High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
Open accessAbstract
Hypoxia-inducible factor (HIF) regulates the major transcriptional cascade central to the response of all mammalian cells to alterations in oxygen tension. Expression arrays indicate that many hundreds of genes are regulated by this pathway, controlling diverse processes that in turn orchestrate both oxygen delivery and utilization. However, the extent to which HIF exerts direct versus indirect control over gene expression together with the factors dictating the range of HIF-regulated genes remains unclear. Using chromatin immunoprecipitation linked to high throughput sequencing, we identify HIF-binding sites across the genome, independently of gene architecture. Using gene set enrichment analysis, we demonstrate robust associations with the regulation of gene expression by HIF, indicating that these sites operate over long genomic intervals. Analysis of HIF-binding motifs demonstrates sequence preferences outside of the core RCGTG-binding motif but does not reveal any additional absolute sequence requirements. Across the entire genome, only a small proportion of these potential binding sites are bound by HIF, although occupancy of potential sites was enhanced approximately 20-fold at normoxic DNAse1 hypersensitivity sites (irrespective of distance from promoters), suggesting that epigenetic regulation of chromatin may have an important role in defining the response to hypoxia.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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.
“A study using chromatin immunoprecipitation 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).”
From Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer (2016) · cites this paper as Schodel et al., 2011
The Results report many ChIP-seq HIF-binding sites outside promoter regions. They also report sequence preferences flanking the core RCGTG motif and enrichment of an AP-1-like motif in HIF-binding regions. They do not establish that HIF binds an alternative motif instead of the core motif, as the citing sentence may imply. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe global architecture of HIF-1- and HIF-2-dependent target gene networks remains largely conserved across different cell types.
“Notwithstanding these distinctions, the global architecture of HIF-1- and HIF-2-dependent target gene networks remains largely conserved across different cell types [7,66,68,70]”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [68]
The Discussion (page unavailable) suggests that isoform-specific HIF-binding patterns might extend across cell types and reports some overlap in binding sites between cell types. It does not establish that the global architecture of HIF-1- and HIF-2-dependent target gene networks remains largely conserved; the cross-cell comparison found 42% promoter-site and 36% promoter-distant-site overlap. (LLM, conf=0.85)
Experimental — accuracy not yet measuredFor HIF-2α, as many as 70% of the identified HIF-2 binding sites lay outside promoter regions.
“This was particularly true for HIF-2α, for which as many as 70% of the identified HIF-2 binding sites lay outside promoter regions.”
From Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer (2016) · cites this paper as Schodel et al., 2011
Promoter-proximal HIF-1 binding correlates with a higher transcript abundance.
“Promoter-proximal HIF-1 binding correlates with a higher transcript abundance [68,71,79,82]”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [68]
Most functional HREs reside within open chromatin, and HIF-1 preferentially binds promoter-proximal regions, whereas HIF-2 more frequently occupies distal enhancers.
“Most functional HREs reside within open chromatin [68,80,81] and HIF-1 preferentially binds promoter-proximal regions, whereas HIF-2 more frequently occupies distal enhancers”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [68]
Within the nucleus, transcriptionally active HIF heterodimers bind hypoxia-responsive elements (HREs) containing an asymmetric E-box core motif (RCGTG, where R = A or G).
“Within the nucleus, transcriptionally active HIF heterodimers bind hypoxia-responsive elements (HREs) containing an asymmetric E-box core motif (RCGTG, where R = A or G) [68,76]”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [68]
In the nucleus, HIF-α subunits dimerize with ARNT and bind to hypoxia-responsive elements in target genes to activate gene transcription by recruiting transcriptional coactivators including p300/CBP.
“In the nucleus, HIF-α subunits dimerize with aryl hydrocarbon receptor nuclear translocator (ARNT) and bind to hypoxia-responsive elements in target genes to activate gene transcription by recruiting transcriptional coactivators including p300/CBP”
From Hypoxic control of metastasis (2016) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625 · see citing works
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197 · see citing works
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Sequence logos: a new way to display consensus sequences
Schneider, T. D., & Stephens, R. M. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.20.6097 · Cited by 3,354 · see citing works
Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.
Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251 · see citing works
Self-citationSemenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617 · see citing works
Oxygen sensing by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068 · see citing works
Self-citationAn oestrogen-receptor-α-bound human chromatin interactome
Fullwood, M. J., Liu, M. H., Pan, Y. F., Liu, J., Han, X., Mohamed, Y. B., Orlov, Y. L., Velkov, S., Ho, A., Poh, H. M., et al. (2009) · Nature · doi:10.1038/nature08497 · Cited by 1,728 · see citing works
Hypoxia signalling in cancer and approaches to enforce tumour regression
Pouysségur, J., Dayan, F., & Mazure, N. M. (2006) · Nature · doi:10.1038/nature04871 · Cited by 1,676 · see citing works
Sequencing of 50 Human Exomes Reveals Adaptation to High Altitude
Yi, X., Liang, Y., Huerta-Sanchez, E., Jin, X., Cuo, Z. X. P., Pool, J. E., Xu, X., Jiang, H., Vinckenbosch, N., Korneliussen, T. S., et al. (2010) · Science · doi:10.1126/science.1190371 · Cited by 1,611 · see citing works
GSEA-P : a desktop application for Gene Set Enrichment Analysis
Subramanian, A., Kuehn, H., Gould, J., Tamayo, P., & Mesirov, J. P. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm369 · Cited by 1,380 · see citing works
The impact of O2 availability on human cancer
Bertout, J. A., Patel, S. A., & Simon, M. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2540 · Cited by 1,365 · see citing works
Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
Manalo, D. J., Rowan, A., Lavoie, T., Natarajan, L., Kelly, B. D., Ye, S. Q., Garcia, J. G. N., & Semenza, G. L. (2005) · Blood · doi:10.1182/blood-2004-07-2958 · Cited by 1,154 · see citing works
Integration of Oxygen Signaling at the Consensus HRE
Wenger, R. H., Stiehl, D. P., & Camenisch, G. (2005) · Science's STKE · doi:10.1126/stke.3062005re12 · Cited by 1,032 · see citing works
Semenza, G. L., Nejfelt, M. K., Chi, S. M., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5680 · Cited by 990 · see citing works
Chromatin accessibility pre-determines glucocorticoid receptor binding patterns
John, S., Sabo, P. J., Thurman, R. E., Sung, M.-H., Biddie, S. C., Johnson, T. A., Hager, G. L., & Stamatoyannopoulos, J. A. (2011) · Nature Genetics · doi:10.1038/ng.759 · Cited by 954 · see citing works
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447-5454.1992 · Cited by 951 · see citing works
Beall, C. M., Cavalleri, G. L., Deng, L., Elston, R. C., Gao, Y., Knight, J., Li, C., Li, J. C., Liang, Y., McCormack, M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002443107 · Cited by 845 · see citing works
Covello, K. L., Kehler, J., Yu, H., Gordan, J. D., Arsham, A. M., Hu, C., Labosky, P. A., Simon, M. C., & Keith, B. (2006) · Genes & Development · doi:10.1101/gad.1399906 · Cited by 818 · see citing works
The von Hippel–Lindau tumour suppressor protein: O2 sensing and cancer
Kaelin, W. G. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2502 · Cited by 729 · see citing works
An integrated software system for analyzing ChIP-chip and ChIP-seq data
Ji, H., Jiang, H., Ma, W., Johnson, D. S., Myers, R., & Wong, W. H. (2008) · Nature Biotechnology · doi:10.1038/nbt.1505 · Cited by 716 · see citing works
Semenza, G. L. (2007) · Science · doi:10.1126/science.1147949 · Cited by 706 · see citing works
HIF-1α induces cell cycle arrest by functionally counteracting Myc
Koshiji, M., Kageyama, Y., Pete, E. A., Horikawa, I., Barrett, J. C., & Huang, L. E. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600196 · Cited by 652 · see citing works
Mole, D. R., Blancher, C., Copley, R. R., Pollard, P. J., Gleadle, J. M., Ragoussis, J., & Ratcliffe, P. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901790200 · Cited by 552 · see citing works
Self-citationDisruption of oxygen homeostasis underlies congenital Chuvash polycythemia
Ang, S. O., Chen, H., Hirota, K., Gordeuk, V. R., Jelinek, J., Guan, Y., Liu, E., Sergueeva, A. I., Miasnikova, G. Y., Mole, D., et al. (2002) · Nature Genetics · doi:10.1038/ng1019 · Cited by 510 · see citing works
Self-citationHIF-α effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma
Gordan, J. D., Lal, P., Dondeti, V. R., Letrero, R., Parekh, K. N., Oquendo, C. E., Greenberg, R. A., Flaherty, K. T., Rathmell, W. K., Keith, B., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.10.016 · Cited by 493 · see citing works
Elvidge, G. P., Glenny, L., Appelhoff, R. J., Ratcliffe, P. J., Ragoussis, J., & Gleadle, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511408200 · Cited by 464 · see citing works
