PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 G Homo sapiens 0-3 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 G Homo sapiens 0-3 17609268-7 2007 Like TRIMCyp, Fv1-Cyp restricts HIV-1 and FIV and is sensitive to inhibition by cyclosporine. Cyclosporine 80-92 peptidylprolyl isomerase G Homo sapiens 9-12 20451281-1 2010 BACKGROUND & AIMS: The cyclophilin (Cyp) inhibitors - cyclosporine A (CsA), NIM811, Debio 025, and SCY 635 - block HCV replication both in vitro and in vivo, and represent a novel class of potent anti-HCV agents. Cyclosporine 58-72 peptidylprolyl isomerase G Homo sapiens 27-38 20451281-1 2010 BACKGROUND & AIMS: The cyclophilin (Cyp) inhibitors - cyclosporine A (CsA), NIM811, Debio 025, and SCY 635 - block HCV replication both in vitro and in vivo, and represent a novel class of potent anti-HCV agents. Cyclosporine 58-72 peptidylprolyl isomerase G Homo sapiens 40-43 19659609-1 2009 We have so far reported that an immunosuppressant cyclosporin A (CsA), a well-known cyclophilin (CyP) inhibitor (CPI), strongly suppressed hepatitis C virus (HCV) replication in cell culture, and that CyPB was a cellular cofactor for viral replication. Cyclosporine 50-63 peptidylprolyl isomerase G Homo sapiens 84-95 19659609-1 2009 We have so far reported that an immunosuppressant cyclosporin A (CsA), a well-known cyclophilin (CyP) inhibitor (CPI), strongly suppressed hepatitis C virus (HCV) replication in cell culture, and that CyPB was a cellular cofactor for viral replication. Cyclosporine 50-63 peptidylprolyl isomerase G Homo sapiens 97-100 19659609-1 2009 We have so far reported that an immunosuppressant cyclosporin A (CsA), a well-known cyclophilin (CyP) inhibitor (CPI), strongly suppressed hepatitis C virus (HCV) replication in cell culture, and that CyPB was a cellular cofactor for viral replication. Cyclosporine 65-68 peptidylprolyl isomerase G Homo sapiens 84-95 19659609-1 2009 We have so far reported that an immunosuppressant cyclosporin A (CsA), a well-known cyclophilin (CyP) inhibitor (CPI), strongly suppressed hepatitis C virus (HCV) replication in cell culture, and that CyPB was a cellular cofactor for viral replication. Cyclosporine 65-68 peptidylprolyl isomerase G Homo sapiens 97-100 19659609-6 2009 Knockdown of individual CyP subtypes revealed CyP40, in addition to CyPA and CyPB, contributed to viral replication, and CsA-resistant replicons acquired independence from CyPA for efficient replication. Cyclosporine 121-124 peptidylprolyl isomerase G Homo sapiens 24-27 19503092-7 2009 The Cyp inhibitor cyclosporine A (CsA) caused similar effects. Cyclosporine 18-32 peptidylprolyl isomerase G Homo sapiens 4-7 19503092-7 2009 The Cyp inhibitor cyclosporine A (CsA) caused similar effects. Cyclosporine 34-37 peptidylprolyl isomerase G Homo sapiens 4-7 17707777-8 2007 Most of the single substitution mutations also decreased Cyp-CsA inhibition. Cyclosporine 61-64 peptidylprolyl isomerase G Homo sapiens 57-60 19499554-1 2009 Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction. Cyclosporine 130-143 peptidylprolyl isomerase G Homo sapiens 89-102 18095667-2 2008 Its immunosuppressive activity is due to the formation of a complex with cyclophilin A (Cyp), in which the cis 9MeLeu-10MeLeu amide bond of CsA assumes a trans conformation. Cyclosporine 140-143 peptidylprolyl isomerase G Homo sapiens 73-86 18095667-2 2008 Its immunosuppressive activity is due to the formation of a complex with cyclophilin A (Cyp), in which the cis 9MeLeu-10MeLeu amide bond of CsA assumes a trans conformation. Cyclosporine 140-143 peptidylprolyl isomerase G Homo sapiens 88-91 18095667-3 2008 The mechanism of the conformational inversion has not been delineated, but it has been postulated that metal ions binding induces a conformational change that enables CsA to bind Cyp. Cyclosporine 167-170 peptidylprolyl isomerase G Homo sapiens 179-182 17609268-10 2007 This notion is supported by the observation that infectivity of Fv1-Cyp restricted virus can be rescued by cyclosporine for several hours after infection, whereas virus restricted by