Oxygen‐sensing mechanisms in cells

Chromatin modifications and their function

Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works

Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1

Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836 · see citing works

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O ₂ -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · see citing works

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O ₂ Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · see citing works

The Role of Chromatin during Transcription

Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,503 · see citing works

Dynamic RNA Modifications in Gene Expression Regulation

Roundtree, I. A., Evans, M., Pan, T., & He, C. (2017) · Cell · doi:10.1016/j.cell.2017.05.045 · Cited by 3,459 · see citing works

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333 · 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

A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617 · see citing works

A conserved family of prolyl-4-hydroxylases that modify HIF

Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549 · see citing works

Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification

Ito, S., D’Alessio, A. C., Taranova, O., Hong, K., Sowers, L. C., & Zhang, Y. (2010) · Nature · doi:10.1038/nature09303 · Cited by 2,542 · see citing works

Integrating cell-signalling pathways with NF-κB and IKK function

Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350 · see citing works

The diverse roles of DNA methylation in mammalian development and disease

Greenberg, M., & Bourc’his, D. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0159-6 · Cited by 2,160 · 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

30 Years of NF-κB: A Blossoming of Relevance to Human Pathobiology

Zhang, Q., Lenardo, M. J., & Baltimore, D. (2017) · Cell · doi:10.1016/j.cell.2016.12.012 · Cited by 1,979 · see citing works

Chromatin accessibility and the regulatory epigenome

Klemm, S. L., Shipony, Z., & Greenleaf, W. J. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-018-0089-8 · Cited by 1,793 · see citing works

TET-mediated active DNA demethylation: mechanism, function and beyond

Wu, X., & Zhang, Y. (2017) · Nature Reviews Genetics · doi:10.1038/nrg.2017.33 · Cited by 1,661 · see citing works

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550 · see citing works

The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate-Dependent Nucleic Acid Demethylase

Gerken, T., Girard, C. A. J., Tung, Y. L., Webby, C. J., Saudek, V., Hewitson, K. S., Yeo, G. S. H., McDonough, M. A., Cunliffe, S. L., McNeill, L. A., et al. (2007) · Science · doi:10.1126/science.1151710 · Cited by 1,519 · see citing works

Pyruvate Kinase M2 Is a PHD3-Stimulated Coactivator for Hypoxia-Inducible Factor 1

Luo, W., Hu, H., Chang, R., Zhong, J., Knabel, M., O'Meally, R., Cole, R. N., Pandey, A., & Semenza, G. L. (2011) · Cell · doi:10.1016/j.cell.2011.03.054 · Cited by 1,463 · see citing works

m 6 A Demethylase ALKBH5 Maintains Tumorigenicity of Glioblastoma Stem-like Cells by Sustaining FOXM1 Expression and Cell Proliferation Program

Zhang, S., Zhao, B. S., Zhou, A., Lin, K., Zheng, S., Lu, Z., Chen, Y., Sulman, E. P., Xie, K., Bögler, O., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.02.013 · Cited by 1,453 · see citing works

FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity

Mahon, P. C., Hirota, K., & Semenza, G. L. (2001) · Genes & Development · doi:10.1101/gad.924501 · Cited by 1,385 · see citing works

HIF prolyl‐hydroxylase 2 is the key oxygen sensor setting low steady‐state levels of HIF‐1α in normoxia

Berra, E., Benizri, E., Ginouvès, A., Volmat, V., Roux, D., & Pouysségur, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg392 · Cited by 1,348 · see citing works

Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension

Jiang, B. H., Semenza, G. L., Bauer, C., & Marti, H. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.4.c1172 · Cited by 1,213 · see citing works

Differential Function of the Prolyl Hydroxylases PHD1, PHD2, and PHD3 in the Regulation of Hypoxia-inducible Factor

Appelhoff, R. J., Tian, Y.-M., Raval, R. R., Turley, H., Harris, A. L., Pugh, C. W., Ratcliffe, P. J., & Gleadle, J. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406026200 · Cited by 1,108 · see citing works

Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation

Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5197 · Cited by 1,014 · see citing works

Hypoxia induces the breast cancer stem cell phenotype by HIF-dependent and ALKBH5-mediated m 6 A-demethylation of NANOG mRNA

Zhang, C., Samanta, D., Lu, H., Bullen, J. W., Zhang, H., Chen, I., He, X., & Semenza, G. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602883113 · Cited by 977 · see citing works

The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing

De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., & Natoli, G. (2007) · Cell · doi:10.1016/j.cell.2007.08.019 · Cited by 965 · see citing works

Regulation of nucleosome dynamics by histone modifications

Zentner, G. E., & Henikoff, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2470 · Cited by 923 · see citing works

Molecular mechanisms and potential functions of histone demethylases

Kooistra, S. M., & Helin, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3327 · Cited by 882 · see citing works

HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation

Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181341498 · Cited by 796 · see citing works

Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

Hirsilä, M., Koivunen, P., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304982200 · Cited by 794 · see citing works

Prolyl hydroxylase-1 negatively regulates IκB kinase-β, giving insight into hypoxia-induced NFκB activity

Cummins, E. P., Berra, E., Comerford, K. M., Ginouves, A., Fitzgerald, K. T., Seeballuck, F., Godson, C., Nielsen, J. E., Moynagh, P., Pouyssegur, J., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602235103 · Cited by 788 · see citing works

Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

Min, J.-H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.1073440 · Cited by 765 · see citing works

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751 · see citing works

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y.-M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200273200 · Cited by 719 · see citing works

Expression switching in the stevor and Pfmc‐2TM superfamilies in Plasmodium falciparum