Self-citationXia, X., Lemieux, M. E., Li, W., Carroll, J. S., Brown, M., Liu, X. S., & Kung, A. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810067106 · Cited by 410 · see citing works
HIF-1α Induces Genetic Instability by Transcriptionally Downregulating MutSα Expression
Koshiji, M., To, K. K.-W., Hammer, S., Kumamoto, K., Harris, A. L., Modrich, P., & Huang, L. E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.015 · Cited by 346 · see citing works
Inhibition of Prolyl Hydroxylases Increases Erythropoietin Production in ESRD
Bernhardt, W. M., Wiesener, M. S., Scigalla, P., Chou, J., Schmieder, R. E., Günzler, V., & Eckardt, K.-U. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010010116 · Cited by 340 · see citing works
Krieg, A. J., Rankin, E. B., Chan, D., Razorenova, O., Fernandez, S., & Giaccia, A. J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00444-09 · Cited by 334 · see citing works
A Gain-of-Function Mutation in the <i>HIF2A</i> Gene in Familial Erythrocytosis
Percy, M. J., Furlow, P. W., Lucas, G. S., Li, X., Lappin, T. R. J., McMullin, M. F., & Lee, F. S. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa073123 · Cited by 314 · see citing works
Genome-scale mapping of DNase I sensitivity in vivo using tiling DNA microarrays
Sabo, P. J., Kuehn, M. S., Thurman, R. E., Johnson, B., Johnson, E. M., Cao, H., Yu, M., Rosenzweig, E., Goldy, J., Haydock, A. K., et al. (2006) · Nature Methods · doi:10.1038/nmeth890 · Cited by 314 · see citing works
Wang, V., Davis, D. A., Haque, M., Huang, E. L., & Yarchoan, R. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4130 · Cited by 309 · see citing works
Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure
Minamishima, Y. A., Moslehi, J., Bardeesy, N., Cullen, D., Bronson, R. T., & Kaelin, W. G. (2008) · Blood · doi:10.1182/blood-2007-10-117812 · Cited by 294 · see citing works
Hu, C., Iyer, S. R., Sataur, A., Covello, K. L., Chodosh, L. A., & Simon, M. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.9.3514-3526.2006 · Cited by 267 · see citing works
Pescador, N., Cuevas, Y., Suárez, S. N., Alcaide, M., Villar, D., Landázuri, M. O., & del Peso, L. (2005) · Biochemical Journal · doi:10.1042/bj20042121 · Cited by 240 · see citing works
Miyazaki, K., Kawamoto, T., Tanimoto, K., Nishiyama, M., Honda, H., & Kato, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204938200 · Cited by 227 · see citing works
CisModule: De novo discovery of cis-regulatory modules by hierarchical mixture modeling
Zhou, Q., & Wong, W. H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402858101 · Cited by 216 · see citing works
Ortiz-Barahona, A., Villar, D., Pescador, N., Amigo, J., & del Peso, L. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1205 · Cited by 202 · see citing works
Hsieh, M. M., Linde, N. S., Wynter, A., Metzger, M., Wong, C., Langsetmo, I., Lin, A., Smith, R., Rodgers, G. P., Donahue, R. E., et al. (2007) · Blood · doi:10.1182/blood-2007-02-073254 · Cited by 171 · see citing works
Hypoxia Induces Transcription Factor ETS-1 via the Activity of Hypoxia-Inducible Factor-1
Oikawa, M., Abé, M., Kurosawa, H., Hida, W., Shirato, K., & Sato, Y. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5927 · Cited by 161 · see citing works
DNA binding and protein interactions of the AHR/ARNT heterodimer that facilitate gene activation.
Swanson, H. I. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00066-2 · Cited by 158 · see citing works
Discovery of functional noncoding elements by digital analysis of chromatin structure
Sabo, P. J., Hawrylycz, M., Wallace, J. C., Humbert, R., Yu, M., Shafer, A., Kawamoto, J., Hall, R., Mack, J., Dorschner, M. O., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407387101 · Cited by 139 · see citing works
Oxygen‐dependent regulation of hypoxia‐inducible factors by prolyl and asparaginyl hydroxylation
Lando, D., Gorman, J. J., Whitelaw, M. L., & Peet, D. J. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03445.x · Cited by 138 · see citing works
Xia, X., & Kung, A. L. (2009) · Genome biology · doi:10.1186/gb-2009-10-10-r113 · Cited by 132 · see citing works
The response of c-Jun/AP-1 to chronic hypoxia is hypoxia-inducible factor 1α dependent
Laderoute, K. R., Calaoagan, J. M., Gustafson-Brown, C., Knapp, A. M., Li, G.-C., Mendonca, H. L., Ryan, H. E., Wang, Z., & Johnson, R. S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2515-2523.2002 · Cited by 105 · see citing works
Lau, K. W., Tian, Y.-M., Raval, R. R., Ratcliffe, P. J., & Pugh, C. W. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603675 · Cited by 104 · see citing works