TRIMCyp is terminally restricted after around 40 min. Cyclosporine 107-119 peptidylprolyl isomerase G Homo sapiens 68-71 12357034-4 2002 We report the crystal structure of a Cyp/CsA/Cn ternary complex, determined to a resolution of 3.1 A. Residues 3-9 of CsA, particularly N-methyl leucines 4 and 6, and Trp-121 of Cyp form a composite surface for interaction with Cn. Cyclosporine 41-44 peptidylprolyl isomerase G Homo sapiens 37-40 16354247-9 2005 CONCLUSIONS: Determination of the levels of leukocyte CyP mRNA may be of assistance in cyclosporine A therapy. Cyclosporine 87-101 peptidylprolyl isomerase G Homo sapiens 54-57 16299069-4 2006 In the complex with its target (Cyp), CsA adopts a conformation with all trans peptide bonds and this feature is very important for its pharmacological action. Cyclosporine 38-41 peptidylprolyl isomerase G Homo sapiens 32-35 15832403-2 2005 We synthesized a series of electrophilic cyclosporin (CsA) derivatives by varying electrophiles and linker lengths, prepared a series of nucleophilic cysteine mutations on the surface of cyclophilin A (Cyp), and examined their reactivity and specificity in proximity-accelerated reactions. Cyclosporine 54-57 peptidylprolyl isomerase G Homo sapiens 187-200 15353287-1 2004 Cyclophilin (CyP) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA). Cyclosporine 68-81 peptidylprolyl isomerase G Homo sapiens 0-11 15353287-1 2004 Cyclophilin (CyP) is a cytosolic receptor of immunosuppressive drug cyclosporin A (CsA). Cyclosporine 68-81 peptidylprolyl isomerase G Homo sapiens 13-16 12357034-4 2002 We report the crystal structure of a Cyp/CsA/Cn ternary complex, determined to a resolution of 3.1 A. Residues 3-9 of CsA, particularly N-methyl leucines 4 and 6, and Trp-121 of Cyp form a composite surface for interaction with Cn. Cyclosporine 41-44 peptidylprolyl isomerase G Homo sapiens 178-181 12357034-4 2002 We report the crystal structure of a Cyp/CsA/Cn ternary complex, determined to a resolution of 3.1 A. Residues 3-9 of CsA, particularly N-methyl leucines 4 and 6, and Trp-121 of Cyp form a composite surface for interaction with Cn. Cyclosporine 118-121 peptidylprolyl isomerase G Homo sapiens 37-40 11694517-1 2002 The immunosuppressive agents cyclosporin A (CsA) and tacrolimus (FK506) bind to unrelated intracellular immunophilin receptors, cyclophilin (CyP) and FK506-binding protein (FKBP), respectively. Cyclosporine 29-42 peptidylprolyl isomerase G Homo sapiens 128-139 11694517-1 2002 The immunosuppressive agents cyclosporin A (CsA) and tacrolimus (FK506) bind to unrelated intracellular immunophilin receptors, cyclophilin (CyP) and FK506-binding protein (FKBP), respectively. Cyclosporine 29-42 peptidylprolyl isomerase G Homo sapiens 141-144 11694517-1 2002 The immunosuppressive agents cyclosporin A (CsA) and tacrolimus (FK506) bind to unrelated intracellular immunophilin receptors, cyclophilin (CyP) and FK506-binding protein (FKBP), respectively. Cyclosporine 44-47 peptidylprolyl isomerase G Homo sapiens 128-139 11694517-1 2002 The immunosuppressive agents cyclosporin A (CsA) and tacrolimus (FK506) bind to unrelated intracellular immunophilin receptors, cyclophilin (CyP) and FK506-binding protein (FKBP), respectively. Cyclosporine 44-47 peptidylprolyl isomerase G Homo sapiens 141-144 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 129-142 peptidylprolyl isomerase G Homo sapiens 79-90 10966874-4 2000 It is a cyclosporin A (CsA) sensitive CyP with a MW of 19.4kDa. Cyclosporine 8-21 peptidylprolyl isomerase G Homo sapiens 38-41 10966874-4 2000 It is a cyclosporin A (CsA) sensitive CyP with a MW of 19.4kDa. Cyclosporine 23-26 peptidylprolyl isomerase G Homo sapiens 38-41 10966874-5 2000 The PPIase activity and CsA sensitivity of this CyP is higher at higher salt concentration in the medium. Cyclosporine 24-27 peptidylprolyl isomerase G Homo sapiens 48-51 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 129-142 peptidylprolyl isomerase G Homo sapiens 92-95 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 144-147 peptidylprolyl isomerase G Homo sapiens 79-90 