Lavazec, C., Sanyal, S., & Templeton, T. J. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05767.x · Cited by 659 · see citing works

Mechanisms and Functions of ATP-Dependent Chromatin-Remodeling Enzymes

Narlikar, G. J., Sundaramoorthy, R., & Owen‐Hughes, T. (2013) · Cell · doi:10.1016/j.cell.2013.07.011 · Cited by 659 · see citing works

Tumour hypoxia causes DNA hypermethylation by reducing TET activity

Thienpont, B., Steinbacher, J., Zhao, H., D’Anna, F., Kuchnio, A., Ploumakis, A., Ghesquière, B., Van Dyck, L., Boeckx, B., Schoonjans, L., et al. (2016) · Nature · doi:10.1038/nature19081 · Cited by 635 · see citing works

Hypoxia induces accumulation of p53 protein, but activation of a G1-phase checkpoint by low-oxygen conditions is independent of p53 status.

Graeber, T. G., Peterson, J., Tsai, M., Monica, K., Fornace, A. J., & Giaccia, A. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.6264 · Cited by 613 · see citing works

Stabilization of HIF-1α is critical to improve wound healing in diabetic mice

Botusan, I. R., Sunkari, V. G., Savu, O., Catrina, A. I., Grünler, J., Lindberg, S., Pereira, T., Ylä-Herttuala, S., Poellinger, L., Brismar, K., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805230105 · Cited by 533 · see citing works

Arterial Blood Gases and Oxygen Content in Climbers on Mount Everest

Grocott, M. P. W., Martín, D., Levett, D. Z. H., McMorrow, R., Windsor, J. S., & Montgomery, H. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0801581 · Cited by 527 · see citing works

Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism

Aragonés, J., Schneider, M. A., Geyte, K. V., Fraisl, P., Dresselaers, T., Mazzone, M., Dirkx, R., Zacchigna, S., Lemieux, H., Jeoung, N. H., et al. (2008) · Nature Genetics · doi:10.1038/ng.2007.62 · Cited by 472 · see citing works

HIGH ALTITUDE INCREASES CIRCULATING INTERLEUKIN-6, INTERLEUKIN-1 RECEPTOR ANTAGONIST AND C-REACTIVE PROTEIN

Hartmann, G., Tschöp, M. H., Fischer, R., Bidlingmaier, C., Riepl, R. L., Tschöp, K., Hautmann, H., Endres, S., & Toepfer, M. (2000) · Cytokine · doi:10.1006/cyto.1999.0533 · Cited by 470 · see citing works

Hypoxia-responsive transcription factors

Cummins, E. P., & Taylor, C. T. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1413-7 · Cited by 462 · see citing works

Ubiquitin-mediated activation of TAK1 and IKK

Adhikari, A., Xu, M., & Chen, Z. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210413 · Cited by 455 · see citing works

Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

Koivunen, P., Hirsilä, M., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312254200 · Cited by 447 · see citing works

Histone demethylase KDM6A directly senses oxygen to control chromatin and cell fate

Chakraborty, A. A., Laukka, T., Myllykoski, M., Ringel, A. E., Booker, M. A., Tolstorukov, M. Y., Meng, Y. J., Meier, S. R., Jennings, R. B., Creech, A. L., et al. (2019) · Science · doi:10.1126/science.aaw1026 · Cited by 432 · see citing works

Oxidative demethylation of 3‐methylthymine and 3‐methyluracil in single‐stranded DNA and RNA by mouse and human FTO

Jia, G., Yang, C., Yang, S., Jian, X., Yi, C., Zhou, Z., & He, C. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.08.019 · Cited by 424 · see citing works

Placental but Not Heart Defects Are Associated with Elevated Hypoxia-Inducible Factor α Levels in Mice Lacking Prolyl Hydroxylase Domain Protein 2

Takeda, K., Ho, V. C., Takeda, H., Duan, L.-J., Nagy, A., & Fong, G.-H. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00425-06 · Cited by 401 · see citing works

Inhibition of 2-oxoglutarate dependent oxygenases

Rose, N. R., McDonough, M. A., King, O. N. F., Kawamura, A., & Schofield, C. J. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00203h · Cited by 395 · see citing works

Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α

Elkins, J. M., Hewitson, K. S., McNeill, L. A., Seibel, J. F., Schlemminger, I., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200644200 · Cited by 391 · see citing works

The VHL/HIF axis in clear cell renal carcinoma

Shen, C., & Kaelin, W. G. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.06.001 · Cited by 387 · see citing works

Hypoxia induces rapid changes to histone methylation and reprograms chromatin

Batie, M., Frost, J., Frost, M., Wilson, J. W., Schofield, P., & Rocha, S. (2019) · Science · doi:10.1126/science.aau5870 · Cited by 385 · see citing works

NF ‐κB and HIF crosstalk in immune responses

D’Ignazio, L., Bandarra, D., & Rocha, S. (2015) · FEBS Journal · doi:10.1111/febs.13578 · Cited by 367 · see citing works

Targeting hypoxia signalling for the treatment of ischaemic and inflammatory diseases

Eltzschig, H. K., Bratton, D. L., & Colgan, S. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4422 · Cited by 363 · see citing works

The Histone Demethylases JMJD1A and JMJD2B Are Transcriptional Targets of Hypoxia-inducible Factor HIF

Beyer, S., Kristensen, M. M., Jensen, K. S., Johansen, J. V., & Staller, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804578200 · Cited by 341 · see citing works

