prolyl cis-trans isomerase (PPIase) enzymatic activity. Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 0-13 20204291-3 2010 Cyclophilin A (CypA), a target of immunosuppressive drugs cyclosporin A (CsA) and sanglifehrin A (SFA), is an intracellular protein that has peptidyl-prolyl cis-trans isomerase (PPIase) enzymatic activity. Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 15-19 20204291-10 2010 In conclusion, CsA or SFA in combination with cisplatin synergistically enhances cisplatin-induced apoptosis in C6 glioma cells via inhibition of PPIase activity of CypA, indicating that development of new drugs that selectively inhibit the CypA PPIase activity without immune suppression may facilitate alleviation of chemoresistance in treatment of high-grade glioma. Cyclosporine 15-18 peptidylprolyl isomerase A Homo sapiens 165-169 20204291-10 2010 In conclusion, CsA or SFA in combination with cisplatin synergistically enhances cisplatin-induced apoptosis in C6 glioma cells via inhibition of PPIase activity of CypA, indicating that development of new drugs that selectively inhibit the CypA PPIase activity without immune suppression may facilitate alleviation of chemoresistance in treatment of high-grade glioma. Cyclosporine 15-18 peptidylprolyl isomerase A Homo sapiens 241-245 19865066-1 2009 Cyclophilin A (CypA) is a cytosolic binding protein of the immunosuppressive drug cyclosporin A. Cyclosporine 82-95 peptidylprolyl isomerase A Homo sapiens 0-13 19691347-2 2009 The activities of the two most potent CypA inhibitors (3h and 3i) are 2.59 and 1.52 nM, respectively, which are about 16 and 27 times more potent than that of cyclosporin A. Cyclosporine 159-172 peptidylprolyl isomerase A Homo sapiens 38-42 19211263-7 2009 Noncovalent complexes of holomyoglobin and the protein-ligand complex between CypA and cyclosporin A (CsA) were also investigated at a neutral pH using the CSI-MS method. Cyclosporine 87-100 peptidylprolyl isomerase A Homo sapiens 78-82 19480458-5 2009 CypA binding of this inhibitor has been characterized by fluorescence anisotropy- and isothermal titration calorimetry-based cyclosporin competition assays. Cyclosporine 125-136 peptidylprolyl isomerase A Homo sapiens 0-4 19380579-9 2009 We then mutated residues that reside in the hydrophobic pocket of CypA where proline-containing peptide substrates and cyclosporine A bind and that are vital for the enzymatic or the hydrophobic pocket binding activity of CypA. Cyclosporine 119-133 peptidylprolyl isomerase A Homo sapiens 66-70 19451286-0 2009 Cyclosporine inhibits flavivirus replication through blocking the interaction between host cyclophilins and viral NS5 protein. Cyclosporine 0-12 peptidylprolyl isomerase A Homo sapiens 91-103 19451286-7 2009 Furthermore, antiviral experiments demonstrated that cyclosporine (Cs; an 11-amino-acid cyclic peptide known to block the PPIase activity of CyPA) inhibits flavivirus replication in cell culture at nontoxic concentrations. Cyclosporine 53-65 peptidylprolyl isomerase A Homo sapiens 141-145 19680534-8 2009 By selecting for resistance against the cyclosporine analogue DEBIO-025 that targets CypA in a dose-dependent manner, we identified two mutations (V2440A and V2440L) close to the cleavage site between nonstructural protein 5A and the RNA-dependent RNA polymerase in nonstructural protein 5B that slow down cleavage kinetics at this site and reduce CypA dependence of viral replication. Cyclosporine 40-52 peptidylprolyl isomerase A Homo sapiens 85-89 19680534-8 2009 By selecting for resistance against the cyclosporine analogue DEBIO-025 that targets CypA in a dose-dependent manner, we identified two mutations (V2440A and V2440L) close to the cleavage site between nonstructural protein 5A and the RNA-dependent RNA polymerase in nonstructural protein 5B that slow down cleavage kinetics at this site and reduce CypA dependence of viral replication. Cyclosporine 40-52 peptidylprolyl isomerase A Homo sapiens 348-352 19211263-7 2009 Noncovalent complexes of holomyoglobin and the protein-ligand complex between CypA and cyclosporin A (CsA) were also investigated at a neutral pH using the CSI-MS method. Cyclosporine 102-105 peptidylprolyl isomerase A Homo sapiens 78-82 18816083-8 2008 In addition, pretreatment of KB/V cells with a CyPA-binding immunosuppressive drug, cyclosporine A (CsA), enhanced their chemosensitivity to VCR and 5-Fu. Cyclosporine 84-98 peptidylprolyl isomerase A Homo sapiens 47-51 18673375-1 2008 BACKGROUND: The cyclophilin A (CypA)-cyclosporine (CsA) complex promotes immune response. Cyclosporine 51-54 peptidylprolyl isomerase A Homo sapiens 16-29 18673375-1 2008 BACKGROUND: The cyclophilin A (CypA)-cyclosporine (CsA) complex promotes immune response. Cyclosporine 51-54 peptidylprolyl isomerase A Homo sapiens 31-35 18673375-2 2008 The variation at the CypA gene could explain CsA-pharmacokinetics and clinical outcomes among CsA-treated patients. Cyclosporine 45-48 peptidylprolyl isomerase A Homo sapiens 21-25 18673375-2 2008 The variation at the CypA gene could explain CsA-pharmacokinetics and clinical outcomes among CsA-treated patients. Cyclosporine 94-97 peptidylprolyl isomerase A Homo sapiens 21-25 18673375-12 2008 Replication of this study in other populations is necessary to define the role of CypA-variants in the main clinical outcomes among CsA-treated kidney-transplanted patients. Cyclosporine 132-135 peptidylprolyl isomerase A Homo sapiens 82-86 18704644-4 2009 Wild-type U2OS cells treated with cyclosporine A (CsA), a peptidyl-prolyl isomerase inhibitor, displayed the same phenotype as knockdown CypA cells, suggesting that the isomerase activity of CypA is required to maintain a normal phenotype. Cyclosporine 34-48 peptidylprolyl isomerase A Homo sapiens 191-195 18704644-4 2009 Wild-type U2OS cells treated with cyclosporine A (CsA), a peptidyl-prolyl isomerase inhibitor, displayed the same phenotype as knockdown CypA cells, suggesting that the isomerase activity of CypA is required to maintain a normal phenotype. Cyclosporine 50-53 peptidylprolyl isomerase A Homo sapiens 191-195 18816083-8 2008 In addition, pretreatment of KB/V cells with a CyPA-binding immunosuppressive drug, cyclosporine A (CsA), enhanced their chemosensitivity to VCR and 5-Fu. Cyclosporine 100-103 peptidylprolyl isomerase A Homo sapiens 47-51 18567920-7 2008 CSA and HAb18G/CD147 antagonistic peptide AP-9 against CD147, respectively, dramatically decreased MMP-2 and MMP-9 expression, both in the absence or presence of CypA. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 162-166 18829531-4 2008 Loss of PRLr-CypA binding, following treatment with the PPI inhibitor cyclosporine A (CsA), or overexpression of a dominant-negative PRLr mutant (P334A) resulted in a loss of PRLr/Jak2-mediated signaling. Cyclosporine 86-89 peptidylprolyl isomerase A Homo sapiens 13-17 18653356-7 2008 Although novel ligands for cyclophilin A were not discovered, cyclosporin A, a known ligand to CypA and a blind control in the library, was identified as a hit. Cyclosporine 62-75 peptidylprolyl isomerase A Homo sapiens 95-99 17267487-2 2007 The immunosuppressive drug cyclosporine A (CsA) and its nonimmunosuppressive analogs bind with high affinity to CypA and inhibit HIV-1 replication. Cyclosporine 27-41 peptidylprolyl isomerase A Homo sapiens 112-116 17919644-7 2008 Pretreatment of CyPA with cyclosporine A prevented its effect on THP-1 cell migration; similarly, PPIase-deficient mutant CyPA protein did not induce migration of these cells. Cyclosporine 26-40 peptidylprolyl isomerase A Homo sapiens 16-20 17927958-2 2007 We used the database-mining program LIDAEUS and in silico screening to discover the dimedone family of inhibitors which show a conserved "ball and socket" binding mode with a dimethyl group in the hydrophobic binding pocket of human cyclophilin A (CypA) mimicking a key interaction of the natural inhibitor cyclosporin A (CsA). Cyclosporine 307-320 peptidylprolyl isomerase A Homo sapiens 233-246 17927958-2 2007 We used the database-mining program LIDAEUS and in silico screening to discover the dimedone family of inhibitors which show a conserved "ball and socket" binding mode with a dimethyl group in the hydrophobic binding pocket of human cyclophilin A (CypA) mimicking a key interaction of the natural inhibitor cyclosporin A (CsA). Cyclosporine 322-325 peptidylprolyl isomerase A Homo sapiens 233-246 17927958-3 2007 The most potent derivative binds CypA with a K(d) of 11.2+/-9.2 microM and an IC50 for activity against Caenorhabditis elegans (C. elegans) of 190 microM compared to 28 microM for CsA. Cyclosporine 180-183 peptidylprolyl isomerase A Homo sapiens 33-37 17609268-0 2007 Fusion of cyclophilin A to Fv1 enables cyclosporine-sensitive restriction of human and feline immunodeficiency viruses. Cyclosporine 39-51 peptidylprolyl isomerase A Homo sapiens 10-23 17609268-4 2007 Infectivity is rescued by agents such as cyclosporine that disrupt CypA binding to its substrates. Cyclosporine 41-53 peptidylprolyl isomerase A Homo sapiens 67-71 18367226-5 2008 This inhibitory action depended upon the interaction of the CypA moiety with HIV-1 capsid and disruption of CypA and capsid interaction by cyclosporine A enhanced the HIV-1 susceptibility of OWM cells even in the absence of functional TRIM5alpha. Cyclosporine 139-153 peptidylprolyl isomerase A Homo sapiens 108-112 18385230-0 2008 Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro. Cyclosporine 101-113 peptidylprolyl isomerase A Homo sapiens 0-13 18385230-4 2008 A strong correlation between CsA resistance and reduced dependency on cyclophilin A (CyPA) for replication was identified. Cyclosporine 29-32 peptidylprolyl isomerase A Homo sapiens 70-83 18385230-4 2008 A strong correlation between CsA resistance and reduced dependency on cyclophilin A (CyPA) for replication was identified. Cyclosporine 29-32 peptidylprolyl isomerase A Homo sapiens 85-89 18385230-8 2008 Depletion of CyPA alone in the CsA-resistant replicon cells eliminated CsA resistance, indicating that CyPA is the chief mediator of the observed CsA resistance. Cyclosporine 31-34 peptidylprolyl isomerase A Homo sapiens 13-17 18385230-8 2008 Depletion of CyPA alone in the CsA-resistant replicon cells eliminated CsA resistance, indicating that CyPA is the chief mediator of the observed CsA resistance. Cyclosporine 71-74 peptidylprolyl isomerase A Homo sapiens 13-17 18385230-8 2008 Depletion of CyPA alone in the CsA-resistant replicon cells eliminated CsA resistance, indicating that CyPA is the chief mediator of the observed CsA resistance. Cyclosporine 71-74 peptidylprolyl isomerase A Homo sapiens 13-17 18385230-10 2008 An interaction between CyPA and HCV RNA as well as the viral polymerase that is sensitive to CsA treatment in wild-type but not in resistant replicons was detected. Cyclosporine 93-96 peptidylprolyl isomerase A Homo sapiens 23-27 18385230-11 2008 These findings reveal the molecular mechanism of CsA resistance and identify CyPA as a critical cellular cofactor for HCV replication and infection. Cyclosporine 49-52 peptidylprolyl isomerase A Homo sapiens 77-81 17728232-5 2007 Notably, these mutations also enhanced viral resistance to the drug cyclosporine A, indicating a reduced dependence of the compensated virus on CypA that is normally essential for optimal infectivity. Cyclosporine 68-82 peptidylprolyl isomerase A Homo sapiens 144-148 17267487-2 2007 The immunosuppressive drug cyclosporine A (CsA) and its nonimmunosuppressive analogs bind with high affinity to CypA and inhibit HIV-1 replication. Cyclosporine 43-46 peptidylprolyl isomerase A Homo sapiens 112-116 17267487-3 2007 Previous studies have identified two mutations, A92E and G94D, in the CypA-binding loop of CA that confer the ability of HIV-1 to replicate in the presence of CsA. Cyclosporine 159-162 peptidylprolyl isomerase A Homo sapiens 70-74 16737676-1 2006 Peptidyl prolyl cis/trans isomerase cyclophilin A (CypA) serves as a cellular receptor for the important immunosuppressant drug, cyclosporin A. Cyclosporine 129-142 peptidylprolyl isomerase A Homo sapiens 36-49 16737676-1 2006 Peptidyl prolyl cis/trans isomerase cyclophilin A (CypA) serves as a cellular receptor for the important immunosuppressant drug, cyclosporin A. Cyclosporine 129-142 peptidylprolyl isomerase A Homo sapiens 51-55 16643975-6 2006 Inhibition of Cyp A function by cyclosporine significantly decreased the efficiency of TRIM5alpha-mediated restriction only when the restricted virus capsid interacted with Cyp A. Cyclosporine 32-44 peptidylprolyl isomerase A Homo sapiens 14-19 15963461-1 2005 Cyclophilins (CyPs) are a widespreading protein family in living organisms and possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase), which is inhibited by cyclosporin A (CsA). Cyclosporine 186-189 peptidylprolyl isomerase A Homo sapiens 0-12 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 150-163 peptidylprolyl isomerase A Homo sapiens 0-13 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 150-163 peptidylprolyl isomerase A Homo sapiens 15-19 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 150-163 peptidylprolyl isomerase A Homo sapiens 36-48 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 165-168 peptidylprolyl isomerase A Homo sapiens 0-13 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 165-168 peptidylprolyl isomerase A Homo sapiens 15-19 16307882-1 2006 Cyclophilin