The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
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O-GlcNAcylation regulates EZH2 protein stability and functionO-GlcNAc modification of Sp1 inhibits the functional interaction between Sp1 and Oct1Hexosamines, insulin resistance, and the complications of diabetes: current status.Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brainThe C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cellsProtein tyrosine phosphatases as wardens of STAT signalingSTAT5 in hematopoietic stem cell biology and transplantationSignal transducer and activator of transcription 5A/B in prostate and breast cancersThe hexosamine signaling pathway: deciphering the "O-GlcNAc code"Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucoseNuclear localization of STAT5A modified with O-linked N-acetylglucosamine and early involution in the mammary gland of Hirosaki hairless ratPhosphorylation modification of wheat lectin VER2 is associated with vernalization-induced O-GlcNAc signaling and intracellular motility.STAT5 requires the N-domain for suppression of miR15/16, induction of bcl-2, and survival signaling in myeloproliferative diseaseO-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin.O-GlcNAc signaling in the cardiovascular system.Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of I{kappa}B kinases in mice: impact on histone acetylation.The different functions of Stat5 and chromatin alteration through Stat5 proteinsMass spectrometry-based proteomics: the road to lung cancer biomarker discovery.Alternative ways of modulating JAK-STAT pathway: Looking beyond phosphorylation.Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1Transcription factor Stat5a/b as a therapeutic target protein for prostate cancer.In vivo and in vitro evidence that chronic activation of the hexosamine biosynthetic pathway interferes with leptin-dependent STAT3 phosphorylation.Signal transducer and activator of transcription 5a/b: biomarker and therapeutic target in prostate and breast cancerCellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.Chemical approaches to understanding O-GlcNAc glycosylation in the brain.Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity.O-GlcNAcylation of kinases.Glucose mediates the translocation of NeuroD1 by O-linked glycosylation.Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-β-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes.STAT5 requires the N-domain to maintain hematopoietic stem cell repopulating function and appropriate lymphoid-myeloid lineage output.Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling.Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux.Inteferons pen the JAK-STAT pathway.Loss of STAT5 causes liver fibrosis and cancer development through increased TGF-{beta} and STAT3 activation.TRIB3 mediates glucose-induced insulin resistance via a mechanism that requires the hexosamine biosynthetic pathway.O-GlcNAc cycling: implications for neurodegenerative disorders.Modulation of transcription factor function by O-GlcNAc modification.Dietary components in the development of leptin resistance.STAT5-mediated self-renewal of normal hematopoietic and leukemic stem cells.
P2860
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P2860
The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The coactivator of transcripti ...... he glycosylated form of Stat5.
@en
type
label
The coactivator of transcripti ...... he glycosylated form of Stat5.
@en
prefLabel
The coactivator of transcripti ...... he glycosylated form of Stat5.
@en
P2093
P2860
P356
P1476
The coactivator of transcripti ...... he glycosylated form of Stat5.
@en
P2093
Bernd Groner
Christian Beisenherz-Huss
Christina Gewinner
Gerald Hart
Natasha Zachara
Robert Cole
P2860
P304
P356
10.1074/JBC.M306449200
P407
P577
2003-11-03T00:00:00Z