about
Heterogeneous Effects of Direct Hypoxia Pathway Activation in Kidney CancerNormoxic stabilization of hypoxia-inducible factor-1alpha by modulation of the labile iron pool in differentiating U937 macrophages: effect of natural resistance-associated macrophage protein 1HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stabilityDetermination and comparison of specific activity of the HIF-prolyl hydroxylases.Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease.Regulation of the HIF pathway: enzymatic hydroxylation of a conserved prolyl residue in hypoxia-inducible factor alpha subunits governs capture by the pVHL E3 ubiquitin ligase complex.Regulation of HIF by the von Hippel-Lindau tumour suppressor: implications for cellular oxygen sensing.Tumor hypoxia induces nuclear paraspeckle formation through HIF-2α dependent transcriptional activation of NEAT1 leading to cancer cell survival.Destruction of a distal hypoxia response element abolishes trans-activation of the PAG1 gene mediated by HIF-independent chromatin looping.High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq.Regulation of HIF: prolyl hydroxylases.miR-210 is a target of hypoxia-inducible factors 1 and 2 in renal cancer, regulates ISCU and correlates with good prognosis.Cellular oxygen sensing in health and disease.Hypoxia, Hypoxia-inducible Transcription Factors, and Renal Cancer.Genome-wide association of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha DNA binding with expression profiling of hypoxia-inducible transcripts.Clinical features of the pathogenic m.5540G>A mitochondrial transfer RNA tryptophan gene mutation.Iron homeostasis and its interaction with prolyl hydroxylases.Integrated analysis of microRNA and mRNA expression and association with HIF binding reveals the complexity of microRNA expression regulation under hypoxia.Extensive regulation of the non-coding transcriptome by hypoxia: role of HIF in releasing paused RNApol2.Pan-genomic binding of hypoxia-inducible transcription factors.Multiple renal cancer susceptibility polymorphisms modulate the HIF pathway.Capture-C reveals preformed chromatin interactions between HIF-binding sites and distant promotersCommon genetic variants at the 11q13.3 renal cancer susceptibility locus influence binding of HIF to an enhancer of cyclin D1 expression.Regulation of type II transmembrane serine proteinase TMPRSS6 by hypoxia-inducible factors: new link between hypoxia signaling and iron homeostasis.Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha.Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases.Genetic evidence of a precisely tuned dysregulation in the hypoxia signaling pathway during oncogenesis.Genetic variation at the 8q24.21 renal cancer susceptibility locus affects HIF binding to a MYC enhancer.Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiationHypoxic regulation of the noncoding genome and NEAT1.Analogues of dealanylalahopcin are inhibitors of human HIF prolyl hydroxylases.2-oxoglutarate analogue inhibitors of HIF prolyl hydroxylase.Tumor hypoxia induces nuclear paraspeckle formation through HIF-2α dependent transcriptional activation of NEAT1 leading to cancer cell survival.Unlocking the complexity of hypoxia non-coding transcriptome landscape of breast cancer.Regulation of growth differentiation factor 15 expression by intracellular iron.The SIN3A histone deacetylase complex is required for a complete transcriptional response to hypoxia.Postprandial alkaline tide: does it exist?Hypoxia-inducible factors: where, when and why?Regulation of hepcidin expression at high altitudeUnlocking the complexity of hypoxia non-coding transcriptome landscape of breast cancer
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
David Robert Mole
@ast
David Robert Mole
@en
David Robert Mole
@es
David Robert Mole
@nl
David Robert Mole
@sl
type
label
David Robert Mole
@ast
David Robert Mole
@en
David Robert Mole
@es
David Robert Mole
@nl
David Robert Mole
@sl
prefLabel
David Robert Mole
@ast
David Robert Mole
@en
David Robert Mole
@es
David Robert Mole
@nl
David Robert Mole
@sl
P106
P21
P31
P496
0000-0002-0984-300X