Self-citationJi, H., Vokes, S. A., & Wong, W. H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl803 · Cited by 69 · see citing works
Pugh, C. W., Ebert, B. L., Ebrahim, O., & Ratcliffe, P. J. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90289-5 · Cited by 45 · see citing works
Self-citationChoi, S., Oh, H., & Park, H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06686.x · Cited by 23 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Hypoxia-inducible factors in physiology and medicine
Semenza, G. L. (2012) · Cell · doi:10.1016/j.cell.2012.01.021 · Cited by 3,645 · see citing works
HIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progression
Keith, B., Johnson, R. S., & Simon, M. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3183 · Cited by 1,693 · see citing works
Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy
Semenza, G. L. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.01.005 · Cited by 1,514 · see citing works
Rankin, E. B., & Giaccia, A. J. (2016) · Science · doi:10.1126/science.aaf4405 · Cited by 1,340 · see citing works
HIF-1 mediates metabolic responses to intratumoral hypoxia and oncogenic mutations
Semenza, G. L. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67230 · Cited by 1,335 · see citing works
ERK signalling: A master regulator of cell behaviour, life and fate
Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185 · see citing works
Oxygen Sensing, Hypoxia-Inducible Factors, and Disease Pathophysiology
Semenza, G. L. (2013) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104720 · Cited by 1,159 · see citing works
Regulation of glycolysis by the hypoxia-inducible factor (HIF): Implications for cellular physiology
Kierans, S. J., & Taylor, C. T. (2021) · The Journal of Physiology · doi:10.1113/jp280572 · Cited by 1,015 · see citing works
Regulation of pyruvate metabolism and human disease
Gray, L. R., Tompkins, S. C., & Taylor, E. B. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1539-2 · Cited by 951 · see citing works
Advances in Hypoxia-Inducible Factor Biology
Choudhry, H., & Harris, A. L. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.005 · Cited by 873 · see citing works
Regulation of erythropoiesis by hypoxia-inducible factors
Haase, V. H. (2013) · Blood Reviews · doi:10.1016/j.blre.2012.12.003 · Cited by 787 · see citing works
VHL, the story of a tumour suppressor gene
Gossage, L., Eisen, T. G., & Maher, E. R. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3844 · Cited by 777 · see citing works
Transcriptional regulation by hypoxia inducible factors
Dengler, V. L., Galbraith, M. D., & Espinosa, J. M. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.838205 · Cited by 774 · see citing works
Hypoxia and Metabolic Adaptation of Cancer Cells
Eales, K. L., Hollinshead, K. E. R., & Tennant, D. A. (2016) · Oncogenesis · doi:10.1038/oncsis.2015.50 · Cited by 724 · see citing works
Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer
Wigerup, C., Påhlman, S., & Bexell, D. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.04.009 · Cited by 687 · see citing works
“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).”
BackgroundMethodCellular mechanotransduction in health and diseases: from molecular mechanism to therapeutic targets
Di, X., Gao, X., Peng, L., Ai, J., Jin, X., Qi, S., Li, H., Wang, K., & Luo, D. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01501-9 · Cited by 660 · see citing works
Mitochondrial composition and function under the control of hypoxia
Fuhrmann, D. C., & Brüne, B. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.012 · Cited by 646 · see citing works
Hypoxia-Inducible Factor 1 and Cardiovascular Disease
Semenza, G. L. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170322 · Cited by 608 · see citing works
Zimna, A., & Kurpisz, M. (2015) · BioMed Research International · doi:10.1155/2015/549412 · Cited by 604 · see citing works
Hypoxia-inducible factors: cancer progression and clinical translation
Wicks, E. E., & Semenza, G. L. (2022) · Journal of Clinical Investigation · doi:10.1172/jci159839 · Cited by 600 · see citing works
The LINK-A lncRNA activates normoxic HIF1α signalling in triple-negative breast cancer
Lin, A., Li, C., Xing, Z., Hu, Q., Liang, K., Han, L., Wang, C., Hawke, D. H., Wang, S., Zhang, Y., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3295 · Cited by 561 · see citing works
Zheng, L., Kelly, C. J., & Colgan, S. P. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00191.2015 · Cited by 489 · see citing works
Hypoxia, Hypoxia-inducible Transcription Factors, and Renal Cancer