Regulation of the Histone Demethylase JMJD1A by Hypoxia-Inducible Factor 1α Enhances Hypoxic Gene Expression and Tumor Growth

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

The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators

Hu, R., Sheng, J., Qi, X., Xu, Z., Takahashi, T. T., & Varshavsky, A. J. (2005) · Nature · doi:10.1038/nature04027 · Cited by 316 · see citing works

Adora2b-elicited Per2 stabilization promotes a HIF-dependent metabolic switch crucial for myocardial adaptation to ischemia

Eckle, T., Hartmann, K., Bonney, S., Reithel, S., Mittelbronn, M., Walker, L. A., Lowes, B. D., Han, J., Borchers, C. H., Buttrick, P. M., et al. (2012) · Nature Medicine · doi:10.1038/nm.2728 · Cited by 314 · 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

Fumarate and Succinate Regulate Expression of Hypoxia-inducible Genes via TET Enzymes

Laukka, T., Mariani, C. J., Ihantola, T., Cao, J. Z., Hokkanen, J., Kaelin, W. G., Godley, L. A., & Koivunen, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.688762 · Cited by 307 · see citing works

Histone variants: dynamic punctuation in transcriptionPreprint

Weber, C. M., & Henikoff, S. (2014) · Genes & Development · doi:10.1101/gad.238873.114 · Cited by 297 · see citing works

Oral Hypoxia–Inducible Factor Prolyl Hydroxylase Inhibitor Roxadustat (FG-4592) for the Treatment of Anemia in Patients with CKD

Provenzano, R., Besarab, A., Sun, C. H., Diamond, S. A., Durham, J. H., Cangiano, J. L., Aiello, J. R., Novak, J. E., Lee, T. T., Leong, R., et al. (2016) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.06890615 · Cited by 295 · see citing works

Catecholamines, Cardiac β-Adrenergic Receptors, and Heart Failure

Lefkowitz, R. J., Rockman, H. A., & Koch, W. J. (2000) · Circulation · doi:10.1161/01.cir.101.14.1634 · Cited by 291 · see citing works

Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

Cockman, M. E., Lancaster, D. E., Stolze, I. P., Hewitson, K. S., McDonough, M. A., Coleman, M. L., Coles, C. H., Yu, X., Hay, R. T., Ley, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606877103 · Cited by 285 · see citing works

Multiple Splice Variants of the Human HIF-3α Locus Are Targets of the von Hippel-Lindau E3 Ubiquitin Ligase Complex

Maynard, M. A., Qi, H., Chung, J., Lee, E. H. L., Kondo, Y., Hara, S., Conaway, R. C., Conaway, J. W., & Ohh, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208681200 · Cited by 283 · see citing works

Regulation of NF-κB by NSD1/FBXL11-dependent reversible lysine methylation of p65

Lu, T., Jackson, M. W., Wang, B., Yang, M., Chance, M. R., Miyagi, M., Gudkov, A. V., & Stark, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912493107 · Cited by 281 · see citing works

Inhibition of Hypoxia Inducible Factor Hydroxylases Protects Against Renal Ischemia-Reperfusion Injury

Hill, P., Shukla, D., Tran, M. G. B., Aragonés, J., Cook, H. T., Carmeliet, P., & Maxwell, P. H. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006090998 · Cited by 280 · see citing works

The EGLN-HIF O 2 -Sensing System: Multiple Inputs and Feedbacks

Ivan, M., & Kaelin, W. G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.002 · Cited by 273 · see citing works

The human side of hypoxia‐inducible factor

Smith, T. G., Robbins, P. A., & Ratcliffe, P. J. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07029.x · Cited by 264 · see citing works

Regulation of gene expression by hypoxia

Kenneth, N. S., & Rocha, S. (2008) · Biochemical Journal · doi:10.1042/bj20081055 · Cited by 264 · see citing works

Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins

Takeda, K., Aguila, H. L., Parikh, N. S., Li, X., Lamothe, K., Duan, L.-J., Takeda, H., Lee, F. S., & Fong, G.-H. (2008) · Blood · doi:10.1182/blood-2007-09-114561 · Cited by 263 · see citing works

Plasmodium falciparum var gene expression is developmentally controlled at the level of RNA polymerase II‐mediated transcription initiation

Kyes, S., Christodoulou, Z., Pinches, R. A., Kriek, N., Horrocks, P., & Newbold, C. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05587.x · Cited by 257 · see citing works

Hypoxia induces a novel signature of chromatin modifications and global repression of transcription

Johnson, A. B., Denko, N., & Barton, M. C. (2008) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2008.01.001 · Cited by 250 · see citing works

Protein Hydroxylation by Hypoxia-Inducible Factor (HIF) Hydroxylases: Unique or Ubiquitous?

Strowitzki, M. J., Cummins, E. P., & Taylor, C. T. (2019) · Cells · doi:10.3390/cells8050384 · Cited by 248 · see citing works

Inflammation and Hypoxia: HIF and PHD Isoform Selectivity

Watts, E., & Walmsley, S. R. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.10.006 · Cited by 236 · see citing works

Mechanism of Hypoxia-Induced NF-κB

Culver, C. A., Sundqvist, A., Mudie, S., Melvin, A., Xirodimas, D. P., & Rocha, S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00409-10 · Cited by 229 · see citing works

Histone demethylase JMJD2C is a coactivator for hypoxia-inducible factor 1 that is required for breast cancer progression

Luo, W., Chang, R., Zhong, J., Pandey, A., & Semenza, G. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217394109 · Cited by 228 · see citing works

Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay

Ehrismann, D., Flashman, E., Genn, D. N., Mathioudakis, N., Hewitson, K. S., Ratcliffe, P. J., & Schofield, C. J. (2007) · Biochemical Journal · doi:10.1042/bj20061151 · Cited by 225 · see citing works

Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants

Masson, N., Keeley, T. P., Giuntoli, B., White, M. D., Lavilla-Puerta, M., Pierdomenico Perata, A., Hopkinson, R. J., Flashman, E., Licausi, F., & Ratcliffe, P. J. (2019) · Science · doi:10.1126/science.aaw0112 · Cited by 224 · see citing works

Human Cep192 Is Required for Mitotic Centrosome and Spindle Assembly

Gómez-Ferrerı́a, M. A., Rath, U., Buster, D. W., Chanda, S. K., Caldwell, J. S., Rines, D. R., & Sharp, D. J. (2007) · Current Biology · doi:10.1016/j.cub.2007.10.019 · Cited by 222 · see citing works

Hypoxic Stress Induces Dimethylated Histone H3 Lysine 9 through Histone Methyltransferase G9a in Mammalian Cells

Chen, H., Yan, Y., Davidson, T. L., Shinkai, Y., & Costa, M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0101 · Cited by 222 · see citing works

Gene regulation under low oxygen: holding your breath for transcription

Rocha, S. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.06.005 · Cited by 219 · see citing works

Oxygen-dependent ATF-4 stability is mediated by the PHD3 oxygen sensor

Köditz, J., Nesper, J., Wottawa, M., Stiehl, D. P., Camenisch, G., Franke, C., Myllyharju, J., Wenger, R. H., & Katschinski, D. M. (2007) · Blood · doi:10.1182/blood-2007-06-094441 · Cited by 214 · see citing works

NF-κB Suppression by the Deubiquitinating Enzyme Cezanne

Enesa, K., Zakkar, M., Chaudhury, H., Luong, L. A., Rawlinson, L. M., Mason, J. C., Haskard, D. O., Dean, J. L. E., & Evans, P. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708690200 · Cited by 213 · see citing works

The role of p53 in hypoxia-induced apoptosis

Hammond, E. M., & Giaccia, A. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.154 · Cited by 208 · see citing works

Hypoxia and Inflammation in Cancer, Focus on HIF and NF-κB

D’Ignazio, L., Batie, M., & Rocha, S. (2017) · Biomedicines · doi:10.3390/biomedicines5020021 · Cited by 206 · see citing works

Methylation: lost in hydroxylation?

Trewick, S. C., McLaughlin, P., & Allshire, R. C. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400379 · Cited by 205 · see citing works

pVHL suppresses kinase activity of Akt in a proline-hydroxylation–dependent manner

Guo, J., Chakraborty, A. A., Liu, P., Gan, W., Zheng, X., Inuzuka, H., Wang, B., Zhang, J., Zhang, L., Yuan, M., et al. (2016) · Science · doi:10.1126/science.aad5755 · Cited by 205 · see citing works

The Mammalian SPD-2 Ortholog Cep192 Regulates Centrosome Biogenesis

Zhu, F., Lawo, S., Bird, A., Pinchev, D., Ralph, A., Richter, C., Müller‐Reichert, T., Kittler, R., Hyman, A. A., & Pelletier, L. (2008) · Current Biology · doi:10.1016/j.cub.2007.12.055 · Cited by 195 · see citing works

HIF-1 expression in healing wounds: HIF-1α induction in primary inflammatory cells by TNF-α

Albina, J. E., Mastrofrancesco, B., Vessella, J. A., Louis, C. A., Henry, W. L., & Reichner, J. S. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.6.c1971 · Cited by 192 · see citing works

Regulation of IL-1β-induced NF-κB by hydroxylases links key hypoxic and inflammatory signaling pathways

Scholz, C. C., Cavadas, M. A. S., Tambuwala, M. M., Hams, E., Rodríguez, J., Kriegsheim, A. V., Cotter, P., Bruning, U., Fallon, P. G., Cheong, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309718110 · Cited by 186 · see citing works

Mammalian <i>EGLN</i> genes have distinct patterns of mRNA expression and regulation

Lieb, M. E., Menzies, K., Moschella, M. C., Ni, R., & Taubman, M. B. (2002) · Biochemistry and Cell Biology · doi:10.1139/o02-115 · Cited by 186 · see citing works

Abnormal Sympathoadrenal Development and Systemic Hypotension in PHD3−/− Mice

Bishop, T., Gallagher, D., Pascual, A., Lygate, C. A., de Bono, J. P., Nicholls, L. G., Ortega‐Sáenz, P., Oster, H., Wijeyekoon, B., Sutherland, A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02041-07 · Cited by 181 · 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

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

Disturbed hypoxic responses as a pathogenic mechanism of diabetic foot ulcers

Catrina, S., & Zheng, X. (2015) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2742 · Cited by 164 · see citing works

Epigenetic Regulation by Histone Demethylases in Hypoxia

Hancock, R. L., Dunne, K., Walport, L. J., Flashman, E., & Kawamura, A. (2015) · Epigenomics · doi:10.2217/epi.15.24 · Cited by 162 · see citing works

Prolyl Hydroxylase-3 Is Down-regulated in Colorectal Cancer Cells and Inhibits IKKβ Independent of Hydroxylase Activity

Xue, J., Li, X., Jiao, S., Wei, Y., Wu, G., & Fang, J. S. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.09.049 · Cited by 150 · see citing works

Oxygen-Regulated β 2 -Adrenergic Receptor Hydroxylation by EGLN3 and Ubiquitylation by pVHL

Xie, L., Xiao, K., Whalen, E. J., Forrester, M. T., Freeman, R. S., Fong, G., Gygi, S. P., Lefkowitz, R. J., & Stamler, J. S. (2009) · Science Signaling · doi:10.1126/scisignal.2000444 · Cited by 148 · see citing works

Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation.

