FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins.
about
Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexesElucidating TOR signaling and rapamycin action: lessons from Saccharomyces cerevisiae.FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomeraseThe yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1.Yeast FKBP-13 is a membrane-associated FK506-binding protein encoded by the nonessential gene FKB2.All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeastA novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's diseaseTargets for cell cycle arrest by the immunosuppressant rapamycin in yeastIdentification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residueTarget of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progressionCrystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolutionProtein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions.Sphingomyelin homeostasis is required to form functional enzymatic domains at the trans-Golgi network.Immunophilins: structure-function relationship and possible role in microbial pathogenicity.Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicityThe chemistry of signal transduction.The Golgi apparatus maintains its organization independent of the endoplasmic reticulum.Target of rapamycin (TOR) in nutrient signaling and growth controlProline isomerases function during heat shock.A three-hybrid system for detecting small ligand-protein receptor interactions.The immunosuppressant FK506 inhibits amino acid import in Saccharomyces cerevisiae.Neisseria meningitidis encodes an FK506-inhibitable rotamase.Light-regulated, tissue-specific immunophilins in a higher plant.The immunosuppressant FK-506 specifically inhibits mitogen-induced activation of the interleukin-2 promoter and the isolated enhancer elements NFIL-2A and NF-AT1Antifungal properties of the immunosuppressant FK-506: identification of an FK-506-responsive yeast gene distinct from FKB1.Requirements for peptidyl-prolyl isomerization activity: a comprehensive mutational analysis of the substrate-binding cavity of FK506-binding protein 12.The Target of Rapamycin and Mechanisms of Cell Growth.A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli.
P2860
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P2860
FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins.
description
1991 nî lūn-bûn
@nan
1991 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@ast
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@en
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@nl
type
label
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@ast
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@en
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@nl
prefLabel
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@ast
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@en
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@nl
P2093
P2860
P356
P1476
FKB1 encodes a nonessential FK ...... homology to the cyclophilins.
@en
P2093
Brizuela L
Elliston K
Siekierka JJ
Wiederrecht G
P2860
P304
P356
10.1073/PNAS.88.3.1029
P407
P577
1991-02-01T00:00:00Z