A (CypA) is a member of cyclophilins, a family of the highly homologous peptidyl prolyl cis-trans isomerases (PPIases), which can bind to cyclosporin A (CsA). Cyclosporine 165-168 peptidylprolyl isomerase A Homo sapiens 36-48 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Cyclosporine 170-184 peptidylprolyl isomerase A Homo sapiens 43-47 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Cyclosporine 170-184 peptidylprolyl isomerase A Homo sapiens 155-159 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Cyclosporine 186-189 peptidylprolyl isomerase A Homo sapiens 43-47 16372262-2 2006 CypA is an abundantly expressed cytosolic protein, target of the immunosuppressive drug cyclosporin A (CsA), for which a variety of functions has been described. Cyclosporine 88-101 peptidylprolyl isomerase A Homo sapiens 0-4 16372262-2 2006 CypA is an abundantly expressed cytosolic protein, target of the immunosuppressive drug cyclosporin A (CsA), for which a variety of functions has been described. Cyclosporine 103-106 peptidylprolyl isomerase A Homo sapiens 0-4 16471698-1 2006 The structure of the complex of cyclophilin A (CypA) with cyclosporin A (CsA, 1) shows a cluster of four water molecules buried at the binding interface, which is rearranged when CsA is replaced by (5-hydroxynorvaline)-2-cyclosporin (2). Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 32-45 16471698-1 2006 The structure of the complex of cyclophilin A (CypA) with cyclosporin A (CsA, 1) shows a cluster of four water molecules buried at the binding interface, which is rearranged when CsA is replaced by (5-hydroxynorvaline)-2-cyclosporin (2). Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 47-51 16471698-1 2006 The structure of the complex of cyclophilin A (CypA) with cyclosporin A (CsA, 1) shows a cluster of four water molecules buried at the binding interface, which is rearranged when CsA is replaced by (5-hydroxynorvaline)-2-cyclosporin (2). Cyclosporine 179-182 peptidylprolyl isomerase A Homo sapiens 32-45 16471698-1 2006 The structure of the complex of cyclophilin A (CypA) with cyclosporin A (CsA, 1) shows a cluster of four water molecules buried at the binding interface, which is rearranged when CsA is replaced by (5-hydroxynorvaline)-2-cyclosporin (2). Cyclosporine 179-182 peptidylprolyl isomerase A Homo sapiens 47-51 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Cyclosporine 186-189 peptidylprolyl isomerase A Homo sapiens 155-159 16571786-7 2006 CsA abolished CypA-Vpr binding but had no effect on induction of G2 arrest or Vpr steady-state levels. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 14-18 16199531-2 2005 To address this issue, we sought viruses for CypA independence using Debio-025, a cyclosporine A (CsA) analog that disrupts CypA-capsid interaction. Cyclosporine 98-101 peptidylprolyl isomerase A Homo sapiens 124-128 15963461-5 2005 Superposition of the structure of the C domain of hCyP33 with the structure of CypA suggests that the C domain contains PPIase active site which binds to CsA. Cyclosporine 154-157 peptidylprolyl isomerase A Homo sapiens 79-83 15283571-0 2004 Thermodynamic analysis of cyclosporin a binding to cyclophilin a in a lung tumor tissue lysate. Cyclosporine 26-39 peptidylprolyl isomerase A Homo sapiens 51-64 15706440-1 2005 Cyclophilins are originally identified as cellular binding proteins for the immunosuppressive drug cyclosporin A. Cyclosporine 99-112 peptidylprolyl isomerase A Homo sapiens 0-12 15466660-1 2004 Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A, is a cis-trans-peptidyl-prolyl isomerase (PPIase). Cyclosporine 65-78 peptidylprolyl isomerase A Homo sapiens 0-13 15466660-1 2004 Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A, is a cis-trans-peptidyl-prolyl isomerase (PPIase). Cyclosporine 65-78 peptidylprolyl isomerase A Homo sapiens 15-19 15466660-11 2004 Inhibition of PPIase activity of CypA with cyclosporin A also blocks the inhibitory effect of CypA on GC-c activity. Cyclosporine 43-56 peptidylprolyl isomerase A Homo sapiens 33-37 15466660-11 2004 Inhibition of PPIase activity of CypA with cyclosporin A also blocks the inhibitory effect of CypA on GC-c activity. Cyclosporine 43-56 peptidylprolyl isomerase A Homo sapiens 94-98 15542632-5 2004 Disruption of the CA-CypA interaction, either by the competitive inhibitor cyclosporine (CsA) or by mutation of CA residue G89 or P90, suggested that producer cell CypA was required for full virion infectivity. Cyclosporine 75-87 peptidylprolyl isomerase A Homo sapiens 21-25 15542632-5 2004 Disruption of the CA-CypA interaction, either by the competitive inhibitor cyclosporine (CsA) or by mutation of CA residue G89 or P90, suggested that producer cell CypA was required for full virion infectivity. Cyclosporine 75-87 peptidylprolyl isomerase A Homo sapiens 164-168 15542632-5 2004 Disruption of the CA-CypA interaction, either by the competitive inhibitor cyclosporine (CsA) or by mutation of CA residue G89 or P90, suggested that producer cell CypA was required for full virion infectivity. Cyclosporine 89-92 peptidylprolyl isomerase A Homo sapiens 21-25 15283571-2 2004 A SUPREX-derived binding free energy (i.e. DeltaDeltaG(f) value) and dissociation constant (i.e., K(d) value) were determined for the binding of cyclosporin A (CsA) to a cyclophilin A (CypA) sample in which the protein was a component of a tissue lysate derived from fresh frozen lung tumor. Cyclosporine 145-158 peptidylprolyl isomerase A Homo sapiens 170-183 15283571-2 2004 A SUPREX-derived binding free energy (i.e. DeltaDeltaG(f) value) and dissociation constant (i.e., K(d) value) were determined for the binding of cyclosporin A (CsA) to a cyclophilin A (CypA) sample in which the protein was a component of a tissue lysate derived from fresh frozen lung tumor. Cyclosporine 145-158 peptidylprolyl isomerase A Homo sapiens 185-189 15283571-2 2004 A SUPREX-derived binding free energy (i.e. DeltaDeltaG(f) value) and dissociation constant (i.e., K(d) value) were determined for the binding of cyclosporin A (CsA) to a cyclophilin A (CypA) sample in which the protein was a component of a tissue lysate derived from fresh frozen lung tumor. Cyclosporine 160-163 peptidylprolyl isomerase A Homo sapiens 170-183 15283571-2 2004 A SUPREX-derived binding free energy (i.e. DeltaDeltaG(f) value) and dissociation constant (i.e., K(d) value) were determined for the binding of cyclosporin A (CsA) to a cyclophilin A (CypA) sample in which the protein was a component of a tissue lysate derived from fresh frozen lung tumor. Cyclosporine 160-163 peptidylprolyl isomerase A Homo sapiens 185-189 15283571-3 2004 The DeltaDeltaG(f) and K(d) values determined by SUPREX for CsA binding to CypA