Schödel, J., Grampp, S., Maher, E. R., Moch, H., Ratcliffe, P. J., Russo, P., & Mole, D. R. (2015) · European Urology · doi:10.1016/j.eururo.2015.08.007 · Cited by 411 · see citing works
Self-citationShalova, I. N., Lim, J. Y., Chittezhath, M., Zinkernagel, A. S., Beasley, F. C., Hernández-Jiménez, E., Toledano, V., Cubillos‐Zapata, C., Rapisarda, A., Chen, J., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.001 · Cited by 412 · see citing works
Redox control of inflammation in macrophages
Brüne, B., Dehne, N., Grossmann, N., Jung, M., Namgaladze, D., Schmid, T., von Knethen, A., & Weigert, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4785 · Cited by 377 · see citing works
Human high-altitude adaptation: forward genetics meets the HIF pathwayPreprint
Bigham, A. W., & Lee, F. S. (2014) · Genes & Development · doi:10.1101/gad.250167.114 · Cited by 350 · see citing works
Regulation of Metabolism by Hypoxia-Inducible Factor 1
Semenza, G. L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010678 · Cited by 342 · see citing works
Keeley, T. P., & Mann, G. E. (2019) · Physiological Reviews · doi:10.1152/physrev.00041.2017 · Cited by 329 · see citing works
Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis
Liu, Q., Davidoff, O., Niss, K., & Haase, V. H. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63924 · Cited by 328 · see citing works
Gameiro, P. A., Yang, J., Metelo, A. M., Pérez-Carro, R., Baker, R., Wang, Z., Arreola, A., Rathmell, W. K., Olumi, A., López-Larrubia, P., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.002 · Cited by 325 · see citing works
Choudhry, H., Albukhari, A., Morotti, M., Haider, S. A., Moralli, D., Smythies, J., Schödel, J., Green, C., Camps, C., Buffa, F. M., et al. (2014) · Oncogene · doi:10.1038/onc.2014.378 · Cited by 317 · see citing works
Self-citationAllosteric inhibition of hypoxia inducible factor-2 with small molecules
Scheuermann, T. H., Li, Q., Ma, H.-W., Key, J., Zhang, L., Chen, R., Garcia, J. A., Naidoo, J., Longgood, J., Frantz, D. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1185 · Cited by 315 · see citing works
Anaemia in kidney disease: harnessing hypoxia responses for therapy
Koury, M. J., & Haase, V. H. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.82 · Cited by 313 · see citing works
Mechanisms of hypoxia signalling: new implications for nephrology
Schödel, J., & Ratcliffe, P. J. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0182-z · Cited by 309 · see citing works
Self-citationTime of exercise specifies the impact on muscle metabolic pathways and systemic energy homeostasis
Sato, S., Basse, A. L., Schönke, M., Chen, S., Samad, M., Altıntaş, A., Laker, R. C., Dalbram, E., Barrès, R., Baldi, P., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.03.013 · Cited by 298 · see citing works
Oxygen sensing and hypoxia signalling pathways in animals: The implications of physiology for cancer
Ratcliffe, P. J. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.251470 · Cited by 294 · see citing works
Self-citationPharmacologic Targeting of Hypoxia-Inducible Factors
Semenza, G. L. (2019) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021637 · Cited by 288 · see citing works
HIF prolyl hydroxylase inhibitors for the treatment of renal anaemia and beyond
Maxwell, P. H., & Eckardt, K. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.193 · Cited by 286 · see citing works
Role of hypoxia-inducible factors in breast cancer metastasis
Gilkes, D. M., & Semenza, G. L. (2013) · Future Oncology · doi:10.2217/fon.13.92 · Cited by 274 · see citing works
Weisel, F. J., Mullett, S. J., Elsner, R. A., Menk, A. V., Trivedi, N. H., Luo, W., Wikenheiser, D. J., Hawse, W. F., Chikina, M. D., Smita, S., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0598-4 · Cited by 274 · see citing works
Wu, Q., Zhou, W., Yin, S., Zhou, Y., Chen, T., Qian, J., Su, R., Hong, L., Lu, H., Zhang, F., et al. (2019) · Hepatology · doi:10.1002/hep.30593 · Cited by 268 · see citing works
Broekgaarden, M., Weijer, R., van Gulik, T. M., Hamblin, M. R., & Heger, M. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9588-7 · Cited by 261 · see citing works
An Overview: The Diversified Role of Mitochondria in Cancer Metabolism
Liu, Y., Sun, Y., Guo, Y., Shi, X., Chen, X., Feng, W., Wu, L., Zhang, J., Yu, S., Wang, Y., et al. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.81609 · Cited by 260 · see citing works
Mimura, I., Nangaku, M., Kanki, Y., Tsutsumi, S., Inoue, T., Kohro, T., Yamamoto, S., Fujita, T., Shimamura, T., Suehiro, J.-I., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06643-11 · Cited by 251 · see citing works
