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Mechanism for specificity by HMG-1 in enhanceosome assembly

Mechanism for specificity by HMG-1 in enhanceosome assembly

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HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes Role of nucleosome remodeling in neurodevelopmental and intellectual disability disorders High-mobility group box 1: an amplifier of stem and progenitor cell activity after stroke High-mobility-group proteins NHP6A and NHP6B participate in activation of the RNA polymerase III SNR6 gene.HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences Extracellular processing of amphoterin generates a peptide active on erythroleukaemia cell differentiation Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors The role of response elements organization in transcription factor selectivity: the IFN-β enhanceosome example Role of the acidic tail of high mobility group protein B1 (HMGB1) in protein stability and DNA bending High-mobility group protein box-1 and its relevance to cerebral ischemia The DNA architectural protein HMGB1 displays two distinct modes of action that promote enhanceosome assembly.HMGB1 in health and disease.HMBG1 mediates ischemia-reperfusion injury by TRIF-adaptor independent Toll-like receptor 4 signaling Expanding the paradigm for estrogen receptor binding and transcriptional activation Priming the nucleosome: a role for HMGB proteins?The bounty of RAGs: recombination signal complexes and reaction outcomes.Effects of nucleoid proteins on DNA repression loop formation in Escherichia coli Identification of a TAL1 target gene reveals a positive role for the LIM domain-binding protein Ldb1 in erythroid gene expression and differentiation.Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding.Mitochondrial Translocation of High Mobility Group Box 1 Facilitates LIM Kinase 2-Mediated Programmed Necrotic Neuronal Death Nuclear functions of the HMG proteins.Biphasic actions of HMGB1 signaling in inflammation and recovery after stroke.Transient HMGB protein interactions with B-DNA duplexes and complexes.Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding.Fine structure and activity of discrete RAG-HMG complexes on V(D)J recombination signals.The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity.Kaposi's sarcoma-associated herpesvirus (KSHV) Rta and cellular HMGB1 proteins synergistically transactivate the KSHV ORF50 promoter.The DNA architectural protein HMGB1 facilitates RTA-mediated viral gene expression in gamma-2 herpesviruses.Both high mobility group (HMG)-boxes and the acidic tail of HMGB1 regulate recombination-activating gene (RAG)-mediated recombination signal synapsis and cleavage in vitro.The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB.Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement Upwardly mobile proteins. Workshop: the role of HMG proteins in chromatin structure, gene expression and neoplasia.Understanding apparent DNA flexibility enhancement by HU and HMGB architectural proteins Determinants of HMGB proteins required to promote RAG1/2-recombination signal sequence complex assembly and catalysis during V(D)J recombination.Enhancement of DNA flexibility in vitro and in vivo by HMGB box A proteins carrying box B residues.18β-glycyrrhetic acid inhibits immune activation triggered by HMGB1, a pro-inflammatory protein found in the tear fluid during conjunctivitis and blepharitis.Pivotal neuroinflammatory and therapeutic role of high mobility group box 1 in ischemic stroke.Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana.The binding interaction of HMG-1 with the TATA-binding protein/TATA complex.

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Mechanism for specificity by HMG-1 in enhanceosome assembly

http://www.wikidata.org/entity/Q33963973

description

2000 nî lūn-bûn

@nan

2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Mechanism for specificity by HMG-1 in enhanceosome assembly

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Mechanism for specificity by HMG-1 in enhanceosome assembly

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type

label

Mechanism for specificity by HMG-1 in enhanceosome assembly

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Mechanism for specificity by HMG-1 in enhanceosome assembly

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prefLabel

Mechanism for specificity by HMG-1 in enhanceosome assembly

@ast

Mechanism for specificity by HMG-1 in enhanceosome assembly

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MCB.20.12.4359-4370.2000

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Molecular and Cellular Biology

P1476

Mechanism for specificity by HMG-1 in enhanceosome assembly

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P2093

K B Ellwood

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R C Johnson

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Y M Yen

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P2860

The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures

High mobility group protein-1 (HMG-1) is a unique activator of p53

High-mobility group (HMG) protein HMG-1 and TATA-binding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation

High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells

The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2

HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation

High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors

Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding

Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins

The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition

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4359-4370

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