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 144-147 peptidylprolyl isomerase G Homo sapiens 92-95 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 174-177 peptidylprolyl isomerase G Homo sapiens 79-90 10486755-1 1999 The affinity capillary electrophoretic separation of the complex of the enzyme cyclophilin (Cyp) with the immunosuppressive drug cyclosporin A (CsA) from uncomplexed Cyp and CsA in phosphate buffer (pH 8) under non-denaturing conditions by equilibrium-mixture analysis is reported. Cyclosporine 174-177 peptidylprolyl isomerase G Homo sapiens 92-95 8679570-1 1996 Binding of mitochondrial cyclophilin (CyP) to the inner mitochondrial membrane is induced by treatment of mitochondria with thiol reagents or oxidative stress and correlates with a sensitization to [Ca2+] of the cyclosporin A-sensitive mitochondrial permeability transition pore (MTP) [Connern, C. P., & Halestrap, A. P. (1994) Biochem. Cyclosporine 212-225 peptidylprolyl isomerase G Homo sapiens 25-36 10189702-5 1999 This Ca(2+)-stimulated phosphatase activity was inhibited by CsA, suggesting the presence of both cytosolic CyP and calcineurin-like protein phosphatase in guard cells. Cyclosporine 61-64 peptidylprolyl isomerase G Homo sapiens 108-111 9709036-1 1998 The immunosuppressive fungal products cyclosporin A (CsA) and FK506 bind with high affinity to intracellular receptor proteins: cyclophilin (CYP) is one of the receptors for CsA and FK506-binding protein (FKBP) is one of the receptors for FK506. Cyclosporine 38-51 peptidylprolyl isomerase G Homo sapiens 128-139 9709036-1 1998 The immunosuppressive fungal products cyclosporin A (CsA) and FK506 bind with high affinity to intracellular receptor proteins: cyclophilin (CYP) is one of the receptors for CsA and FK506-binding protein (FKBP) is one of the receptors for FK506. Cyclosporine 38-51 peptidylprolyl isomerase G Homo sapiens 141-144 9472618-4 1998 It was demonstrated that analogues with strong Cyp-binding activity, such as CsC, CsG and [MeAla6]CsA, also exhibit a strong antiviral effect. Cyclosporine 98-101 peptidylprolyl isomerase G Homo sapiens 47-50 9472618-6 1998 The data obtained suggest a correlation between the ability of CsA to block VV replication and Cyp binding activity, and indicate the involvement of Cyps in the VV replicative cycle. Cyclosporine 63-66 peptidylprolyl isomerase G Homo sapiens 95-98 9075347-1 1997 The drug cyclosporin A (CsA) exerts its immunosuppressive action by binding to the cytosolic protein, cyclophilin (CyP) and, as a complex, binding to and inhibiting the calcium/calmodulin-dependent serine threonine phosphatase, calcineurin. Cyclosporine 9-22 peptidylprolyl isomerase G Homo sapiens 102-113 9075347-1 1997 The drug cyclosporin A (CsA) exerts its immunosuppressive action by binding to the cytosolic protein, cyclophilin (CyP) and, as a complex, binding to and inhibiting the calcium/calmodulin-dependent serine threonine phosphatase, calcineurin. Cyclosporine 9-22 peptidylprolyl isomerase G Homo sapiens 115-118 9075347-1 1997 The drug cyclosporin A (CsA) exerts its immunosuppressive action by binding to the cytosolic protein, cyclophilin (CyP) and, as a complex, binding to and inhibiting the calcium/calmodulin-dependent serine threonine phosphatase, calcineurin. Cyclosporine 24-27 peptidylprolyl isomerase G Homo sapiens 102-113 9075347-1 1997 The drug cyclosporin A (CsA) exerts its immunosuppressive action by binding to the cytosolic protein, cyclophilin (CyP) and, as a complex, binding to and inhibiting the calcium/calmodulin-dependent serine threonine phosphatase, calcineurin. Cyclosporine 24-27 peptidylprolyl isomerase G Homo sapiens 115-118 9075347-5 1997 Both proteins were calcium- and calmodulin-dependent and were inhibited by mammalian cyclophilin complexed with cyclosporin A (IC50 values of 0.75 microgram CyP for H. microstoma and 0.90 microgram CyP for H. diminuta). Cyclosporine 112-125 peptidylprolyl isomerase G Homo sapiens 85-96 9075347-5 1997 Both proteins were calcium- and calmodulin-dependent and were inhibited by mammalian cyclophilin