Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors
about
Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complexMondoA-Mlx heterodimers are candidate sensors of cellular energy status: mitochondrial localization and direct regulation of glycolysisGlucose activates ChREBP by increasing its rate of nuclear entry and relieving repression of its transcriptional activityRole for the mortality factors MORF4, MRGX, and MRG15 in transcriptional repression via associations with Pf1, mSin3A, and Transducin-Like Enhancer of Split.A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex.MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like networkFunctional interactions among members of the MAX and MLX transcriptional network during oncogenesisMxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional repression potentialIsolation and characterization of BEN, a member of the TFII-I family of DNA-binding proteins containing distinct helix-loop-helix domainsTOM1L1 is a Lyn substrate involved in FcepsilonRI signaling in mast cells.The Max network gone mad.Activation and repression of glucose-stimulated ChREBP requires the concerted action of multiple domains within the MondoA conserved regionMyc, mondo, and metabolismExpression and mutation analysis of genes that encode the Myc antagonists Mad1, Mxi1 and Rox in acute leukaemia.Deregulated Myc requires MondoA/Mlx for metabolic reprogramming and tumorigenesisMetabolic reprogramming in triple-negative breast cancer through Myc suppression of TXNIPA critical role for the loop region of the basic helix-loop-helix/leucine zipper protein Mlx in DNA binding and glucose-regulated transcription.Assembly of b/HLH/z proteins c-Myc, Max, and Mad1 with cognate DNA: importance of protein-protein and protein-DNA interactions.MondoA senses adenine nucleotides: transcriptional induction of thioredoxin-interacting proteinMio acts in the Drosophila brain to control nutrient storage and feeding.Contrasting Patterns in the Evolution of Vertebrate MLX Interacting Protein (MLXIP) and MLX Interacting Protein-Like (MLXIPL) Genes.A C. elegans Myc-like network cooperates with semaphorin and Wnt signaling pathways to control cell migration.Mio/dChREBP coordinately increases fat mass by regulating lipid synthesis and feeding behavior in Drosophila.The glucose-sensing transcription factor MLX promotes myogenesis via myokine signalingAn overview of MYC and its interactome.Hepatic glucose sensing and integrative pathways in the liver.Acquisition of essential somatic cell cycle regulatory protein expression and implied activity occurs at the second to third cell division in mouse preimplantation embryos.MNT and Emerging Concepts of MNT-MYC AntagonismElevated glucose represses liver glucokinase and induces its regulatory protein to safeguard hepatic phosphate homeostasisGlucose induces protein targeting to glycogen in hepatocytes by fructose 2,6-bisphosphate-mediated recruitment of MondoA to the promoter.Target metabolomics revealed complementary roles of hexose- and pentose-phosphates in the regulation of carbohydrate-dependent gene expression.A novel role of the Mad family member Mad3 in cerebellar granule neuron precursor proliferation.Mmip-2/Rnf-17 enhances c-Myc function and regulates some target genes in common with glucocorticoid hormones.Asn(78) and His(81) form a destabilizing locus within the Max HLH-LZ homodimer.Impaired glucose metabolism in subjects with the Williams-Beuren syndrome: A five-year follow-up cohort study.ChREBP*Mlx is the principal mediator of glucose-induced gene expression in the liver.Fructose 2,6-bisphosphate is essential for glucose-regulated gene transcription of glucose-6-phosphatase and other ChREBP target genes in hepatocytes.
P2860
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P2860
Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@ast
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en-gb
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@nl
type
label
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@ast
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en-gb
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@nl
prefLabel
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@ast
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en-gb
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@nl
P2093
P356
P1476
Mlx, a novel Max-like BHLHZip ...... twork of transcription factors
@en
P2093
P304
P356
10.1074/JBC.274.51.36344
P407
P577
1999-12-17T00:00:00Z