Redox sensor CtBP mediates hypoxia-induced tumor cell migration. - Wikidata - wikimedia - TriplyDB

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

http://www.wikidata.org/entity/Q34694766

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SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation Quantitative magnetic resonance and optical imaging biomarkers of melanoma metastatic potential The conserved NAD(H)-dependent corepressor CTBP-1 regulates Caenorhabditis elegans life span Imaging mitochondrial redox potential and its possible link to tumor metastatic potential Crystal structures of human CtBP in complex with substrate MTOB reveal active site features useful for inhibitor design RETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex CIBZ, a novel BTB domain-containing protein, is involved in mouse spinal cord injury via mitochondrial pathway independent of p53 gene Biochemical issues in estimation of cytosolic free NAD/NADH ratio Interaction with cyclin H/cyclin-dependent kinase 7 (CCNH/CDK7) stabilizes C-terminal binding protein 2 (CtBP2) and promotes cancer cell migration CtBPs promote cell survival through the maintenance of mitotic fidelity.What have novel imaging techniques revealed about metabolism in the aging brain?CtBP1 interacts with Ikaros and modulates pituitary tumor cell survival and response to hypoxia Real-time assessment of the metabolic profile of living cells with genetically encoded NADH sensors Genome-wide profiles of CtBP link metabolism with genome stability and epithelial reprogramming in breast cancer.C-Terminal Binding Protein: A Molecular Link between Metabolic Imbalance and Epigenetic Regulation in Breast Cancer.Redox-dependent Brca1 transcriptional regulation by an NADH-sensor CtBP1.The transcriptional corepressor CtBP: a foe of multiple tumor suppressors.Transcriptional down-regulation of Brca1 and E-cadherin by CtBP1 in breast cancer Intracellular redox state revealed by in vivo (31) P MRS measurement of NAD(+) and NADH contents in brains.Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor Small Molecule, NSC95397, Inhibits the CtBP1-Protein Partner Interaction and CtBP1-Mediated Transcriptional Repression.Serial analysis of chromatin occupancy identifies beta-catenin target genes in colorectal carcinoma cells.Genetically encoded fluorescent sensors for intracellular NADH detection.The ternary complex factor net is downregulated by hypoxia and regulates hypoxia-responsive genes.CtBP1 overexpression in keratinocytes perturbs skin homeostasis.Frex and FrexH: Indicators of metabolic states in living cells.The miR-200 family and its targets regulate type II cell differentiation in human fetal lung.Genetic alterations in fatty acid transport and metabolism genes are associated with metastatic progression and poor prognosis of human cancers.Mitochondrial complex I activity and NAD+/NADH balance regulate breast cancer progression.Deciphering HIC1 control pathways to reveal new avenues in cancer therapeutics.Regulation of metastasis in colorectal adenocarcinoma: a collision between development and tumor biology.In vivo (31) P MRS assessment of intracellular NAD metabolites and NAD(+) /NADH redox state in human brain at 4 T.CtBP1 is expressed in melanoma and represses the transcription of p16INK4a and Brca1.Molecular determinants of brown adipocyte formation and function.Imaging heterogeneity in the mitochondrial redox state of premalignant pancreas in the pancreas-specific PTEN-null transgenic mouse model Disease-specific classification using deconvoluted whole blood gene expression HSCARG regulates NF-kappaB activation by promoting the ubiquitination of RelA or COMMD1 Phosphorylation of CtBP1 by cAMP-dependent protein kinase modulates induction of CYP17 by stimulating partnering of CtBP1 and 2.Nicotinamide phosphoribosyltransferase in malignancy: a review.Non-invasive in-cell determination of free cytosolic [NAD+]/[NADH] ratios using hyperpolarized glucose show large variations in metabolic phenotypes.

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Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

http://www.wikidata.org/entity/Q34694766

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2006 nî lūn-bûn

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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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name

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@ast

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@en

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@nl

type

label

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@ast

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@en

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@nl

prefLabel

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@ast

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@en

Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

@nl

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Redox sensor CtBP mediates hypoxia-induced tumor cell migration.

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Amanda C Nottke

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David W Piston

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Jonathan V Rocheleau

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Qinghong Zhang

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Richard H Goodman

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Su-Yan Wang

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state

A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis

The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver

Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha

Hypoxia attenuates the expression of E-cadherin via up-regulation of SNAIL in ovarian carcinoma cells

Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase

CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases.

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