in this unpurified protein sample, 4.7 +/- 0.8 kcal/mol and 77 +/- 17 nM, respectively, were comparable to the those obtained when SUPREX was used to analyze the binding of CsA to a highly purified CypA sample, 4.2 +/- 1.0 kcal/mol and 32 +/- 20 nM, respectively. Cyclosporine 60-63 peptidylprolyl isomerase A Homo sapiens 75-79 15283571-3 2004 The DeltaDeltaG(f) and K(d) values determined by SUPREX for CsA binding to CypA in this unpurified protein sample, 4.7 +/- 0.8 kcal/mol and 77 +/- 17 nM, respectively, were comparable to the those obtained when SUPREX was used to analyze the binding of CsA to a highly purified CypA sample, 4.2 +/- 1.0 kcal/mol and 32 +/- 20 nM, respectively. Cyclosporine 60-63 peptidylprolyl isomerase A Homo sapiens 278-282 15283571-3 2004 The DeltaDeltaG(f) and K(d) values determined by SUPREX for CsA binding to CypA in this unpurified protein sample, 4.7 +/- 0.8 kcal/mol and 77 +/- 17 nM, respectively, were comparable to the those obtained when SUPREX was used to analyze the binding of CsA to a highly purified CypA sample, 4.2 +/- 1.0 kcal/mol and 32 +/- 20 nM, respectively. Cyclosporine 253-256 peptidylprolyl isomerase A Homo sapiens 75-79 15283571-4 2004 Moreover, the SUPREX-derived K(d) values determined in this work were both in the range of those previously reported for the CypA-CsA complex. Cyclosporine 130-133 peptidylprolyl isomerase A Homo sapiens 125-129 12881522-5 2003 The CypA inhibitor cyclosporin A and non-immunosuppressive PPIase inhibitors such as NIM811 and sanglifehrin A block expression of Vpr without affecting pre- or post-translational events such as transcription, intracellular transport, or virus incorporation of Vpr. Cyclosporine 19-32 peptidylprolyl isomerase A Homo sapiens 4-8 15130913-1 2004 OBJECTIVE: Cyclophilin A (CyPA) is an abundant intracellular protein that is considered to be the main target of the immunosuppressive drug cyclosporine A. Cyclosporine 140-154 peptidylprolyl isomerase A Homo sapiens 11-24 15130913-1 2004 OBJECTIVE: Cyclophilin A (CyPA) is an abundant intracellular protein that is considered to be the main target of the immunosuppressive drug cyclosporine A. Cyclosporine 140-154 peptidylprolyl isomerase A Homo sapiens 26-30 12871122-6 2003 CsA is cytoprotective in many cellular and animal models, but protection may result from either inhibition of the MPT through an interaction with CYP D or inhibition of calcineurin-mediated dephosphorylation of BAD through an interaction with CYP A. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 243-248 12897779-3 2003 In certain nonhuman primate cells, the CA-CypA interaction is essential for restriction: HIV-1 infectivity is increased >100-fold by cyclosporin A (CsA), a competitive inhibitor of the interaction, or by an HIV-1 CA mutation that disrupts CypA binding. Cyclosporine 136-149 peptidylprolyl isomerase A Homo sapiens 42-46 12897779-3 2003 In certain nonhuman primate cells, the CA-CypA interaction is essential for restriction: HIV-1 infectivity is increased >100-fold by cyclosporin A (CsA), a competitive inhibitor of the interaction, or by an HIV-1 CA mutation that disrupts CypA binding. Cyclosporine 136-149 peptidylprolyl isomerase A Homo sapiens 242-246 12897779-3 2003 In certain nonhuman primate cells, the CA-CypA interaction is essential for restriction: HIV-1 infectivity is increased >100-fold by cyclosporin A (CsA), a competitive inhibitor of the interaction, or by an HIV-1 CA mutation that disrupts CypA binding. Cyclosporine 151-154 peptidylprolyl isomerase A Homo sapiens 42-46 12897779-3 2003 In certain nonhuman primate cells, the CA-CypA interaction is essential for restriction: HIV-1 infectivity is increased >100-fold by cyclosporin A (CsA), a competitive inhibitor of the interaction, or by an HIV-1 CA mutation that disrupts CypA binding. Cyclosporine 151-154 peptidylprolyl isomerase A Homo sapiens 242-246 12885921-5 2003 CypA relocation to viral factories required the synthesis of viral postreplicative proteins, and treatment of infected cells with cyclosporine (CsA) prevented CypA relocation, clearly excluding the virosomes from CypA staining. Cyclosporine 130-142 peptidylprolyl isomerase A Homo sapiens 159-163 12885921-5 2003 CypA relocation to viral factories required the synthesis of viral postreplicative proteins, and treatment of infected cells with cyclosporine (CsA) prevented CypA relocation, clearly excluding the virosomes from CypA staining. Cyclosporine 130-142 peptidylprolyl isomerase A Homo sapiens 159-163 12885921-5 2003 CypA relocation to viral factories required the synthesis of viral postreplicative proteins, and treatment of infected cells with cyclosporine (CsA) prevented CypA relocation, clearly excluding the virosomes from CypA staining. Cyclosporine 144-147 peptidylprolyl isomerase A Homo sapiens 159-163 12885921-5 2003 CypA relocation to viral factories required the synthesis of viral postreplicative proteins, and treatment of infected cells with cyclosporine (CsA) prevented CypA relocation, clearly excluding the virosomes from CypA staining. Cyclosporine 144-147 peptidylprolyl isomerase A Homo sapiens 159-163 12668872-4 2003 In addition, in vitro binding assays demonstrated a direct interaction of CypA with the PRLR, in the presence or absence of cyclosporine. Cyclosporine 124-136 peptidylprolyl isomerase A Homo sapiens 74-78 12634401-3 2003 Our results show that the infectivity of virions depleted of CyPA by treatment with cyclosporine A could be restored by NERT treatment, while mutants in the CyPA binding loop of capsid could only be partially restored. Cyclosporine 84-98 peptidylprolyl isomerase A Homo sapiens 61-65 12207006-0 2002 Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity. Cyclosporine 0-13 peptidylprolyl isomerase A Homo sapiens 140-153 12207006-0 2002 Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity. Cyclosporine 0-13 peptidylprolyl isomerase A Homo sapiens 155-168 12207006-0 2002 Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity. Cyclosporine 193-206 peptidylprolyl isomerase A Homo sapiens 140-153 12207006-0 2002 Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity. Cyclosporine 193-206 peptidylprolyl isomerase A Homo sapiens 155-168 11836403-9 2002 Using this system, we found that Vpr-CypA rescues the infectivity of viruses lacking CypA, either produced in the presence of CsA or mutated in the CypA packaging signal of CA. Cyclosporine 126-129 peptidylprolyl isomerase A Homo sapiens 37-41 12218175-4 2002 The CyPA-CsA complex binds to a composite surface formed by the catalytic and regulatory subunits of CN, where the complex of FK506 and its binding protein FKBP also binds. Cyclosporine 9-12 peptidylprolyl isomerase A