complexed with cyclosporin A (IC50 values of 0.75 microgram CyP for H. microstoma and 0.90 microgram CyP for H. diminuta). Cyclosporine 112-125 peptidylprolyl isomerase G Homo sapiens 157-160 9075347-5 1997 Both proteins were calcium- and calmodulin-dependent and were inhibited by mammalian cyclophilin complexed with cyclosporin A (IC50 values of 0.75 microgram CyP for H. microstoma and 0.90 microgram CyP for H. diminuta). Cyclosporine 112-125 peptidylprolyl isomerase G Homo sapiens 198-201 9010851-9 1996 The complex of CsA or FK506 with CyP or FKBP, respectively, inhibits the activation of calcineurin. Cyclosporine 15-18 peptidylprolyl isomerase G Homo sapiens 33-36 8939689-0 1996 Controlling programmed cell death with a cyclophilin-cyclosporin-based chemical inducer of dimerization. Cyclosporine 53-64 peptidylprolyl isomerase G Homo sapiens 41-52 8679570-1 1996 Binding of mitochondrial cyclophilin (CyP) to the inner mitochondrial membrane is induced by treatment of mitochondria with thiol reagents or oxidative stress and correlates with a sensitization to [Ca2+] of the cyclosporin A-sensitive mitochondrial permeability transition pore (MTP) [Connern, C. P., & Halestrap, A. P. (1994) Biochem. Cyclosporine 212-225 peptidylprolyl isomerase G Homo sapiens 38-41 7524680-2 1994 The charged states of the histidine residues in FKBP and CyP, which were characterized by their pKa values, have been determined in the absence and presence of the immunosuppressant ligands, ascomycin and cyclosporin A (CsA), respectively, by using a heteronuclear two-dimensional NMR method. Cyclosporine 205-218 peptidylprolyl isomerase G Homo sapiens 57-60 7529995-3 1995 The existence of a slow cis-trans interconversion of an imidic bond in the inhibitor molecule during the course of the formation of the CsA-CyP18cy complex (where CyP18cy is human 18 kDa cytosolic CyP) prompted us to investigate the reaction of the peptidomacrolides FK506, ascomycin and rapamycin with two specific binding-proteins in more detail. Cyclosporine 136-139 peptidylprolyl isomerase G Homo sapiens 140-143 7524680-2 1994 The charged states of the histidine residues in FKBP and CyP, which were characterized by their pKa values, have been determined in the absence and presence of the immunosuppressant ligands, ascomycin and cyclosporin A (CsA), respectively, by using a heteronuclear two-dimensional NMR method. Cyclosporine 220-223 peptidylprolyl isomerase G Homo sapiens 57-60 7524680-7 1994 His-126, which is part of the CsA and substrate binding site, has a pKa of 6.3 in free CyP. Cyclosporine 30-33 peptidylprolyl isomerase G Homo sapiens 87-90 7509138-7 1993 Both the FKBP/FK-506 complex and the Cyp/CsA complex can bind to calcineurin, thereby inhibiting its phosphatase activity. Cyclosporine 41-44 peptidylprolyl isomerase G Homo sapiens 37-40 8312269-1 1994 Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase (PPIase). Cyclosporine 78-91 peptidylprolyl isomerase G Homo sapiens 0-11 8312269-1 1994 Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase (PPIase). Cyclosporine 78-91 peptidylprolyl isomerase G Homo sapiens 13-16 8312269-1 1994 Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase (PPIase). Cyclosporine 93-96 peptidylprolyl isomerase G Homo sapiens 0-11 8312269-1 1994 Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase (PPIase). Cyclosporine 93-96 peptidylprolyl isomerase G Homo sapiens 13-16 8031755-9 1994 Cross-reactivity studies with a series of Cs derivatives showed that Cyp-C binds CsA with a fine specificity similar to that of Cyp-A and Cyp-B. Cyclosporine 81-84 peptidylprolyl isomerase G Homo sapiens 69-72 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 G Homo sapiens 9-12 8075536-0 1994 Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex. Cyclosporine 65-78 peptidylprolyl isomerase G Homo sapiens 51-64 8075536-1 1994 The three-dimensional NMR solution structure of the cyclophilin A (Cyp)-cyclosporin A (CsA) complex was determined, and here we provide a detailed description of the analysis of the NMR data and the structure calculation. Cyclosporine 