Alarcon, R. M., Koumenis, C., Geyer, R. K., Maki, C. G., & Giaccia, A. J. (1999) · PubMed · Cited by 143 · see citing works

Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase

Zhou, X., Sun, H., Chen, H., Zavadil, J., Kluz, T., Arita, A., & Costa, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2942 · Cited by 134 · see citing works

Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity

Tausendschön, M., Dehne, N., & Brüne, B. (2011) · Cytokine · doi:10.1016/j.cyto.2010.11.002 · Cited by 132 · see citing works

Prolyl hydroxylation by EglN2 destabilizes FOXO3a by blocking its interaction with the USP9x deubiquitinasePreprint

Chen, X., Zhai, B., Koivunen, P., Shin, S. J., Lü, G., Liu, J., Geisen, C., Chakraborty, A. A., Moslehi, J. J., Smalley, D. M., et al. (2014) · Genes & Development · doi:10.1101/gad.242131.114 · Cited by 128 · see citing works

Cell cycle progression in response to oxygen levels

Ortmann, B. M., Druker, J., & Rocha, S. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1645-9 · Cited by 121 · see citing works

Synergistic effect of HIF-1α gene therapy and HIF-1-activated bone marrow-derived angiogenic cells in a mouse model of limb ischemia

Rey, S., Lee, K., Wang, C. J., Gupta, K., Chen, S., McMillan, A., Bhise, N. S., Levchenko, A., & Semenza, G. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911921106 · Cited by 120 · see citing works

Replication Stress and Chromatin Context Link ATM Activation to a Role in DNA Replication

Olcina, M. M., Foskolou, I. P., Anbalagan, S., Senra, J. M., Pires, I. M., Jiang, Y., Ryan, A. J., & Hammond, E. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.019 · Cited by 110 · see citing works

N 6 -methyladenosine is required for the hypoxic stabilization of specific mRNAs

Fry, N. J., Law, B. A., Ilkayeva, O., Holley, C. L., & Mansfield, K. D. (2017) · RNA · doi:10.1261/rna.061044.117 · Cited by 110 · see citing works

Novel Erythropoiesis-Stimulating Agents

Macdougall, I. C. (2007) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.03840907 · Cited by 109 · see citing works

Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates

Cockman, M. E., Lippl, K., Tian, Y., Pegg, H. B., Figg, W. D., Abboud, M. I., Heilig, R., Fischer, R., Myllyharju, J., Schofield, C. J., et al. (2019) · eLife · doi:10.7554/elife.46490 · Cited by 101 · see citing works

Chromatin and oxygen sensing in the context of JmjC histone demethylases

Shmakova, A., Batie, M., Druker, J., & Rocha, S. (2014) · Biochemical Journal · doi:10.1042/bj20140754 · Cited by 99 · see citing works

2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process

Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99 · see citing works

Cezanne (OTUD7B) regulates HIF‐1α homeostasis in a proteasome‐independent manner

Bremm, A., Moniz, S., Mader, J. K., Rocha, S., & Komander, D. (2014) · EMBO Reports · doi:10.15252/embr.201438850 · Cited by 97 · see citing works

Substrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways

Rodríguez, J., Pilkington, R., Muñoz, A. G., Nguyen, L. K., Rauch, N., Kennedy, S. A., Monsefi, N., Herrero, A., Taylor, C. T., & von Kriegsheim, A. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.043 · Cited by 95 · see citing works

PHD1 Links Cell-Cycle Progression to Oxygen Sensing through Hydroxylation of the Centrosomal Protein Cep192

Moser, S. C., Bensaddek, D., Ortmann, B. M., Maure, J.-F., Mudie, S., Blow, J. J., Lamond, A. I., Swedlow, J. R., & Rocha, S. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.06.014 · Cited by 93 · see citing works

Hypoxia‐inducible factor stabilizers and other small‐molecule erythropoiesis‐stimulating agents in current and preventive doping analysis

Beuck, S., Schänzer, W., & Thevis, M. (2012) · Drug Testing and Analysis · doi:10.1002/dta.390 · Cited by 92 · see citing works

Kinetic Investigations of the Role of Factor Inhibiting Hypoxia-inducible Factor (FIH) as an Oxygen Sensor

Tarhonskaya, H., Hardy, A., Howe, E. A., Loik, N. D., Kramer, H., McCullagh, J., Schofield, C. J., & Flashman, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.653014 · Cited by 91 · see citing works

The Activity of JmjC Histone Lysine Demethylase KDM4A is Highly Sensitive to Oxygen Concentrations

Hancock, R. L., Masson, N., Dunne, K., Flashman, E., & Kawamura, A. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b00958 · Cited by 89 · see citing works

Hypoxia increases genome-wide bivalent epigenetic marking by specific gain of H3K27me3

Prickaerts, P., Adriaens, M. E., van den Beucken, T., Koch, E., Dubois, L. J., Dahlmans, V. E. H., Gits, C. M. M., Evelo, C. T., Chan‐Seng‐Yue, M., Wouters, B. G., et al. (2016) · Epigenetics & Chromatin · doi:10.1186/s13072-016-0086-0 · Cited by 87 · see citing works

The Factor Inhibiting HIF Asparaginyl Hydroxylase Regulates Oxidative Metabolism and Accelerates Metabolic Adaptation to Hypoxia