Homo sapiens 4-8 11943775-1 2002 Cyclophilin A (CyPA), a ubiquitously distributed intracellular protein, is a peptidylprolyl cis-trans-isomerase and the major target of the potent immunosuppressive drug cyclosporin A. Cyclosporine 170-183 peptidylprolyl isomerase A Homo sapiens 15-19 12009870-8 2002 Furthermore, Cyp A incorporation was inhibited by cyclosporin in all cases. Cyclosporine 50-61 peptidylprolyl isomerase A Homo sapiens 13-18 11836403-4 2002 Preventing CypA incorporation, either by mutations in the binding region of CA or by the presence of CsA, abrogates virus infectivity. Cyclosporine 101-104 peptidylprolyl isomerase A Homo sapiens 11-15 12181673-8 2002 Pre-treatment of the HIV-1 inocula with CsA, blocking the function of virus-associated CypA, did not inhibit the ensuing yield of infection. Cyclosporine 40-43 peptidylprolyl isomerase A Homo sapiens 87-91 11943775-1 2002 Cyclophilin A (CyPA), a ubiquitously distributed intracellular protein, is a peptidylprolyl cis-trans-isomerase and the major target of the potent immunosuppressive drug cyclosporin A. Cyclosporine 170-183 peptidylprolyl isomerase A Homo sapiens 0-13 9705263-5 1998 In single-cycle infection assays, nef-defective virions were partially resistant to cyclosporin A (CsA), a drug that inhibits the binding of CyPA to the HIV-1 Gag precursor and CyPA incorporation into virions. Cyclosporine 84-97 peptidylprolyl isomerase A Homo sapiens 177-181 12210730-6 2002 These results are further evidenced by the effect of RB on both calcineurin (CN) and NFAT binding activity in vitro, suggesting that the interaction of RB with CypA interferes with the CsA:CypA complex and blocks CsA-inhibited CN activity. Cyclosporine 185-188 peptidylprolyl isomerase A Homo sapiens 160-164 12210730-6 2002 These results are further evidenced by the effect of RB on both calcineurin (CN) and NFAT binding activity in vitro, suggesting that the interaction of RB with CypA interferes with the CsA:CypA complex and blocks CsA-inhibited CN activity. Cyclosporine 185-188 peptidylprolyl isomerase A Homo sapiens 189-193 11390463-3 2001 SFA interacts with high affinity with the CsA binding side of CypA and inhibits its peptidyl-prolyl isomerase activity. Cyclosporine 42-45 peptidylprolyl isomerase A Homo sapiens 62-66 11206060-3 2000 In vitro, the CyPB/CsA complex is more effective in inhibiting calcineurin than the CyPA/CsA and CyPC/CsA complexes, pointing to fine structural differences in the calcineurin-binding region. Cyclosporine 89-92 peptidylprolyl isomerase A Homo sapiens 84-88 11206060-3 2000 In vitro, the CyPB/CsA complex is more effective in inhibiting calcineurin than the CyPA/CsA and CyPC/CsA complexes, pointing to fine structural differences in the calcineurin-binding region. Cyclosporine 89-92 peptidylprolyl isomerase A Homo sapiens 84-88 10208939-5 1999 Both cyclosporin treatment and alteration of Gly89 or Pro90 in the CypA-binding site of CA caused a 5- to 20-fold decrease in CypA incorporation. Cyclosporine 5-16 peptidylprolyl isomerase A Homo sapiens 67-71 10208939-5 1999 Both cyclosporin treatment and alteration of Gly89 or Pro90 in the CypA-binding site of CA caused a 5- to 20-fold decrease in CypA incorporation. Cyclosporine 5-16 peptidylprolyl isomerase A Homo sapiens 126-130 9705263-5 1998 In single-cycle infection assays, nef-defective virions were partially resistant to cyclosporin A (CsA), a drug that inhibits the binding of CyPA to the HIV-1 Gag precursor and CyPA incorporation into virions. Cyclosporine 84-97 peptidylprolyl isomerase A Homo sapiens 141-145 9705263-5 1998 In single-cycle infection assays, nef-defective virions were partially resistant to cyclosporin A (CsA), a drug that inhibits the binding of CyPA to the HIV-1 Gag precursor and CyPA incorporation into virions. Cyclosporine 99-102 peptidylprolyl isomerase A Homo sapiens 141-145 9705263-5 1998 In single-cycle infection assays, nef-defective virions were partially resistant to cyclosporin A (CsA), a drug that inhibits the binding of CyPA to the HIV-1 Gag precursor and CyPA incorporation into virions. Cyclosporine 99-102 peptidylprolyl isomerase A Homo sapiens 177-181 9705263-8 1998 Surprisingly, CyPA-deficient virions remained sensitive to inhibition by CsA, in a manner that depended strongly on the presence of a functional nef gene. Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 14-18 9705263-10 1998 They further suggest that in addition to blocking the CyPA-Gag interaction, CsA can also inhibit HIV-1 replication through a novel mechanism involving suppression of Nef-directed enhancement of virus infectivity. Cyclosporine 76-79 peptidylprolyl isomerase A Homo sapiens 54-58 9675023-1 1998 The calcium- and calmodulin-activated protein phosphatase calcineurin (CN) is the target for the immunosuppressive drugs FK506 and cyclosporin A (CsA) when bound to their intracellular receptor proteins, the immunophilins known as FK506-binding protein (FKBP) and cyclophilin A (CypA), respectively. Cyclosporine 131-144 peptidylprolyl isomerase A Homo sapiens 264-277 9675023-1 1998 The calcium- and calmodulin-activated protein phosphatase calcineurin (CN) is the target for the immunosuppressive drugs FK506 and cyclosporin A (CsA) when bound to their intracellular receptor proteins, the immunophilins known as FK506-binding protein (FKBP) and cyclophilin A (CypA), respectively. Cyclosporine 131-144 peptidylprolyl isomerase A Homo sapiens 279-283 9675023-1 1998 The calcium- and calmodulin-activated protein phosphatase calcineurin (CN) is the target for the immunosuppressive drugs FK506 and cyclosporin A (CsA) when bound to their intracellular receptor proteins, the immunophilins known as FK506-binding protein (FKBP) and cyclophilin A (CypA), respectively. Cyclosporine 146-149 peptidylprolyl isomerase A Homo sapiens 264-277 9675023-1 1998 The calcium- and calmodulin-activated protein phosphatase calcineurin (CN) is the target for the immunosuppressive drugs FK506 and cyclosporin A (CsA) when bound to their intracellular receptor proteins, the immunophilins known as FK506-binding protein (FKBP) and cyclophilin A (CypA), respectively. Cyclosporine 146-149 peptidylprolyl isomerase A Homo sapiens 279-283 9675023-10 1998 Inhibition of CN by the CsA x CypA complex was not time-dependent, but the data did conform to a competitive inhibition model like FK506 x FKBP. Cyclosporine 24-27 peptidylprolyl isomerase A Homo sapiens 30-34 9299338-6 1997 15N spin relaxation times and NMR lineshape analyses for CypA in the free form and complexed with cyclosporin A (CsA) revealed transitions of polypeptide loops surrounding the ligand-binding site from locally flexible conformations in the free protein, some of which include well-defined conformational equilibria, to well-defined spatial arrangements in the CypA-CsA complex. Cyclosporine 98-111 peptidylprolyl isomerase A Homo sapiens 57-61 9636359-3 1998 We studied chaperone effects on Gag precursor processing using cyclosporin A (CsA) to bind CypA and prevent its interaction with p55Gag. Cyclosporine 78-81 peptidylprolyl isomerase A Homo sapiens 91-95 9636359-7 1998 CsA has a direct effect on HIV-1 Gag processing that implicates CypA as having an important role in the maturation of HIV-1 particles. