Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
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 calreticulinHepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5AExpression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexesThe 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 proteinsCloning, 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 cellsBcl-2 regulator FKBP38 is activated by Ca2+/calmodulin.Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin ADistribution 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 VprCloning 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 cyclophilinNull mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfectaFKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibitionTwo protein-protein interaction sites on the spliceosome-associated human cyclophilin CypHThe hydrophobic pocket of cyclophilin is the binding site for the human immunodeficiency virus type 1 Gag polyproteinThe cyclophilinsN-linked sugar-regulated protein folding and quality control in the ERFrom Drosophila to humans: reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and diseaseThe Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus ReplicationSCY-635, a Novel Nonimmunosuppressive Analog of Cyclosporine That Exhibits Potent Inhibition of Hepatitis C Virus RNA Replication In VitroBiochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegansThe crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active siteStructural Basis for High-Affinity Peptide Inhibition of Human Pin1The three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activityThe crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1)A Reduced-Amide Inhibitor of Pin1 Binds in a Conformation Resembling a Twisted-Amide Transition StateStructure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptideStructural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1High-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 Cwc27A Structural Ensemble for the Enzyme Cyclophilin Reveals an Orchestrated Mode of Action at Atomic ResolutionCrystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin AFK 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.
P2860
Q22001507-291190C8-2065-4439-8B33-7A05E0282C81Q24290922-D191E08C-C35A-4A17-96E6-97BBDE8707F5Q24299896-B12685EC-DF52-4BA7-9008-297D2A99EB3EQ24301154-B8C0DB99-8362-4D5B-8B9F-BA4DEECACADAQ24301260-F2069A9F-BF59-4470-92F1-AD2CC4C93AFBQ24303838-ADB11F2B-C7B5-426B-AD53-F1BAA7FD1EADQ24304321-CCFE9BBA-76D2-4E65-9868-87ABB7DACFB0Q24312016-DCDD42DD-5002-408A-B7D9-E27E166C6D6CQ24317548-85946C67-7E92-4442-9558-0182CC9E0B99Q24320071-376C32A7-F4B9-4588-8612-3E8DFAD19C42Q24531464-663BF063-A4BE-4912-BFC2-88DDA6478BE0Q24534698-77F007D4-A033-43FD-A1CB-C605D79B8559Q24538183-27EBD637-1A33-4C49-B769-FFF90C2F88ACQ24543218-D4CE9FFB-5E6E-49F9-90F1-0984CC32D08EQ24562087-D75DBB7D-3FD7-4E30-B3F1-0B022F67BD48Q24563425-169141C6-7724-4316-82DB-B398B15263D2Q24598079-6DE163DD-77B7-43DF-9242-AE0DB986D026Q24617020-18DEB474-2AC1-4F6F-8733-42EE9A6A3416Q24651519-2A6E705C-C63C-4820-96D6-BB26C1A6B742Q24670824-F70E2167-32D8-4BEE-A005-570C3B317120Q24678636-BCBF2340-D774-47F9-8924-AE6DA838F026Q24812580-C44442DA-85C5-4D42-8742-408297579928Q26827318-2D200095-6A93-4A52-B2F2-227991221A56Q26829060-1E2B31DD-EE2D-48C7-BE6D-8569EEC61C7FQ27489053-F6ECABF2-6E9F-40E8-A73F-25839FAB7C93Q27490844-1D1BEC9A-25E0-4890-BDA7-6F7B9B0AF148Q27620496-3CBCA560-4E0A-457A-8357-EAE8219B34BEQ27641943-B1ABAED7-5B31-4863-BBA2-A2F5DCF2C375Q27644848-992BBEEF-3E47-4BC1-BA24-FF57C1EB9DC0Q27646423-4151D044-C249-4E32-9928-12BFB78A623AQ27650272-C38EAB9F-BB66-440E-90C4-B036BBEA4F68Q27674779-146D25BB-7F78-4A30-A81F-D2F17721EA3EQ27678171-6C624304-6B64-4B91-820A-4E56BF2C19B1Q27684248-6A5426F2-CA73-431F-92C8-2E365FFBACEDQ27684278-451B55CE-7DB6-47C8-85A6-80AE2D77C90BQ27696314-3C598658-F169-4143-A9A0-919EF63F3834Q27701785-888540F0-23B4-47BE-BDEA-7278818EABDEQ27731514-1C672D2C-B6FC-4F14-B29F-3CD30385A57DQ27931207-7E728BD0-1C83-4F2F-A3CB-625E3523B7BFQ27933866-E9D03DD0-3E45-493C-9163-EDD3B183433A
P2860
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
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
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@ast
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@en
type
label
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@ast
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@en
prefLabel
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@ast
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@en
P2093
P3181
P356
P1433
P1476
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
@en
P2093
Kiefhaber T
Wittmann-Liebold B
P2888
P3181
P356
10.1038/337476A0
P407
P577
1989-02-02T00:00:00Z
P6179
1052387479