The Roles of Hypoxia Signaling in the Pathogenesis of Cardiovascular Diseases
Abe, H., Semba, H., & Takeda, N. (2017) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.rv17009 · Cited by 237 · see citing works
McNamee, E. N., Korns Johnson, D., Homann, D., & Clambey, E. T. (2013) · Immunologic Research · doi:10.1007/s12026-012-8349-8 · Cited by 234 · see citing works
Regulatory mechanisms of hypoxia‐inducible factor 1 activity: Two decades of knowledge
Koyasu, S., Kobayashi, M., Gotö, Y., Hiraoka, M., & Harada, H. (2017) · Cancer Science · doi:10.1111/cas.13483 · Cited by 226 · see citing works
Eisenreich, W., Rudel, T., Heesemann, J., & Goebel, W. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00042 · Cited by 218 · see citing works
Blair, J. D., Yuen, R. K. C., Lim, B., McFadden, D. E., von Dadelszen, P., & Robinson, W. P. (2013) · Molecular Human Reproduction · doi:10.1093/molehr/gat044 · Cited by 216 · see citing works
Slominski, A. T., Kim, T.-K., Brożyna, A. A., Janjetović, Z., Brooks, D. L. P., Schwab, L. P., Skobowiat, C., Jóźwicki, W., & Seagroves, T. N. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.06.030 · Cited by 204 · see citing works
Bartoszewski, R., Moszyńska, A., Serocki, M., Cabaj, A., Polten, A., Ochocka, R., Dell'Italia, L., Bartoszewska, S., Króliczewski, J., Dąbrowski, M., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201802650rr · Cited by 199 · see citing works
Inherent DNA‐binding specificities of the HIF‐1α and HIF‐2α transcription factors in chromatin
Smythies, J. A., Sun, M., Masson, N., Salama, R., Simpson, P. D., Murray, E., Neumann, V., Cockman, M. E., Choudhry, H., Ratcliffe, P. J., et al. (2019) · The EMBO Reports · doi:10.15252/embr.201846401 · Cited by 195 · see citing works
Self-citationLiver Regeneration after Hepatectomy and Partial Liver Transplantation
Yagi, S., Hirata, M., Miyachi, Y., & Uemoto, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218414 · Cited by 192 · see citing works
Suppression of PGC-1α Is Critical for Reprogramming Oxidative Metabolism in Renal Cell Carcinoma
LaGory, E. L., Wu, C., Taniguchi, C. M., Ding, C. C., Chi, J., von Eyben, R., Scott, D. A., Richardson, A. D., & Giaccia, A. J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.006 · Cited by 191 · see citing works
Metabolic adaptation of cancer and immune cells mediated by hypoxia-inducible factors
Samanta, D., & Semenza, G. L. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.002 · Cited by 190 · see citing works
Brooks, D. L. P., Schwab, L. P., Krutilina, R. I., Parke, D. N., Sethuraman, A., Hoogewijs, D., Schörg, A., Gotwald, L., Fan, M., Wenger, R. H., et al. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0510-x · Cited by 190 · see citing works
Simon, J. M., Hacker, K. E., Singh, D., Brannon, A. R., Parker, J. S., Weiser, M., Ho, T. H., Kuan, P.-F., Jonasch, E., Furey, T. S., et al. (2013) · Genome Research · doi:10.1101/gr.158253.113 · Cited by 189 · see citing works
Uterine bleeding: how understanding endometrial physiology underpins menstrual health
Jain, V., Chodankar, R. R., Maybin, J. A., & Critchley, H. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00629-4 · Cited by 188 · see citing works
Endothelial HIF-2 mediates protection and recovery from ischemic kidney injury
Kapitsinou, P. P., Sano, H., Michael, M., Kobayashi, H., Davidoff, O., Bian, A., Yao, B., Zhang, M.-Z., Harris, R. C., Duffy, K. J., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69073 · Cited by 187 · see citing works
Stegen, S., van Gastel, N., Eelen, G., Ghesquière, B., D’Anna, F., Thienpont, B., Goveia, J., Torrekens, S., Looveren, R. V., Luyten, F. P., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.01.002 · Cited by 187 · see citing works
Hypoxia-Inducible Factor Activators in Renal Anemia: Current Clinical Experience
Sanghani, N. S., & Haase, V. H. (2019) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2019.04.004 · Cited by 187 · see citing works
New horizons in hypoxia signaling pathways
Pugh, C. W., & Ratcliffe, P. J. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.008 · Cited by 186 · see citing works
Self-citationMiranda, E., Nordgren, I. K., Male, A. L., Lawrence, C. E., Hoakwie, F., Cuda, F., Court, W., Fox, K. R., Townsend, P. A., Packham, G. K., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja402993u · Cited by 185 · see citing works
Up-regulation of glycolytic metabolism is required for HIF1α-driven bone formation
Regan, J. N., Lim, J., Shi, Y., Joeng, K. S., Arbeit, J. M., Shohet, R. V., & Long, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324290111 · Cited by 182 · see citing works