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 64-68 9380739-1 1997 HIV-1 specifically incorporates the peptidyl prolyl isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA). Cyclosporine 148-151 peptidylprolyl isomerase A Homo sapiens 62-75 9380739-1 1997 HIV-1 specifically incorporates the peptidyl prolyl isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA). Cyclosporine 148-151 peptidylprolyl isomerase A Homo sapiens 77-81 9380739-2 1997 HIV-1 replication is inhibited by CsA as well as by nonimmunosuppressive CsA analogues that bind to CyPA and interfere with its virion association. Cyclosporine 73-76 peptidylprolyl isomerase A Homo sapiens 100-104 9380739-5 1997 We report here that the transfer of HIV-1 CA residues 86-93, which form part of an exposed loop, to the corresponding position in SIVmac resulted in the efficient incorporation of CyPA and conferred an HIV-1-like sensitivity to a nonimmunosuppressive cyclosporin. Cyclosporine 251-262 peptidylprolyl isomerase A Homo sapiens 180-184 9380739-9 1997 By demonstrating that CyPA-binding-site residues can induce cyclosporin sensitivity in a heterologous context, this study provides direct in vivo evidence that the exposed loop between helices IV and V of HIV-1 CA not merely constitutes a docking site for CyPA but is a functional target of this cellular protein. Cyclosporine 60-71 peptidylprolyl isomerase A Homo sapiens 22-26 9380739-9 1997 By demonstrating that CyPA-binding-site residues can induce cyclosporin sensitivity in a heterologous context, this study provides direct in vivo evidence that the exposed loop between helices IV and V of HIV-1 CA not merely constitutes a docking site for CyPA but is a functional target of this cellular protein. Cyclosporine 60-71 peptidylprolyl isomerase A Homo sapiens 256-260 9299338-6 1997 15N spin relaxation times and NMR lineshape analyses for CypA in the free form and complexed with cyclosporin A (CsA) revealed transitions of polypeptide loops surrounding the ligand-binding site from locally flexible conformations in the free protein, some of which include well-defined conformational equilibria, to well-defined spatial arrangements in the CypA-CsA complex. Cyclosporine 98-111 peptidylprolyl isomerase A Homo sapiens 359-363 9299338-6 1997 15N spin relaxation times and NMR lineshape analyses for CypA in the free form and complexed with cyclosporin A (CsA) revealed transitions of polypeptide loops surrounding the ligand-binding site from locally flexible conformations in the free protein, some of which include well-defined conformational equilibria, to well-defined spatial arrangements in the CypA-CsA complex. Cyclosporine 113-116 peptidylprolyl isomerase A Homo sapiens 57-61 9299338-6 1997 15N spin relaxation times and NMR lineshape analyses for CypA in the free form and complexed with cyclosporin A (CsA) revealed transitions of polypeptide loops surrounding the ligand-binding site from locally flexible conformations in the free protein, some of which include well-defined conformational equilibria, to well-defined spatial arrangements in the CypA-CsA complex. Cyclosporine 113-116 peptidylprolyl isomerase A Homo sapiens 359-363 9299338-7 1997 Compared to the crystal structure of free CypA, where the ligand-binding area is extensively involved in lattice contacts, the NMR structure presents a highly relevant reference for studies of changes in structure and internal mobility of the binding pocket upon ligand binding, and possible consequences of this conformational variability for calcineurin recognition by the CypA-CsA complex. Cyclosporine 380-383 peptidylprolyl isomerase A Homo sapiens 42-46 9261445-1 1997 Human immunodeficiency virus type 1 (HIV-1) incorporates the cellular peptidyl-prolyl cis-trans isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA). Cyclosporine 177-190 peptidylprolyl isomerase A Homo sapiens 121-125 9305737-4 1997 While the interconversion rate is too slow to measure by kinetic NMR methods in the absence of CyPA, these methods, saturation transfer and NOE experiments, established that CyPA enhanced the rate of trans-cis interconversion, a process inhibited by cyclosporin A (CsA). Cyclosporine 250-263 peptidylprolyl isomerase A Homo sapiens 174-178 9305737-4 1997 While the interconversion rate is too slow to measure by kinetic NMR methods in the absence of CyPA, these methods, saturation transfer and NOE experiments, established that CyPA enhanced the rate of trans-cis interconversion, a process inhibited by cyclosporin A (CsA). Cyclosporine 265-268 peptidylprolyl isomerase A Homo sapiens 174-178 9261445-1 1997 Human immunodeficiency virus type 1 (HIV-1) incorporates the cellular peptidyl-prolyl cis-trans isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA). Cyclosporine 192-195 peptidylprolyl isomerase A Homo sapiens 121-125 9261445-2 1997 CsA inhibits the incorporation of CyPA and reduces HIV-1 virion infectivity but is inactive against closely related primate lentiviruses that do not interact with CyPA. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 34-38 9261445-4 1997 CsA, which disrupts the interaction with CA, binds at the active site of CyPA. Cyclosporine 0-3 peptidylprolyl isomerase A Homo sapiens 73-77 9261445-8 1997 One CyPA mutant with a substantially decreased sensitivity to CsA was incorporated with wild-type efficiency, demonstrating that the requirements for binding to CsA and to HIV-1 CA are not identical. Cyclosporine 62-65 peptidylprolyl isomerase A Homo sapiens 4-8 9261445-8 1997 One CyPA mutant with a substantially decreased sensitivity to CsA was incorporated with wild-type efficiency, demonstrating that the requirements for binding to CsA and to HIV-1 CA are not identical. Cyclosporine 161-164 peptidylprolyl isomerase A Homo sapiens 4-8 9032343-7 1997 These studies indicate that, as with other proline-containing peptides or cyclosporine A, HIV-1 Gag directly contacts residues in the hydrophobic pocket of CyPA. Cyclosporine 74-88 peptidylprolyl isomerase A Homo sapiens 156-160 9016720-1 1997 BACKGROUND: Cyclophilin A (CyPA), a receptor of the immunosuppressive drug cyclosporin A, catalyzes the cis-trans isomerization of