Phosphorylation of nuclear MyoD is required for its rapid degradation.
about
Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysisNotch signaling induces rapid degradation of achaete-scute homolog 1.The functional role of an interleukin 6-inducible CDK9.STAT3 complex in human gamma-fibrinogen gene expressionTip60 regulates myoblast differentiation by enhancing the transcriptional activity of MyoD via their physical interactionsA role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic programMultiple phosphorylation events control mitotic degradation of the muscle transcription factor Myf5.The beneficial role of proteolysis in skeletal muscle growth and stress adaptationMicroRNAs regulate and provide robustness to the myogenic transcriptional networkDifferential modulation of cell cycle progression distinguishes members of the myogenic regulatory factor family of transcription factorsCoordinating cell proliferation and differentiation: Antagonism between cell cycle regulators and cell type-specific gene expressionActivation of MyoD-dependent transcription by cdk9/cyclin T2Stabilization of MyoD by direct binding to p57(Kip2)Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2Runx2- and histone deacetylase 3-mediated repression is relieved in differentiating human osteoblast cells to allow high bone sialoprotein expressionDown-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblastsThe E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradationMyogenin protein stability is decreased by BMP-2 through a mechanism implicating Id1Elevating the level of Cdc34/Ubc3 ubiquitin-conjugating enzyme in mitosis inhibits association of CENP-E with kinetochores and blocks the metaphase alignment of chromosomes.p38-{gamma}-dependent gene silencing restricts entry into the myogenic differentiation program.Enhancement of myogenic and muscle repair capacities of human adipose-derived stem cells with forced expression of MyoD.Mammalian target of rapamycin regulates miRNA-1 and follistatin in skeletal myogenesis.cdk1- and cdk2-mediated phosphorylation of MyoD Ser200 in growing C2 myoblasts: role in modulating MyoD half-life and myogenic activity.p57(Kip2) stabilizes the MyoD protein by inhibiting cyclin E-Cdk2 kinase activity in growing myoblasts.Antagonistic regulation of myogenesis by two deubiquitinating enzymes, UBP45 and UBP69.Activation of Ras and the mitogen-activated protein kinase pathway promotes protein degradation in muscle cells of Caenorhabditis elegans.Identification of novel MyoD gene targets in proliferating myogenic stem cellsThe N-terminal domain of MyoD is necessary and sufficient for its nuclear localization-dependent degradation by the ubiquitin systemIdentification of differentially regulated secretome components during skeletal myogenesisMitogen-activated protein kinase kinase 1 (MEK1) stabilizes MyoD through direct phosphorylation at tyrosine 156 during myogenic differentiation.Excitation-transcription coupling in skeletal muscle: the molecular pathways of exercise.Engineering Escherichia coli into a protein delivery system for mammalian cells.Defining the transcriptional signature of skeletal muscle stem cells.Reflections on lineage potential of skeletal muscle satellite cells: do they sometimes go MAD?Multi-site phosphorylation regulates NeuroD4 activity during primary neurogenesis: a conserved mechanism amongst proneural proteins.GEP constitutes a negative feedback loop with MyoD and acts as a novel mediator in controlling skeletal muscle differentiation.Snail regulates MyoD binding-site occupancy to direct enhancer switching and differentiation-specific transcription in myogenesis.Reciprocal inhibition between Pax7 and muscle regulatory factors modulates myogenic cell fate determination.Phosphorylation-dependent degradation of MEF2C contributes to regulate G2/M transitionMutant MyoD lacking Cdc2 phosphorylation sites delays M-phase entry.Mutant DMPK 3'-UTR transcripts disrupt C2C12 myogenic differentiation by compromising MyoD.
P2860
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P2860
Phosphorylation of nuclear MyoD is required for its rapid degradation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Phosphorylation of nuclear MyoD is required for its rapid degradation
@nl
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@ast
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en-gb
type
label
Phosphorylation of nuclear MyoD is required for its rapid degradation
@nl
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@ast
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en-gb
prefLabel
Phosphorylation of nuclear MyoD is required for its rapid degradation
@nl
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@ast
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en-gb
P2093
P2860
P3181
P356
P1476
Phosphorylation of nuclear MyoD is required for its rapid degradation.
@en
P2093
P2860
P304
P3181
P356
10.1128/MCB.18.9.4994
P407
P577
1998-09-01T00:00:00Z