72-85 peptidylprolyl isomerase G Homo sapiens 52-65 8075536-1 1994 The three-dimensional NMR solution structure of the cyclophilin A (Cyp)-cyclosporin A (CsA) complex was determined, and here we provide a detailed description of the analysis of the NMR data and the structure calculation. Cyclosporine 72-85 peptidylprolyl isomerase G Homo sapiens 67-70 8075981-1 1994 BACKGROUND: Cyclophilin (CyP) is a ubiquitious intracellular protein that binds the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 107-120 peptidylprolyl isomerase G Homo sapiens 12-23 8075981-1 1994 BACKGROUND: Cyclophilin (CyP) is a ubiquitious intracellular protein that binds the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 107-120 peptidylprolyl isomerase G Homo sapiens 25-28 1628422-1 1992 Cyclosporin (CsA) is an immunosuppressant which binds to cyclophilin (Cyp). Cyclosporine 0-11 peptidylprolyl isomerase G Homo sapiens 57-68 7686148-1 1993 Calcineurin (CaN), a Ca2+/calmodulin-dependent serine/threonine phosphatase, has been shown to be inhibited by the complex of the immunosuppressant cyclosporin A (CsA) and its receptor, cyclophilin (CyP), but not by either alone. Cyclosporine 163-166 peptidylprolyl isomerase G Homo sapiens 186-197 7686148-1 1993 Calcineurin (CaN), a Ca2+/calmodulin-dependent serine/threonine phosphatase, has been shown to be inhibited by the complex of the immunosuppressant cyclosporin A (CsA) and its receptor, cyclophilin (CyP), but not by either alone. Cyclosporine 163-166 peptidylprolyl isomerase G Homo sapiens 199-202 7686148-3 1993 In the presence of cyclosporin, 125I-CyP, shown to bind to CsA, is extensively cross-linked to the B subunit of CaN but not the catalytic A subunit. Cyclosporine 19-30 peptidylprolyl isomerase G Homo sapiens 37-40 7686148-3 1993 In the presence of cyclosporin, 125I-CyP, shown to bind to CsA, is extensively cross-linked to the B subunit of CaN but not the catalytic A subunit. Cyclosporine 59-62 peptidylprolyl isomerase G Homo sapiens 37-40 7686148-4 1993 However, the A subunit is required for binding of the CyP.CsA complex, since cross-linking to recombinant B subunit alone does not occur. Cyclosporine 58-61 peptidylprolyl isomerase G Homo sapiens 54-57 7686148-8 1993 CyP.CsA cross-linking to CaN is Ca2+/calmodulin-dependent with intact CaN, but Ca2+/calmodulin-independent after digestion to remove the calmodulin binding and autoinhibitory domain. Cyclosporine 4-7 peptidylprolyl isomerase G Homo sapiens 0-3 1628422-1 1992 Cyclosporin (CsA) is an immunosuppressant which binds to cyclophilin (Cyp). Cyclosporine 0-11 peptidylprolyl isomerase G Homo sapiens 70-73 1628422-1 1992 Cyclosporin (CsA) is an immunosuppressant which binds to cyclophilin (Cyp). Cyclosporine 13-16 peptidylprolyl isomerase G Homo sapiens 57-68 1628422-1 1992 Cyclosporin (CsA) is an immunosuppressant which binds to cyclophilin (Cyp). Cyclosporine 13-16 peptidylprolyl isomerase G Homo sapiens 70-73 1628422-2 1992 The relationship between Cyp binding and immunosuppression has been questioned since one of the analogs of CsA, N-methyl-L-alanyl6 cyclosporin (methyl-alanyl CsA) binds to Cyp but is not immunosuppressive. Cyclosporine 107-110 peptidylprolyl isomerase G Homo sapiens 172-175 1628422-2 1992 The relationship between Cyp binding and immunosuppression has been questioned since one of the analogs of CsA, N-methyl-L-alanyl6 cyclosporin (methyl-alanyl CsA) binds to Cyp but is not immunosuppressive. Cyclosporine 158-161 peptidylprolyl isomerase G Homo sapiens 172-175 1628422-4 1992 Cyp is a peptidyl-prolyl isomerase which is abundant in all human tissues, yet the activities of CsA are mostly confined to inhibition of T cell and thymocyte activation, and to neuro- and nephro-toxicity and are independent of inhibition of the isomerase. Cyclosporine 97-100 peptidylprolyl isomerase G Homo sapiens 0-3 1743298-0 1991 1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site. Cyclosporine 81-84 peptidylprolyl isomerase G Homo sapiens 40-51 1743298-1 1991 The backbone 1H, 13C and 15N chemical shifts of cyclophilin (CyP) when bound