peptidyl-prolyl bonds and is required for the infectious activity of human immunodeficiency virus type 1 (HIV-1). Cyclosporine 75-88 peptidylprolyl isomerase A Homo sapiens 27-31 8513493-3 1993 Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. Cyclosporine 0-13 peptidylprolyl isomerase A Homo sapiens 43-47 9043670-3 1997 These are devoid of immunosuppressive activity in vitro but they have binding affinity for cyclophilin A (CypA) similar to that of CsA and thus represent a new class of cyclosporin antagonists. Cyclosporine 169-180 peptidylprolyl isomerase A Homo sapiens 91-104 9043670-3 1997 These are devoid of immunosuppressive activity in vitro but they have binding affinity for cyclophilin A (CypA) similar to that of CsA and thus represent a new class of cyclosporin antagonists. Cyclosporine 169-180 peptidylprolyl isomerase A Homo sapiens 106-110 9043670-5 1997 A comparison of this NMR data with X-ray crystallographic analysis of a CypA/CsA derivative complex demonstrates that the solution structure does not correspond to the bioactive conformation. Cyclosporine 77-80 peptidylprolyl isomerase A Homo sapiens 72-76 7650689-1 1995 Analysis of the contact surface of the cyclophilin A (CypA)/cyclosporin A (CsA, 1) crystal structure delineates a unique cavity between both molecules in the vicinity of the Abu-2 side chain atoms of 1 (Abu pocket). Cyclosporine 60-73 peptidylprolyl isomerase A Homo sapiens 39-52 7650689-1 1995 Analysis of the contact surface of the cyclophilin A (CypA)/cyclosporin A (CsA, 1) crystal structure delineates a unique cavity between both molecules in the vicinity of the Abu-2 side chain atoms of 1 (Abu pocket). Cyclosporine 60-73 peptidylprolyl isomerase A Homo sapiens 54-58 7650689-1 1995 Analysis of the contact surface of the cyclophilin A (CypA)/cyclosporin A (CsA, 1) crystal structure delineates a unique cavity between both molecules in the vicinity of the Abu-2 side chain atoms of 1 (Abu pocket). Cyclosporine 75-78 peptidylprolyl isomerase A Homo sapiens 39-52 7650689-1 1995 Analysis of the contact surface of the cyclophilin A (CypA)/cyclosporin A (CsA, 1) crystal structure delineates a unique cavity between both molecules in the vicinity of the Abu-2 side chain atoms of 1 (Abu pocket). Cyclosporine 75-78 peptidylprolyl isomerase A Homo sapiens 54-58 7590732-0 1995 Cyclophilin A, the major intracellular receptor for the immunosuppressant cyclosporin A, maps to chromosome 7p11.2-p13: four pseudogenes map to chromosomes 3, 10, 14, and 18. Cyclosporine 74-87 peptidylprolyl isomerase A Homo sapiens 0-13 7590732-1 1995 Cyclophilin A (CyP-A), the major intracellular receptor for the immunosuppressant cyclosporin A (CsA), is a member of the immunophilin class of proteins, which all possess peptidyl-prolyl cis-trans isomerase activity and, therefore, are believed to be involved in protein folding and/or intracellular protein transport. Cyclosporine 82-95 peptidylprolyl isomerase A Homo sapiens 0-13 7590732-1 1995 Cyclophilin A (CyP-A), the major intracellular receptor for the immunosuppressant cyclosporin A (CsA), is a member of the immunophilin class of proteins, which all possess peptidyl-prolyl cis-trans isomerase activity and, therefore, are believed to be involved in protein folding and/or intracellular protein transport. Cyclosporine 82-95 peptidylprolyl isomerase A Homo sapiens 15-20 7590732-1 1995 Cyclophilin A (CyP-A), the major intracellular receptor for the immunosuppressant cyclosporin A (CsA), is a member of the immunophilin class of proteins, which all possess peptidyl-prolyl cis-trans isomerase activity and, therefore, are believed to be involved in protein folding and/or intracellular protein transport. Cyclosporine 97-100 peptidylprolyl isomerase A Homo sapiens 0-13 7590732-1 1995 Cyclophilin A (CyP-A), the major intracellular receptor for the immunosuppressant cyclosporin A (CsA), is a member of the immunophilin class of proteins, which all possess peptidyl-prolyl cis-trans isomerase activity and, therefore, are believed to be involved in protein folding and/or intracellular protein transport. Cyclosporine 97-100 peptidylprolyl isomerase A Homo sapiens 15-20 7541038-4 1995 Cyclosporin A and FK506 efficiently disrupt the YY1-CyPA and YY1-FKBP12 interactions. Cyclosporine 0-13 peptidylprolyl isomerase A Homo sapiens 52-56 7829860-1 1995 Cyclophilins A and B (CyPA and CyPB) are known to be the main binding proteins for cyclosporin A (CsA), a potent immunosuppressive drug. Cyclosporine 83-96 peptidylprolyl isomerase A Homo sapiens 22-26 7829860-1 1995 Cyclophilins A and B (CyPA and CyPB) are known to be the main binding proteins for cyclosporin A (CsA), a potent immunosuppressive drug. Cyclosporine 98-101 peptidylprolyl isomerase A Homo sapiens 22-26 8031755-11 1994 However, Cyp-C tolerates a greater variety of structures on Cs at position 2 than Cyp-A does, suggesting that this residue of CsA might not be in tight contact with Cyp-C. Cyclosporine 126-129 peptidylprolyl isomerase A Homo sapiens 82-87 15299416-0 1994 Crystallization of the complex between cyclophilin A and cyclosporin derivatives: the use of cross-seeding. Cyclosporine 57-68 peptidylprolyl isomerase A Homo sapiens 39-52 15299416-7 1994 In this crystal form, CsA has no packing interactions with neighbouring molecules and these crystals could be used to cross-seed other CypA/CsA analog complexes. Cyclosporine 22-25 peptidylprolyl isomerase A Homo sapiens 135-139 15299416-7 1994 In this crystal form, CsA has no packing interactions with neighbouring molecules and these crystals could be used to cross-seed other CypA/CsA analog complexes. Cyclosporine 140-143 peptidylprolyl isomerase A Homo sapiens 135-139 15299416-8 1994 Nine different CypA/ CsA analog complexes could be crystallized using this technique, most of them yielding highly diffracting crystals, quickly solvable by Fourier difference methods. Cyclosporine 21-24 peptidylprolyl isomerase A Homo sapiens 15-19 8518284-6 1993 Sequence alignment with human T-cell cyclophilin based on secondary structure homology implicates several residues in E. coli cyclophilin that may be crucial for binding the peptide substrate AC-A-A-P-A-AMC and the immunosuppressive drug cyclosporin A. Cyclosporine 238-251 peptidylprolyl isomerase A Homo sapiens 30-48 8601841-8 1996 The refined model also shows that steric hindrance to attachment of cyclosporin A (CsA) prevents E. coli CyPA forming a complex with CsA. Cyclosporine 68-81 peptidylprolyl isomerase A Homo sapiens 105-109 8601841-8 1996 The refined model also shows that steric hindrance to attachment of cyclosporin A (CsA) prevents E. coli CyPA forming a complex with CsA. Cyclosporine 83-86 peptidylprolyl isomerase A Homo sapiens 