Sim, J., Cowburn, A. S., Palazón, A., Madhu, B., Tyrakis, P. A., Macías, D., Bargiela, D., Pietsch, S., Gralla, M., Evans, C. E., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.020 · Cited by 87 · see citing works

Therapeutic Manipulation of the HIF Hydroxylases

Nagel, S., Talbot, N. P., Mecinović, J., Smith, T. G., Buchan, A. M., & Schofield, C. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2711 · Cited by 77 · see citing works

PHD3-dependent hydroxylation of HCLK2 promotes the DNA damage response

Xie, L., Pi, X., Mishra, A., Fong, G., Peng, J., & Patterson, C. (2012) · Journal of Clinical Investigation · doi:10.1172/jci62374 · Cited by 74 · see citing works

Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology

Dao, J. H., Kurzeja, R. J. M., Morachis, J. M., Veith, H., Lewis, J. K., Yu, V. L., Tegley, C. M., & Tagari, P. C. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.09.052 · Cited by 71 · see citing works

Capture‐C reveals preformed chromatin interactions between HIF‐binding sites and distant promoters

Platt, J. L., Salama, R. A., Smythies, J., Choudhry, H., Davies, J. O. J., Hughes, J. R., Ratcliffe, P. J., & Mole, D. R. (2016) · EMBO Reports · doi:10.15252/embr.201642198 · Cited by 71 · see citing works

Hypoxia downregulates p53 but induces apoptosis and enhances expression of BAD in cultures of human syncytiotrophoblasts

Chen, B., Longtine, M. S., Sadovsky, Y., & Nelson, D. M. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00154.2010 · Cited by 64 · see citing works

Kinetic Analysis of Iron-Dependent Histone Demethylases: α-Ketoglutarate Substrate Inhibition and Potential Relevance to the Regulation of Histone Demethylation in Cancer Cells

Cascella, B., & Mirica, L. M. (2012) · Biochemistry · doi:10.1021/bi3012466 · Cited by 62 · see citing works

PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359

Rodríguez, J., Herrero, A., Li, S., Rauch, N., Quintanilla, A., Wynne, K. J., Krstić, A., Acosta, J. C., Taylor, C. T., Schlisio, S., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.108 · Cited by 62 · see citing works

Cezanne Regulates Inflammatory Responses to Hypoxia in Endothelial Cells by Targeting TRAF6 for Deubiquitination

Luong, L. A., Fragiadaki, M., Smith, J., Boyle, J., Lutz, J., Dean, J. L. E., Harten, S. K., Ashcroft, M. A., Walmsley, S. R., Haskard, D. O., et al. (2013) · Circulation Research · doi:10.1161/circresaha.111.300119 · Cited by 62 · see citing works

Cezanne regulates E2F1-dependent HIF2α expression

Moniz, S., Bandarra, D., Biddlestone, J., Campbell, K. J., Komander, D., Bremm, A., & Rocha, S. (2015) · Journal of Cell Science · doi:10.1242/jcs.168864 · Cited by 61 · see citing works

Differences in hydroxylation and binding of Notch and HIF-1α demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1)

Wilkins, S. E., Hyvärinen, J., Chicher, J., Gorman, J. J., Peet, D. J., Bilton, R. L., & Koivunen, P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.01.005 · Cited by 59 · see citing works

The Oxygen Sensor PHD2 Controls Dendritic Spines and Synapses via Modification of Filamin A

Segura, I., Lange, C. M., Knevels, E., Moskalyuk, A., Pulizzi, R., Eelen, G., Chaze, T., Tudor, C., Boulègue, C., Holt, M. G., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.047 · Cited by 59 · see citing works

Oral Delivery of Prolyl Hydroxylase Inhibitor

Marks, E., Goggins, B. J., Cardona, J., Cole, S., Minahan, K., Mateer, S. W., Walker, M. M., Shalwitz, R. A., & Keely, S. (2015) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000277 · Cited by 58 · see citing works

Investigations on the oxygen dependence of a 2-oxoglutarate histone demethylase

Sánchez‐Fernández, E. M., Tarhonskaya, H., Al‐Qahtani, K., Hopkinson, R. J., McCullagh, J., Schofield, C. J., & Flashman, E. (2012) · Biochemical Journal · doi:10.1042/bj20121155 · Cited by 55 · see citing works

Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen

Tarhonskaya, H., Chowdhury, R., Leung, I. K. H., Loik, N. D., McCullagh, J., Claridge, T. D. W., Schofield, C. J., & Flashman, E. (2014) · Biochemical Journal · doi:10.1042/bj20140779 · Cited by 54 · see citing works

Aptamer Technology: Adjunct Therapy for Malaria

Kamarudin, N. A. A. N., Mohammed, N., & Mustaffa, K. M. F. (2017) · Biomedicines · doi:10.3390/biomedicines5010001 · Cited by 54 · see citing works

KDM4A regulates HIF-1 levels through H3K9me3

Dobrynin, G., McAllister, T. E., Leszczyńska, K. B., Ramachandran, S., Krieg, A. J., Kawamura, A., & Hammond, E. M. (2017) · Scientific Reports · doi:10.1038/s41598-017-11658-3 · Cited by 50 · see citing works

Prolyl-4-hydroxylase Domain Protein 2 Controls NF-κB/p65 Transactivation and Enhances the Catabolic Effects of Inflammatory Cytokines on Cells of the Nucleus Pulposus

Li, J., Yuan, W., Jiang, S., Ye, W., Yang, H., Shapiro, I. M., & Risbud, M. V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611483 · Cited by 49 · see citing works