to cyclosporin A (CsA) have been assigned from heteronuclear two- and three-dimensional NMR experiments involving selectively 15N- and uniformly 15N- and 15N,13C-labeled cyclophilin. Cyclosporine 95-98 peptidylprolyl isomerase G Homo sapiens 48-59 1743298-1 1991 The backbone 1H, 13C and 15N chemical shifts of cyclophilin (CyP) when bound to cyclosporin A (CsA) have been assigned from heteronuclear two- and three-dimensional NMR experiments involving selectively 15N- and uniformly 15N- and 15N,13C-labeled cyclophilin. Cyclosporine 95-98 peptidylprolyl isomerase G Homo sapiens 61-64 1743298-2 1991 From an analysis of the 1H and 15N chemical shifts of CyP that change upon binding to CsA and from CyP/CsA NOEs, we have determined the regions of cyclophilin involved in binding to CsA. Cyclosporine 86-89 peptidylprolyl isomerase G Homo sapiens 54-57 1743298-2 1991 From an analysis of the 1H and 15N chemical shifts of CyP that change upon binding to CsA and from CyP/CsA NOEs, we have determined the regions of cyclophilin involved in binding to CsA. Cyclosporine 86-89 peptidylprolyl isomerase G Homo sapiens 147-158 1743298-2 1991 From an analysis of the 1H and 15N chemical shifts of CyP that change upon binding to CsA and from CyP/CsA NOEs, we have determined the regions of cyclophilin involved in binding to CsA. Cyclosporine 103-106 peptidylprolyl isomerase G Homo sapiens 147-158 1744118-2 1991 Cyclophilin (CyP), a major cytosolic protein possessing peptidyl-prolyl cis-trans isomerase activity, has been implicated as the specific receptor of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 177-190 peptidylprolyl isomerase G Homo sapiens 0-11 1744118-2 1991 Cyclophilin (CyP), a major cytosolic protein possessing peptidyl-prolyl cis-trans isomerase activity, has been implicated as the specific receptor of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 177-190 peptidylprolyl isomerase G Homo sapiens 13-16 1744118-2 1991 Cyclophilin (CyP), a major cytosolic protein possessing peptidyl-prolyl cis-trans isomerase activity, has been implicated as the specific receptor of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 192-195 peptidylprolyl isomerase G Homo sapiens 0-11 1744118-2 1991 Cyclophilin (CyP), a major cytosolic protein possessing peptidyl-prolyl cis-trans isomerase activity, has been implicated as the specific receptor of the immunosuppressive drug cyclosporin A (CsA). Cyclosporine 192-195 peptidylprolyl isomerase G Homo sapiens 13-16 1744118-12 1991 From both equilibrium considerations and the results of kinetic characterizations it is proposed that of these three CyP proteins, hCyP1 is the most likely intracellular target for CsA. Cyclosporine 181-184 peptidylprolyl isomerase G Homo sapiens 117-120 2004448-0 1991 Determination of cyclosporine by a competitive binding assay with cyclophilin. Cyclosporine 17-29 peptidylprolyl isomerase G Homo sapiens 66-77 1871809-2 1991 To explore a potential relationship between the multiple systemic effects of CsA and the cellular and tissue distribution of CYP, thirty-three different normal porcine tissues were examined using an immunohistochemical technique. Cyclosporine 77-80 peptidylprolyl isomerase G Homo sapiens 125-128 1871809-10 1991 Generally, greater CYP-specific staining was noted in organs amenable to CsA immunosuppression (heart, liver, kidney), compared with organs deemed more immunologically vulnerable when allografted under CsA (pancreas, lung, small bowel). Cyclosporine 73-76 peptidylprolyl isomerase G Homo sapiens 19-22 1871809-11 1991 Similarly, CYP-immunospecific staining was abundant in tissues susceptible to CsA toxicities (neural tissue, smooth muscle, kidney, liver). Cyclosporine 78-81 peptidylprolyl isomerase G Homo sapiens 11-14 1871809-12 1991 This detailed immunohistological examination affords a correlation between CYP content and sensitivity to CsA. Cyclosporine 106-109 peptidylprolyl isomerase G Homo sapiens 75-78 2054356-0 1991 NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding. Cyclosporine 22-33 peptidylprolyl isomerase G Homo sapiens 45-56 