Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
about
Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequenceCyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cellsThe peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stabilityStructural insights into the catalytic mechanism of cyclophilin As-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulinThe 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteinsParvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineageCloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesisA cyclophilin-related protein involved in the function of natural killer cellsRegulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin ACyclophilin A is required for TRIM5{alpha}-mediated resistance to HIV-1 in Old World monkey cellsDistribution of cyclophilin B-binding sites in the subsets of human peripheral blood lymphocytesInduction of G2 arrest and binding to cyclophilin A are independent phenotypes of human immunodeficiency virus type 1 VprComplementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilinCloning and characterization of cyclophilin C-associated protein: a candidate natural cellular ligand for cyclophilin CCyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin AAn endoplasmic reticulum-specific cyclophilinThe cyclophilinsEnzymes: An integrated view of structure, dynamics and functionFrom Drosophila to humans: reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and diseaseBiochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegansStructural Basis for High-Affinity Peptide Inhibition of Human Pin1The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1)High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 moleculesStructure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin ACrystal structure of the macrophage migration inhibitory factor from rat liverCyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae.Calcineurin is essential in cyclosporin A- and FK506-sensitive yeast strains.Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding proteinFKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase.All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.Cyclophilin catalyzes protein folding in yeast mitochondria.Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth.The mitochondrial permeability transition pore: molecular nature and role as a target in cardioprotectionCharacterization of the human cyclophilin gene and of related processed pseudogenesSolution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
P2860
Q22001507-610B431D-74F6-4532-9E15-309F3D4E0B41Q24290922-12A1DAF4-0853-47EB-9756-983353785D05Q24299896-B7D31938-275F-40C7-8078-61BEC4D9B72BQ24301154-D35CEAFB-AA0C-4D36-9DE1-134D154DB79FQ24301260-5D53C0F8-B828-4194-9831-854645329AC7Q24312016-8AAAB41F-2E2B-4F89-84CD-8D2B3811DA57Q24315973-52F74F88-9BC7-42BE-93EA-44BBEBD31903Q24317548-47CD5AA2-4024-42B6-9E31-7DF83EBDEA85Q24320071-50626188-E3C7-48CF-8639-4222B5C59EE6Q24534698-4DC95031-1D97-46C3-8B02-74EF8AA2BE17Q24536359-16CD9452-19F8-454C-A5B6-FC6D58B8A852Q24538183-D5E0027F-B438-4316-8F17-AA164CF5637BQ24543218-9C9436AE-D693-4E5A-9F88-C1859EB12E84Q24557575-4A592C8A-0288-414D-8850-EFA1EC2E8177Q24562087-0134E151-B7A3-4334-BCFC-C6185521B672Q24563425-14DE19BD-3F19-4B0C-B43E-6FE1DEE8F566Q24598079-D86B8A5B-6110-4AD5-AFDC-ED84C2CB838FQ24812580-861B726A-69F8-4BD9-BCC2-759AF1391008Q25255883-72E72214-1D59-442E-8A89-09D5C8FD7BC4Q26829060-642AE2B9-7F53-412E-B885-699382A53353Q27620496-28F35B4B-83A2-4D34-BA10-79C4E09DCBD0Q27644848-64188B63-DAB8-469C-918C-BFF724A09300Q27650272-7E3A6279-FF9D-47C9-91DD-9F85E0621D68Q27684278-0D0C406B-2EBF-4DD0-A981-546F16598903Q27696314-7B1990E5-9BC8-424E-A3AC-C487D10CCF76Q27731514-4B1FC362-A2CA-4B8F-9759-085CCE7ADD8BQ27732627-12A2241A-BD9E-477F-AB80-3D2D60CA0961Q27930786-0C0E04D9-9016-44D8-A825-57FC039347F2Q27931207-80E72F69-ECAF-4F67-8AB1-1E8C6BE31BBDQ27933866-3BEFEFA9-FED7-47E3-B9A9-EE7ED0C1AA1DQ27934061-370B18BF-A61A-4DA2-92FC-C414EBA16A41Q27934220-4B39079A-DFAC-42FF-AB78-AC970A8880AEQ27936501-D279B79F-3DD8-4CD9-A642-CD6368DACC75Q27937279-8B0D2CC8-8693-42C1-B75F-D09DCE3424BBQ27937787-4508EC01-A001-4C42-88BD-A5313F311CDEQ27938570-F960EFAB-C721-46D1-992F-705BB5E28771Q27939546-5D61EDB4-19E9-40BA-A11A-A1C692F03EC0Q28248925-0EB30281-EE63-4AE0-BF6A-6466A2A8665FQ28249641-05D49638-9D5D-409D-B67F-8CF67C10454FQ28273170-03974D08-19A7-48E5-BC55-76DF50E0C8EE
P2860
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
description
1989 nî lūn-bûn
@nan
1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@ast
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en-gb
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@nl
type
label
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@ast
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en-gb
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@nl
prefLabel
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@ast
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en-gb
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@nl
P2093
P3181
P356
P1433
P1476
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
@en
P2093
P2888
P3181
P356
10.1038/337473A0
P407
P577
1989-02-02T00:00:00Z
P6179
1052163322