Hypoxia-Inducible Factor Prolyl 4-Hydroxylases and Metabolism

Koivunen, P., & Kietzmann, T. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.10.004 · Cited by 47 · see citing works

Hydroxylases as therapeutic targets in inflammatory bowel disease

Cummins, E. P., Doherty, G. A., & Taylor, C. T. (2013) · Laboratory Investigation · doi:10.1038/labinvest.2013.9 · Cited by 44 · see citing works

Mechanism of hypoxia-induced NFκB

Melvin, A., Mudie, S., & Rocha, S. (2011) · Cell Cycle · doi:10.4161/cc.10.6.14910 · Cited by 41 · see citing works

KDM2 Family Members are Regulated by HIF-1 in Hypoxia

Batie, M., Druker, J., D’Ignazio, L., & Rocha, S. (2017) · Cells · doi:10.3390/cells6010008 · Cited by 39 · see citing works

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling

Heir, P., Srikumar, T., Bikopoulos, G. J., Bunda, S., Poon, B., Lee, J. E., Raught, B., & Ohh, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.694562 · Cited by 36 · see citing works

Hypoxia-inducible factor prolyl-4-hydroxylase-1 is a convergent point in the reciprocal negative regulation of NF-κB and p53 signaling pathways

Ullah, K., Rosendahl, A.-H., Izzi, V., Bergmann, U., Pihlajaniemi, T. A., Mäki, J. M., & Myllyharju, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-17376-0 · Cited by 34 · see citing works

The role of hypoxia-inducible factor stabilizers in the treatment of anemia in patients with chronic kidney disease

Zhong, H., Zhou, T., Li, H., & Zhong, Z. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s175887 · Cited by 34 · see citing works

N6-methyladenosine contributes to cellular phenotype in a genetically-defined model of breast cancer progression

Fry, N. J., Law, B. A., Ilkayeva, O., Carraway, K., Holley, C. L., & Mansfield, K. D. (2018) · Oncotarget · doi:10.18632/oncotarget.25782 · Cited by 33 · see citing works

A cytosolic domain of the erythropoietin receptor contributes to endoplasmic reticulum‐associated degradation

Supino‐Rosin, L., Yoshimura, A., Altaratz, H., & Neumann, D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00516.x · Cited by 32 · see citing works

Grow₂: the HIF system, energy homeostasis and the cell cycle.

Moniz, S., Biddlestone, J., & Rocha, S. (2014) · PubMed · doi:10.14670/hh-29.10.589 · Cited by 30 · see citing works

A HIF-1α-driven feed-forward loop augments HIF signalling in Hep3B cells by upregulation of ARNT

Mandl, M., Lieberum, M.-K., & Depping, R. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.187 · Cited by 30 · see citing works

Lysine demethylase inhibition protects pancreatic β cells from apoptosis and improves β-cell function

Backe, M. B., Andersson, J., Bacos, K., Christensen, D. P., Hansen, J. B., Dorosz, J., Gajhede, M., Dahlby, T., Bysani, M., Kristensen, L. H., et al. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.07.001 · Cited by 28 · see citing works

Therapeutic inhibition of prolyl hydroxylase domain-containing enzymes in surgery: putative applications and challenges

Schneider, M., Harnoss, J. M., Strowitzki, M. J., Radhakrishnan, P., Platzer, L. K., Harnoss, J. C., Hank, T. P., Cai, J., & Ulrich, A. B. (2015) · Hypoxia · doi:10.2147/hp.s60872 · Cited by 26 · see citing works

Pharmacological prevention of acute mountain sickness. Many climbers and trekkers find acetazolamide 500 mg/day to be useful.

Bärtsch, P., & Schneider, M. (2001) · PubMed Central · Cited by 24 · see citing works

Histone modifiers are oxygen sensors

Gallipoli, P., & Huntly, B. J. P. (2019) · Science · doi:10.1126/science.aaw8373 · Cited by 24 · see citing works

Differential effect of hypoxia on etoposide‐induced DNA damage response and p53 regulation in different cell types

Sermeus, A., Rebucci, M., Fransolet, M., Flamant, L., Desmet, D., Delaive, E., Arnould, T., & Michiels, C. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24409 · Cited by 20 · see citing works

Regulation of histone demethylase KDM6B by hypoxia-inducible factor-2α

Guo, X., Tian, Z., Wang, X., Pan, S., Huang, W., Shen, Y., Gui, Y., Duan, X., & Cai, Z. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmu122 · Cited by 20 · see citing works

Pharmacological prevention of acute mountain sickness

Hackett, P. H. (2001) · BMJ · doi:10.1136/bmj.322.7277.48 · Cited by 19 · see citing works

Outpatient hysteroscopy versus day case hysteroscopy. What exactly is patient satisfaction?

