A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
about
Identification of direct protein targets of small moleculesHuman cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequenceA quantitative chemical proteomics approach to profile the specific cellular targets of andrographolide, a promising anticancer agent that suppresses tumor metastasisExpression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexesFK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53TCloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesisMolecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13FKBP12 regulates the localization and processing of amyloid precursor protein in human cell linesComplementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilinThe 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolinStructure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexesFKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibitionThe 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1Parallel chemical genetic and genome-wide RNAi screens identify cytokinesis inhibitors and targetsModulation of Protein-Protein Interactions for the Development of Novel TherapeuticsFrom Drosophila to humans: reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and diseaseStructure and function of outer dynein arm intermediate and light chain complex.Structural Basis for High-Affinity Peptide Inhibition of Human Pin1A Reduced-Amide Inhibitor of Pin1 Binds in a Conformation Resembling a Twisted-Amide Transition StateStructure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline IsomerizationStructural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1Architecture of human mTOR complex 1Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast.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.Saccharomyces cerevisiae FKBP12 binds Arabidopsis thaliana TOR and its expression in plants leads to rapamycin susceptibility.Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase.A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing.A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycinAtomic structure of FKBP-FK506, an immunophilin-immunosuppressant complexTargets for cell cycle arrest by the immunosuppressant rapamycin in yeastModulation of type-1 Ins(1,4,5)P3 receptor channels by the FK506-binding protein, FKBP12N-terminal extension changes the folding mechanism of the FK506-binding proteinAdverse effects of FK 506 overdosage after liver transplantation
P2860
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P2860
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
description
1989 nî lūn-bûn
@nan
1989 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հոտեմբերին 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
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@ast
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en-gb
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@nl
type
label
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@ast
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en-gb
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@nl
prefLabel
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@ast
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en-gb
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@nl
P2093
P921
P3181
P356
P1433
P1476
A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
@en
P2093
D E Uehling
M W Harding
S L Schreiber
P2888
P304
P3181
P356
10.1038/341758A0
P407
P577
1989-10-26T00:00:00Z
P5875
P6179
1040106884