105-109 8601841-8 1996 The refined model also shows that steric hindrance to attachment of cyclosporin A (CsA) prevents E. coli CyPA forming a complex with CsA. Cyclosporine 133-136 peptidylprolyl isomerase A Homo sapiens 105-109 8601841-9 1996 Thus, the extra amino acid residue of E. coli CyPA, polar Gln89, lies along the pathway to the hydrophobic pocket of CyPA and seems to prevent the access hydrophobic part of CsA to the cleft of CyPA. Cyclosporine 174-177 peptidylprolyl isomerase A Homo sapiens 46-50 8601841-9 1996 Thus, the extra amino acid residue of E. coli CyPA, polar Gln89, lies along the pathway to the hydrophobic pocket of CyPA and seems to prevent the access hydrophobic part of CsA to the cleft of CyPA. Cyclosporine 174-177 peptidylprolyl isomerase A Homo sapiens 117-121 8601841-9 1996 Thus, the extra amino acid residue of E. coli CyPA, polar Gln89, lies along the pathway to the hydrophobic pocket of CyPA and seems to prevent the access hydrophobic part of CsA to the cleft of CyPA. Cyclosporine 174-177 peptidylprolyl isomerase A Homo sapiens 117-121 7529414-4 1995 They interrupt the cytoplasmic portion of T-cell signaling by forming a complex with a binding protein--FKBP12 in the case of FK506 and rapamycin and cyclophilin A (CyPA) in the case of cyclosporin A (CsA). Cyclosporine 186-199 peptidylprolyl isomerase A Homo sapiens 150-163 7529414-4 1995 They interrupt the cytoplasmic portion of T-cell signaling by forming a complex with a binding protein--FKBP12 in the case of FK506 and rapamycin and cyclophilin A (CyPA) in the case of cyclosporin A (CsA). Cyclosporine 186-199 peptidylprolyl isomerase A Homo sapiens 165-169 7529414-4 1995 They interrupt the cytoplasmic portion of T-cell signaling by forming a complex with a binding protein--FKBP12 in the case of FK506 and rapamycin and cyclophilin A (CyPA) in the case of cyclosporin A (CsA). Cyclosporine 201-204 peptidylprolyl isomerase A Homo sapiens 150-163 7529414-4 1995 They interrupt the cytoplasmic portion of T-cell signaling by forming a complex with a binding protein--FKBP12 in the case of FK506 and rapamycin and cyclophilin A (CyPA) in the case of cyclosporin A (CsA). Cyclosporine 201-204 peptidylprolyl isomerase A Homo sapiens 165-169 8031755-7 1994 The binding of recombinant human Cyp-A, -B, and -C to cyclosporin A (CsA) was studied by immunochemical methods. Cyclosporine 54-67 peptidylprolyl isomerase A Homo sapiens 33-38 8031755-7 1994 The binding of recombinant human Cyp-A, -B, and -C to cyclosporin A (CsA) was studied by immunochemical methods. Cyclosporine 69-72 peptidylprolyl isomerase A Homo sapiens 33-38 8197205-3 1994 The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. Cyclosporine 4-7 peptidylprolyl isomerase A Homo sapiens 60-64 8197205-3 1994 The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. Cyclosporine 4-7 peptidylprolyl isomerase A Homo sapiens 161-165 8197205-3 1994 The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. Cyclosporine 69-80 peptidylprolyl isomerase A Homo sapiens 161-165 8075981-0 1994 Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A. Cyclosporine 51-64 peptidylprolyl isomerase A Homo sapiens 22-35 8335079-3 1993 Cyclosporin A (CsA) exerts immunosuppressive activities by binding to immunoregulatory proteins termed cyclophilins. Cyclosporine 15-18 peptidylprolyl isomerase A Homo sapiens 103-115 1338979-7 1992 Although CsA is a competitive inhibitor of PPIase activity, it can complex with enzymatically inactive cyclophilins and inhibit the phosphatase activity of calcineurin. Cyclosporine 9-12 peptidylprolyl isomerase A Homo sapiens 103-115 1453463-9 1992 In addition, CyP A is a closed beta-barrel so that neither the immunosuppressive drug cyclosporin A (CsA) nor the proline-containing substrate can bind to the hydrophobic core of the CyP A barrel, while the hydrophobic core of most other barrels is open for ligation. Cyclosporine 86-99 peptidylprolyl isomerase A Homo sapiens 13-18 1453463-9 1992 In addition, CyP A is a closed beta-barrel so that neither the immunosuppressive drug cyclosporin A (CsA) nor the proline-containing substrate can bind to the hydrophobic core of the CyP A barrel, while the hydrophobic core of most other barrels is open for ligation. Cyclosporine 101-104 peptidylprolyl isomerase A Homo sapiens 13-18 8421501-1 1993 Human cyclophilin A (CypA), a ubiquitous intracellular protein of 165 amino acids, is the major receptor for the cyclic undecapeptide immunosuppressant drug cyclosporin A (CsA), which prevents allograft rejection after transplant surgery and is efficacious in the field of autoimmune diseases. Cyclosporine 172-175 peptidylprolyl isomerase A Homo sapiens 6-19 8421501-1 1993 Human cyclophilin A (CypA), a ubiquitous intracellular protein of 165 amino acids, is the major receptor for the cyclic undecapeptide immunosuppressant drug cyclosporin A (CsA), which prevents allograft rejection after transplant surgery and is efficacious in the field of autoimmune diseases. Cyclosporine 172-175 peptidylprolyl isomerase A Homo sapiens 21-25 8421501-7 1993 Here we describe the crystal structure of a decameric CypA-CsA complex. Cyclosporine 59-62 peptidylprolyl isomerase A Homo sapiens 54-58 34096287-5 2021 CsO exhibited a higher plasma concentration than CsA, which resulted from minimal CypA binding and lower accumulation in red blood cells and moderate oral bioavailability (F = 12%). Cyclosporine 49-52 peptidylprolyl isomerase A Homo sapiens 82-86 34852234-6 2021 Moreover, targeting CypA by cyclosporine A exhibits promising efficacy against chemoresistant CRC when combined with chemotherapeutics. Cyclosporine 28-42 peptidylprolyl isomerase A Homo sapiens 20-24 34533641-8 2021 Treatment with cyclosporin A, used in vitro for the inhibition of CypA, resulted in a 3-log reduction in CHPV titer and an undetectable level of CypA in comparison to an untreated control. Cyclosporine 15-28 peptidylprolyl isomerase A Homo sapiens 66-70 34533641-8 2021 Treatment with cyclosporin A, used in vitro for the inhibition of CypA, resulted in a 3-log reduction in CHPV titer and an undetectable level of CypA in comparison to an untreated control. Cyclosporine 15-28 peptidylprolyl isomerase A Homo sapiens 145-149 33804393-9 2021 Moreover, in silico docking analysis revealed that the structure of compound 9 was a good fit for the cyclosporin A binding cavity of CypA. Cyclosporine 102-115 peptidylprolyl isomerase A Homo sapiens 134-138 35218062-9 2022 In addition, we found that the cyclosporine A-mediated inhibition of CypA did not prevent the formation of the CypA and AIF complex; rather, this only suppressed genomic DNA fragmentation. Cyclosporine 31-45 peptidylprolyl isomerase A Homo sapiens 69-73