Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex - Wikidata - wikimedia - TriplyDB

Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex

Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex

http://www.wikidata.org/entity/Q27642356

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Epigenetic inactivation of the canonical Wnt antagonist SRY-box containing gene 17 in colorectal cancer The transcriptional foundation of pluripotency Sox2 and Oct-3/4: a versatile pair of master regulators that orchestrate the self-renewal and pluripotency of embryonic stem cells Reprogramming cells with synthetic proteins Solution NMR structure of the barrier-to-autointegration factor-Emerin complex Solution Structure of the IIAChitobiose-IIBChitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase System Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering Human mitochondrial transcription factor A induces a U-turn structure in the light strand promoter The crystal structure of the Sox4 HMG domain-DNA complex suggests a mechanism for positional interdependence in DNA recognition A unique Oct4 interface is crucial for reprogramming to pluripotency DNA-dependent formation of transcription factor pairs alters their binding specificity An Oct4-centered protein interaction network in embryonic stem cells Interplay of SOX and POU factors in regulation of the Nestin gene in neural primordial cells Structural Mechanism behind Distinct Efficiency of Oct4/Sox2 Proteins in Differentially Spaced DNA Complexes Reciprocal transcriptional regulation of Pou5f1 and Sox2 via the Oct4/Sox2 complex in embryonic stem cells On the need for mechanistic models in computational genomics and metagenomics Evolutionary conservation of DNA-contact residues in DNA-binding domains.Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Solution NMR-derived global fold of a monomeric 82-kDa enzyme.Tethered-hopping model for protein-DNA binding and unbinding based on Sox2-Oct1-Hoxb1 ternary complex simulations.Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.Structural basis of the association of HIV-1 matrix protein with DNA.The SOX2 response program in glioblastoma multiforme: an integrated ChIP-seq, expression microarray, and microRNA analysis Inferring transcription factor complexes from ChIP-seq data.Sox2 acts as a rheostat of epithelial to mesenchymal transition during neural crest development.Solution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches.Direct reprogramming of mouse and human fibroblasts into multipotent neural stem cells with a single factor.Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system Genome-wide analysis of androgen receptor targets reveals COUP-TF1 as a novel player in human prostate cancer.SOX2 co-occupies distal enhancer elements with distinct POU factors in ESCs and NPCs to specify cell state Modeling stem cell induction processes.Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.Combinatorial binding of transcription factors in the pluripotency control regions of the genome.Transcription factor heterogeneity and epiblast pluripotency.Model of a DNA-protein complex of the architectural monomeric protein MC1 from Euryarchaea.Genome-wide analysis of OCT4 binding sites in glioblastoma cancer cells.Mammalian testis-determining factor SRY and the enigma of inherited human sex reversal: frustrated induced fit in a bent protein-DNA complex.Exploring translocation of proteins on DNA by NMR Intramolecular domain-domain association/dissociation and phosphoryl transfer in the mannitol transporter of Escherichia coli are not coupled Cooperative DNA Recognition Modulated by an Interplay between Protein-Protein Interactions and DNA-Mediated Allostery.

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Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex

http://www.wikidata.org/entity/Q27642356

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունվարին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Molecular basis for synergisti ...... y transcription factor complex

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Molecular basis for synergisti ...... y transcription factor complex

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Molecular basis for synergisti ...... y transcription factor complex

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type

label

Molecular basis for synergisti ...... y transcription factor complex

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Molecular basis for synergisti ...... y transcription factor complex

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Molecular basis for synergisti ...... y transcription factor complex

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prefLabel

Molecular basis for synergisti ...... y transcription factor complex

@ast

Molecular basis for synergisti ...... y transcription factor complex

@en

Molecular basis for synergisti ...... y transcription factor complex

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P1433

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P1433

Journal of Biological Chemistry

P1476

Molecular basis for synergisti ...... y transcription factor complex

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P2093

David C Williams

http://www.w3.org/2001/XMLSchema#string

Mengli Cai

http://www.w3.org/2001/XMLSchema#string

P2860

Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors

Coactivator OBF-1 makes selective contacts with both the POU-specific domain and the POU homeodomain and acts as a molecular clamp on DNA.

Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers

PROCHECK: a program to check the stereochemical quality of protein structures

Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system

Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions

Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occurring point mutation

Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping

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1449-1457

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scholarly article

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4048024

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P356

10.1074/JBC.M309790200

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2

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P478

279

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G. Marius Clore

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2003-10-14T00:00:00Z

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14559893

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P921