The role of hypoxia in inflammatory disease (Review)
Biddlestone, J., Bandarra, D., & Rocha, S. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2079 · Cited by 178 · see citing works
Von Hippel–Lindau disease: insights into oxygen sensing, protein degradation, and cancer
Kaelin, W. G. (2022) · Journal of Clinical Investigation · doi:10.1172/jci162480 · Cited by 178 · see citing works
From oxygen to erythropoietin: Relevance of hypoxia for retinal development, health and disease
Caprara, C., & Grimm, C. (2012) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2011.11.003 · Cited by 176 · see citing works
Hypoxia-Inducible Factor Signaling in Pheochromocytoma: Turning the Rudder in the Right Direction
Jochmanová, I., Yang, C., Zhuang, Z., & Pacák, K. (2013) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djt201 · Cited by 173 · see citing works
The Distinct Role of HIF-1α and HIF-2α in Hypoxia and Angiogenesis
Bakleh, M. Z., & Zen, A. A. H. (2025) · Cells · doi:10.3390/cells14090673 · Cited by 171 · see citing works
HIF Hydroxylase Pathways in Cardiovascular Physiology and Medicine
Bishop, T., & Ratcliffe, P. J. (2015) · Circulation Research · doi:10.1161/circresaha.117.305109 · Cited by 169 · see citing works
Self-citationDifferential but complementary HIF1α and HIF2α transcriptional regulation
Downes, N. L., Laham-Karam, N., Kaikkonen, M. U., & Ylä-Herttuala, S. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.05.004 · Cited by 166 · see citing works
TET1-Mediated Hydroxymethylation Facilitates Hypoxic Gene Induction in Neuroblastoma
Mariani, C. J., Vasanthakumar, A., Madžo, J., Yesilkanal, A. E., Bhagat, T. D., Yu, Y., Bhattacharyya, S., Wenger, R. H., Cohn, S. L., Nanduri, J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.040 · Cited by 165 · see citing works
Choudhry, H., Schödel, J., Oikonomopoulos, S., Camps, C., Grampp, S., Harris, A. L., Ratcliffe, P. J., Ragoussis, J., & Mole, D. R. (2013) · EMBO Reports · doi:10.1002/embr.201337642 · Cited by 165 · see citing works
Self-citationKuiper, C., & Vissers, M. C. M. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00359 · Cited by 163 · see citing works
HIF‐prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism
Haase, V. H. (2017) · Hemodialysis International · doi:10.1111/hdi.12567 · Cited by 161 · see citing works
Schödel, J., Bardella, C., Sciesielski, L. K., Brown, J. M., Pugh, C. W., Buckle, V. J., Tomlinson, I. P. M., Ratcliffe, P. J., & Mole, D. R. (2012) · Nature Genetics · doi:10.1038/ng.2204 · Cited by 157 · see citing works
Self-citationSun, Y., Chen, W., Torphy, R. J., Yao, S., Zhu, G., Lin, R., Lugano, R., Miller, E. N., Fujiwara, Y., Bian, L., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abc8922 · Cited by 159 · see citing works
Camps, C., Saini, H. K., Mole, D. R., Choudhry, H., Reczko, M., Guerra‐Assunção, J. A., Tian, Y., Buffa, F. M., Harris, A. L., Hatzigeorgiou, A. G., et al. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-28 · Cited by 156 · see citing works
Self-citationDown-Regulation ofEPAS1Transcription and Genetic Adaptation of Tibetans to High-Altitude Hypoxia
Peng, Y., Cui, C., He, Y., Ouzhuluobu, Zhang, H., Yang, D., Zhang, Q., Bianbazhuoma, Yang, L., He, Y., et al. (2016) · Molecular Biology and Evolution · doi:10.1093/molbev/msw280 · Cited by 156 · see citing works
da Motta, L. L., Ledaki, I., Purshouse, K. R., Haider, S. A., Bastiani, M. A. D., Baban, D., Morotti, M., Steers, G., Wigfield, S., Bridges, E., et al. (2016) · Oncogene · doi:10.1038/onc.2016.184 · Cited by 154 · see citing works
Hypoxia-Driven Effects in Cancer: Characterization, Mechanisms, and Therapeutic Implications
Shi, R., Liao, C., & Zhang, Q. H. (2021) · Cells · doi:10.3390/cells10030678 · Cited by 148 · see citing works
An overview of transcriptional regulation in response to toxicological insult
Jennings, P., Limonciel, A., Felice, L., & Leonard, M. O. (2012) · Archives of Toxicology · doi:10.1007/s00204-012-0919-y · Cited by 144 · see citing works
Voellenkle, C., García-Manteiga, J. M., Pedrotti, S., Perfetti, A., Toma, I. D., Silva, D. D., Maimone, B., Greco, S., Fasanaro, P., Creo, P., et al. (2016) · Scientific Reports · doi:10.1038/srep24141 · Cited by 141 · see citing works
Hypoxia and cellular metabolism in tumour pathophysiology
Parks, S. K., Cormerais, Y., & Pouysségur, J. (2017) · The Journal of Physiology · doi:10.1113/jp273309 · Cited by 141 · see citing works
Karuppagounder, S. S., Alim, I., Khim, S. J., Bourassa, M. W., Sleiman, S. F., John, R., Thinnes, C. C., Yeh, T.-L., Demetriades, M., Neitemeier, S., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aac6008 · Cited by 141 · see citing works