2054356-1 1991 Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with peptidyl-prolyl isomerase activity. Cyclosporine 0-13 peptidylprolyl isomerase G Homo sapiens 91-102 2054356-1 1991 Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with peptidyl-prolyl isomerase activity. Cyclosporine 0-13 peptidylprolyl isomerase G Homo sapiens 104-107 1917291-2 1991 MeAla6-cyclosporin A (MeAla6-CsA) is a unique CsA analog that shows weak immunosuppressive activity and yet binds strongly to the proposed cytosolic protein receptor, cyclophilin (CyP). Cyclosporine 29-32 peptidylprolyl isomerase G Homo sapiens 167-178 1917291-2 1991 MeAla6-cyclosporin A (MeAla6-CsA) is a unique CsA analog that shows weak immunosuppressive activity and yet binds strongly to the proposed cytosolic protein receptor, cyclophilin (CyP). Cyclosporine 29-32 peptidylprolyl isomerase G Homo sapiens 180-183 2026447-0 1991 Distribution of the cyclosporine binding protein cyclophilin in human tissues. Cyclosporine 20-32 peptidylprolyl isomerase G Homo sapiens 49-60 2026447-1 1991 Cyclophilin (CYP) is the major intracellular binding protein for the immunosuppressive drug cyclosporine (CS). Cyclosporine 92-104 peptidylprolyl isomerase G Homo sapiens 0-11 2026447-1 1991 Cyclophilin (CYP) is the major intracellular binding protein for the immunosuppressive drug cyclosporine (CS). Cyclosporine 92-104 peptidylprolyl isomerase G Homo sapiens 13-16 2026447-1 1991 Cyclophilin (CYP) is the major intracellular binding protein for the immunosuppressive drug cyclosporine (CS). Cyclosporine 106-108 peptidylprolyl isomerase G Homo sapiens 0-11 2026447-1 1991 Cyclophilin (CYP) is the major intracellular binding protein for the immunosuppressive drug cyclosporine (CS). Cyclosporine 106-108 peptidylprolyl isomerase G Homo sapiens 13-16 1705513-1 1991 Structurally unrelated, FK-506 and cyclosporin (CsA) bind to and inhibit the action of distinct cytoplasmic receptors, FK-506-binding protein (FKBP) and cyclophilin (CyP), respectively. Cyclosporine 35-46 peptidylprolyl isomerase G Homo sapiens 153-164 1705513-1 1991 Structurally unrelated, FK-506 and cyclosporin (CsA) bind to and inhibit the action of distinct cytoplasmic receptors, FK-506-binding protein (FKBP) and cyclophilin (CyP), respectively. Cyclosporine 35-46 peptidylprolyl isomerase G Homo sapiens 166-169 1705513-1 1991 Structurally unrelated, FK-506 and cyclosporin (CsA) bind to and inhibit the action of distinct cytoplasmic receptors, FK-506-binding protein (FKBP) and cyclophilin (CyP), respectively. Cyclosporine 48-51 peptidylprolyl isomerase G Homo sapiens 153-164 1705513-1 1991 Structurally unrelated, FK-506 and cyclosporin (CsA) bind to and inhibit the action of distinct cytoplasmic receptors, FK-506-binding protein (FKBP) and cyclophilin (CyP), respectively. Cyclosporine 48-51 peptidylprolyl isomerase G Homo sapiens 166-169 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 40-52 peptidylprolyl isomerase G Homo sapiens 116-127 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 40-52 peptidylprolyl isomerase G Homo sapiens 129-132 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 87-99 peptidylprolyl isomerase G Homo sapiens 116-127 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 87-99 peptidylprolyl isomerase G Homo sapiens 129-132 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 154-167 peptidylprolyl isomerase G Homo sapiens 116-127 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 154-167 peptidylprolyl isomerase G Homo sapiens 129-132 2004448-1 1991 A competitive protein-binding assay for cyclosporine based on use of the intracellular cyclosporine-binding protein cyclophilin (CYP) was used to measure cyclosporin A (CsA) and its bioactive metabolites in whole blood. Cyclosporine 169-172 peptidylprolyl isomerase G Homo sapiens 129-132 2004448-2 1991 CYP from cytoplasmic extracts or erythrocyte lysates was applied in the binding assay with use of [3H]CsA as tracer and charcoal adsorption for separating bound from free tracer. Cyclosporine 102-105 peptidylprolyl isomerase G Homo sapiens 0-3 