High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq.

By Johannes Schödel, S. Oikonomopoulos, Jiannis Ragoussis, C. Pugh, P. Ratcliffe, D. Mole. Blood, 2011

724 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a81273549ea8dd5ce13cf6344d59d6dbd3b3cba8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. S. Påhlman
2. C. Wigerup
3. D. Bexell
4. Cormac T. Taylor
5. V. Haase
6. J. Espinosa
7. V. L. Dengler
8. M. Galbraith

In Molecular Biology

1. S. Påhlman
2. C. Wigerup
3. D. Bexell
4. J. Espinosa
5. V. L. Dengler
6. M. Galbraith
7. V. Haase
8. Cormac T. Taylor

Citations in the corpus

• Regulation of pyruvate metabolism and human disease (2013, background): “In regards to pyruvate metabolism, HIF1 regulates factors involved in glycolysis as well as PDK1, MCT4, and LDHA [150, 151].”
• Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy (2012, background): “at least 1 out of every 30 human genes)[6, 7].”
• Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer. (2016, methodology): “cipitation followed by next-generation high-throughput sequencing (ChIP-seq) showed that HIF binding sites exist outside of promoter sequences and that HIF binds to other sites as well as the core A/GCGTG motif (Schodel et al., 2011).”
• HIF-1 mediates metabolic responses to intratumoral hypoxia and oncogenic mutations. (2013, neutral): “Because the battery of genes that is activated by HIF-1 and HIF-2 in response to hypoxia is unique within each cell, the number of HIF target genes, which currently exceeds 1,000, continues to increase as new cell types are analyzed by ChIP techniques such as ChIP-chip (11, 12) and ChIP-seq (13).”
• Regulation of erythropoiesis by hypoxia-inducible factors (2013, background): “While hypoxic suppression of certain genes has been found to be associated with HIF-1 and/or HIF-2 activation, it is unlikely that HIF acts as a direct transcriptional repressor.(63) Under normoxia, all three HIF α-subunits are targeted for rapid proteasomal degradation by the von Hippel–Lindau tumo”
• Regulation of glycolysis by the hypoxia‐inducible factor (HIF): implications for cellular physiology (2020, background): “RNAs, including coding RNAs such as messenger RNA (mRNA) and non-coding RNAs such as microRNA (miRNA), are heavily regulated by hypoxia in a HIF-dependent manner (Schodel et al. 2011; Choudhry et al. 2014).”
• Transcriptional Regulation by Hypoxia Inducible Factors (2013, background): “Although the HRE consensus sequence is highly abundant across the genome, less than 1% of potential sites are bound by HIFs in response to hypoxia, as demonstrated by a number of recent genomewide analyses of HIF chromatin occupancy (Mole et al., 2009; Schödel et al., 2011,2013; Xia & Kung, 2009).”