Hypoxia Inducible Factor Pathway Inhibitors as Anticancer Therapeutics
Burroughs, S. K., Kaluz, S., Wang, D., Wang, K., Van Meir, E. G., & Wang, B. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.17 · Cited by 140 · see citing works
Yang, J., AlTahan, A. M., Jones, D. T., Buffa, F. M., Bridges, E., Interiano, R. B., Qu, C., Vogt, N., Li, J., Baban, D. F., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422015112 · Cited by 139 · see citing works
Self-citationDevelopment of Inhibitors of the PAS-B Domain of the HIF-2α Transcription Factor
Rogers, J. L., Bayeh, L., Scheuermann, T. H., Longgood, J. C., Key, J., Naidoo, J., Melito, L. M., Shokri, C., Frantz, D. E., Bruick, R. K., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301847z · Cited by 139 · see citing works
Halle, C., Andersen, E. K. F., Lando, M., Aarnes, E., Hasvold, G., Holden, M., Syljuåsen, R. G., Sundfør, K., Kristensen, G. B., Holm, R., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1085 · Cited by 138 · see citing works
Biochemical Underpinnings of Immune Cell Metabolic Phenotypes
Olenchock, B. A., Rathmell, J. C., & Heiden, M. G. V. (2017) · Immunity · doi:10.1016/j.immuni.2017.04.013 · Cited by 136 · see citing works
Transcriptional Response to Hypoxia: The Role of HIF-1-Associated Co-Regulators
Yfantis, A., Mylonis, I., Chachami, G., Nikolaidis, M., Amoutzias, G. D., Paraskeva, E., & Simos, G. (2023) · Cells · doi:10.3390/cells12050798 · Cited by 136 · see citing works
Hypoxia-Inducible Factor-1: A Critical Player in the Survival Strategy of Stressed Cells
Chen, S., & Sang, N. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25283 · Cited by 135 · see citing works
The Genomics and Genetics of Oxygen Homeostasis
Semenza, G. L. (2020) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-111119-073356 · Cited by 134 · see citing works
Hypoxia-induced switch in SNAT2/SLC38A2 regulation generates endocrine resistance in breast cancer
Morotti, M., Bridges, E., Valli, A., Choudhry, H., Sheldon, H., Wigfield, S., Gray, N., Zois, C. E., Grimm, F., Jones, D., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818521116 · Cited by 131 · see citing works
Kapitsinou, P. P., Rajendran, G., Astleford, L., Michael, M., Schonfeld, M. P., Fields, T. A., Shay, S. D., French, J. L., West, J. D., & Haase, V. H. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.01055-15 · Cited by 131 · see citing works
Physiology and pathophysiology of renal erythropoietin-producing cells
Shih, H., Wu, C., & Lin, S. (2018) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2018.03.017 · Cited by 131 · see citing works
Hypoxia Promotes the Production and Inhibits the Destruction of Human Articular Cartilage
Thoms, B. L., Dudek, K., Lafont, J. E., & Murphy, C. L. (2013) · Arthritis & Rheumatism · doi:10.1002/art.37867 · Cited by 130 · see citing works
Xu, M., Pang, Q., Shengquan, X., Ye, C., Lei, R. L., Shen, Y., & Xu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.23225 · Cited by 128 · see citing works
The HIF target MAFF promotes tumor invasion and metastasis through IL11 and STAT3 signaling
Moon, E. J., Mello, S. S., Li, C. G., Chi, J., Thakkar, K. N., Kirkland, J. G., LaGory, E. L., Lee, I. J., Diep, A. N., Miao, Y. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24631-6 · Cited by 128 · see citing works
- Authors
- Schödel, J., Oikonomopoulos, S., Ragoussis, J., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R.
- Affiliations
- University of Oxford (GB)
- Centre for Human Genetics (GB)
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2011-06-09
- Volume
- 117
- Issue
- 23
- Pages
- e207-e217
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC3374576
- OpenAlex
- W1969734439
- Cited by
- 724
- References
- 50
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 32 · 2023: 43 · 2022: 63 · 2021: 72 · 2020: 62 · 2019: 55 · 2018: 45 · 2017: 52 · 2016: 56 · 2015: 44 · 2014: 50 · 2013: 61 · 2012: 22
- FWCI
- 15.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (090532)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- hypoxia-inducible factor, transcriptional regulation, hypoxia response, oxygen partial pressure, chromatin accessibility, epigenetic regulation, gene set enrichment analysis, sequence motifs
- MeSH terms
- Chromosome Mapping, Female, Humans, Oxygen, Genome, Human, Response Elements, Epigenesis, Genetic, Cell Line, Tumor, Chromatin Immunoprecipitation, Basic Helix-Loop-Helix Proteins, Genome-Wide Association Study
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