35242122-7 2022 Consistent with disruption of viral cloaking and innate immune evasion, treatment with Cyp inhibitors such as cyclosporine A (CsA) restores antiviral innate immunity and induces expression of a subset of antiviral genes that restrict viral infection, which may help to explain the broad antiviral spectrum of CsA. Cyclosporine 110-124 peptidylprolyl isomerase G Homo sapiens 87-90 35242122-7 2022 Consistent with disruption of viral cloaking and innate immune evasion, treatment with Cyp inhibitors such as cyclosporine A (CsA) restores antiviral innate immunity and induces expression of a subset of antiviral genes that restrict viral infection, which may help to explain the broad antiviral spectrum of CsA. Cyclosporine 126-129 peptidylprolyl isomerase G Homo sapiens 87-90 35242122-7 2022 Consistent with disruption of viral cloaking and innate immune evasion, treatment with Cyp inhibitors such as cyclosporine A (CsA) restores antiviral innate immunity and induces expression of a subset of antiviral genes that restrict viral infection, which may help to explain the broad antiviral spectrum of CsA. Cyclosporine 309-312 peptidylprolyl isomerase G Homo sapiens 87-90 3043795-0 1988 Cyclophilin, a primary molecular target for cyclosporine. Cyclosporine 44-56 peptidylprolyl isomerase G Homo sapiens 0-11 3043795-3 1988 Our laboratory has presented evidence that cyclophilin (CYP), a low-molecular-weight (Mr 17,737) basic protein, is the primary cytosolic receptor for CsA. Cyclosporine 150-153 peptidylprolyl isomerase G Homo sapiens 43-54 3043795-3 1988 Our laboratory has presented evidence that cyclophilin (CYP), a low-molecular-weight (Mr 17,737) basic protein, is the primary cytosolic receptor for CsA. Cyclosporine 150-153 peptidylprolyl isomerase G Homo sapiens 56-59 3043795-4 1988 The high affinity of CYP for CsA (Kd 30 nM) and specificity for immunosuppressive cyclosporine analogs implicate CYP as a pivotal regulator of T cell and B cell activation. Cyclosporine 29-32 peptidylprolyl isomerase G Homo sapiens 21-24 3043795-4 1988 The high affinity of CYP for CsA (Kd 30 nM) and specificity for immunosuppressive cyclosporine analogs implicate CYP as a pivotal regulator of T cell and B cell activation. Cyclosporine 29-32 peptidylprolyl isomerase G Homo sapiens 113-116 3043795-4 1988 The high affinity of CYP for CsA (Kd 30 nM) and specificity for immunosuppressive cyclosporine analogs implicate CYP as a pivotal regulator of T cell and B cell activation. Cyclosporine 82-94 peptidylprolyl isomerase G Homo sapiens 21-24 3043795-4 1988 The high affinity of CYP for CsA (Kd 30 nM) and specificity for immunosuppressive cyclosporine analogs implicate CYP as a pivotal regulator of T cell and B cell activation. Cyclosporine 82-94 peptidylprolyl isomerase G Homo sapiens 113-116 3043795-8 1988 The ability of CsA to suppress expression of several lymphokine and proto-oncogene products via a transcriptional control mechanism suggests that CYP may function at some level in a signaling pathway linking membrane receptor stimulation to gene regulatory elements in lymphocytes, and possibly nonlymphoid cell types as well. Cyclosporine 15-18 peptidylprolyl isomerase G Homo sapiens 146-149 33548873-9 2021 Interestingly, not only cyclosporin, but also leuprorelin and cetrorelix showed metabolites whose formation was CYP (NADPH) dependent in liver S9. Cyclosporine 24-35 peptidylprolyl isomerase G Homo sapiens 112-115 2966482-4 1988 These results strongly implicate CyP or a related protein in the mechanism of action of cyclosporine. Cyclosporine 88-100 peptidylprolyl isomerase G Homo sapiens 33-36 25193101-1 2015 Calcineurin (CN) is the target of the immunophilin-immunosuppressant complex, cyclophilin/cyclosporin A (CyP/CsA). Cyclosporine 90-103 peptidylprolyl isomerase G Homo sapiens 105-108 25193101-7 2015 Using isothermal titration calorimetry (ITC), we found that the RCAN1-1L/CN or CyP/CsA/CN interactions were exothermic with a dissociation constant of 0.46 muM or 0.17 muM, respectively. Cyclosporine 83-86 peptidylprolyl isomerase G Homo sapiens 79-82