Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers - Test2 - elhamkhani - TriplyDB

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

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

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The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA The high-mobility-group domain of Sox proteins interacts with DNA-binding domains of many transcription factors Oct4/Sox2-regulated miR-302 targets cyclin D1 in human embryonic stem cells 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 Control of cell fate and differentiation by Sry-related high-mobility-group box (Sox) transcription factors Probing the DNA kink structure induced by the hyperthermophilic chromosomal protein Sac7d Reprogramming cells with synthetic proteins The roles of the reprogramming factors Oct4, Sox2 and Klf4 in resetting the somatic cell epigenome during induced pluripotent stem cell generation Gene networks of fully connected triads with complete auto-activation enable multistability and stepwise stochastic transitions 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 DNA intercalation without flipping in the specific ThaI-DNA complex 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 Distinctive Klf4 mutants determine preference for DNA methylation status The early expansion and evolutionary dynamics of POU class genes An Oct4-centered protein interaction network in embryonic stem cells Stemness-related factor Sall4 interacts with transcription factors Oct-3/4 and Sox2 and occupies Oct-Sox elements in mouse embryonic stem cells Orphan nuclear receptor GCNF is required for the repression of pluripotency genes during retinoic acid-induced embryonic stem cell differentiation.A direct physical interaction between Nanog and Sox2 regulates embryonic stem cell self-renewal Interplay of SOX and POU factors in regulation of the Nestin gene in neural primordial cells Oct4 interaction with Hmgb2 regulates Akt signaling and pluripotency A dominant-negative form of mouse SOX2 induces trophectoderm differentiation and progressive polyploidy in mouse embryonic stem cells Structural Mechanism behind Distinct Efficiency of Oct4/Sox2 Proteins in Differentially Spaced DNA Complexes Oct4 kinetics predict cell lineage patterning in the early mammalian embryo Deciphering the Sox-Oct partner code by quantitative cooperativity measurements Reciprocal transcriptional regulation of Pou5f1 and Sox2 via the Oct4/Sox2 complex in embryonic stem cells Mammalian genes induce partially reprogrammed pluripotent stem cells in non-mammalian vertebrate and invertebrate species Co-motif discovery identifies an Esrrb-Sox2-DNA ternary complex as a mediator of transcriptional differences between mouse embryonic and epiblast stem cells Structure solution of DNA-binding proteins and complexes with ARCIMBOLDO libraries.A disorder-to-order structural transition in the COOH-tail of Fz4 determines misfolding of the L501fsX533-Fz4 mutant Post-translational regulation of Oct4 transcriptional activity High-throughput biochemical analysis of in vivo location data reveals novel distinct classes of POU5F1(Oct4)/DNA complexes.Identification of Pou5f1, Sox2, and Nanog downstream target genes with statistical confidence by applying a novel algorithm to time course microarray and genome-wide chromatin immunoprecipitation data.Oct4 targets regulatory nodes to modulate stem cell function Single-molecule dynamics of enhanceosome assembly in embryonic stem cells.Identification of context-dependent motifs by contrasting ChIP binding data.Biologic properties of mesenchymal stem cells derived from bone marrow and adipose tissue Sox2 uses multiple domains to associate with proteins present in Sox2-protein complexes.Tracing the origin of the fungal α1 domain places its ancestor in the HMG-box superfamily: implication for fungal mating-type evolution.

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

http://www.wikidata.org/entity/Q24671880

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2003 nî lūn-bûn

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2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2003 թվականի օգոստոսին հրատարակված գիտական հոդված

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

@ast

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

@en

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

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type

label

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

@ast

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

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Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

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prefLabel

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

@ast

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

@en

Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

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Crystal structure of a POU/HMG ...... Oct4 and Sox2 on two enhancers

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Attila Reményi

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Katharina Lins

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L Johan Nissen

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Rolland Reinbold

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Formation of pluripotent stem cells in the mammalian embryo depends on the POU transcription factor Oct4

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From head to toes: the multiple facets of Sox proteins

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

Pax6 and SOX2 form a co-DNA-binding partner complex that regulates initiation of lens development

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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2048-59

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1892657

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10.1101/GAD.269303

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16

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17

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Matthias Wilmanns

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2003-08-15T00:00:00Z

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10610209

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12923055

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crystal structure

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196258

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