Baker, R. (2001) · PubMed · Cited by 19 · see citing works

CDK-dependent phosphorylation of PHD1 on serine 130 alters its substrate preference in cells

Ortmann, B. M., Bensaddek, D., Carvalhal, S., Moser, S. C., Mudie, S., Griffis, E. R., Swedlow, J. R., Lamond, A. I., & Rocha, S. (2015) · Journal of Cell Science · doi:10.1242/jcs.179911 · Cited by 18 · see citing works

JmjC histone demethylases act as chromatin oxygen sensors

Batie, M., & Rocha, S. (2019) · Molecular & Cellular Oncology · doi:10.1080/23723556.2019.1608501 · Cited by 17 · see citing works

Chemical Basis for the Selectivity of the von Hippel Lindau Tumor Suppressor pVHL for Prolyl-Hydroxylated HIF-1α

Illingworth, C. J. R., Loenarz, C., Schofield, C. J., & Domene, C. (2010) · Biochemistry · doi:10.1021/bi100358t · Cited by 16 · see citing works

Therapeutic inhibition of prolyl hydroxylase domain-containing enzymes in surgery: putative applications and challenges

Harnoss, J. M., Strowitzki, M. J., Radhakrishnan, P., Platzer, L. K., Harnoss, J. C., Hank, T. P., Cai, J., Ulrich, A., & Schneider, M. (2015) · Dove Medical Press (Taylor and Francis Group) · Cited by 16 · see citing works

HIF stabilization by prolyl hydroxylase inhibitors for the treatment of anemia in chronic kidney disease

Wyatt, C. M., & Drüeke, T. B. (2016) · Kidney International · doi:10.1016/j.kint.2016.08.016 · Cited by 15 · see citing works

Structure-based drug design for hypoxia-inducible factor prolyl-hydroxylase inhibitors and its therapeutic potential for the treatment of erythropoiesis-stimulating agent-resistant anemia: raising expectations for exploratory clinical trials

Higashijima, Y., Tanaka, T., & Nangaku, M. (2013) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2013.796358 · Cited by 14 · see citing works

Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding

Mader, J. K., Huber, J., Bonn, F., Dötsch, V., Rogov, V. V., & Bremm, A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010315 · Cited by 13 · see citing works

RNAi-Based Identification of Gene-Specific Nuclear Cofactor Networks Regulating Interleukin-1 Target Genes

Meier‐Soelch, J., Jurida, L., Weber, A., Newel, D., Kim, J., Braun, T. W., Schmitz, M. L., & Kracht, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00775 · Cited by 11 · see citing works

When is a target not a target?

Bersten, D. C., & Peet, D. J. (2019) · eLife · doi:10.7554/elife.50585 · Cited by 6 · see citing works

Hypoxia makes its mark on histones

Strzyz, P. J. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0122-6 · Cited by 5 · see citing works

[Erratum

Melvin, A., Mudie, S., & Rocha, S. (2011) · Cell Cycle · doi:10.4161/cc.10.12.16720 · Cited by 3 · see citing works

Metabolic reprogramming, sensing, and cancer therapy

Mao, Y., Xia, Z., Xia, W., & Jiang, P. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115064 · Cited by 168 · 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

Seeing stars: Development and function of retinal astrocytes

Paisley, C. E., & Kay, J. N. (2021) · Developmental Biology · doi:10.1016/j.ydbio.2021.07.007 · Cited by 72 · see citing works

Hypoxia-inducible factor in cancer: from pathway regulation to therapeutic opportunity

Ortmann, B. M. (2024) · BMJ Oncology · doi:10.1136/bmjonc-2023-000154 · Cited by 67 · see citing works

Role of Hypoxia in the Control of the Cell Cycle

Druker, J., Wilson, J. W., Child, F., Shakir, D., Fasanya, T., & Rocha, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094874 · Cited by 62 · see citing works

The Role of Sumoylation in the Response to Hypoxia: An Overview

Filippopoulou, C., Simos, G., & Chachami, G. (2020) · Cells · doi:10.3390/cells9112359 · Cited by 56 · see citing works

Roxadustat: Not just for anemia

Zhu, X., Jiang, L., Wei, X. S., Long, M., & Du, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.971795 · Cited by 60 · see citing works

Regulation of chromatin accessibility by hypoxia and HIF

Batie, M., Frost, J., Shakir, D., & Rocha, S. (2022) · Biochemical Journal · doi:10.1042/bcj20220008 · Cited by 45 · see citing works

Searching for molecular hypoxia sensors among oxygen-dependent enzymes

Li, L., Shen, S. Q., Bickler, P. E., Jacobson, M. P., Wu, L. F., & Altschuler, S. J. (2023) · eLife · doi:10.7554/elife.87705 · Cited by 41 · see citing works

Clinical Pharmacokinetics and Pharmacodynamics of Roxadustat

Czock, D., & Keller, F. (2021) · Clinical Pharmacokinetics · doi:10.1007/s40262-021-01095-x · Cited by 45 · see citing works

Hydrogen: A Rising Star in Gas Medicine as a Mitochondria-Targeting Nutrient via Activating Keap1-Nrf2 Antioxidant System

Cheng, D., Long, J., Zhao, L., & Liu, J. (2023) · Antioxidants · doi:10.3390/antiox12122062 · Cited by 44 · see citing works

Epigenetic Regulation of Endothelial Dysfunction and Inflammation in Pulmonary Arterial Hypertension

Hudson, J., & Farkas, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212098 · Cited by 43 · see citing works

Roles of HIF and 2-Oxoglutarate-Dependent Dioxygenases in Controlling Gene Expression in Hypoxia

Frost, J., Frost, M. G., Batie, M., Jiang, H., & Rocha, S. (2021) · Cancers · doi:10.3390/cancers13020350 · Cited by 47 · see citing works

Intermittent hypoxia enhances the expression of hypoxia inducible factor HIF1A through histone demethylation

Martinez, C.-A., Jiramongkol, Y., Bal, N., Alwis, I. D., Nedoboy, P. E., Farnham, M. M. J., White, M. D., Cistulli, P. A., & Cook, K. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102536 · Cited by 36 · see citing works

HIF Prolyl Hydroxylase Inhibitors for COVID-19 Treatment: Pros and Cons

Poloznikov, A. A., Nersisyan, S. A., Hushpulian, D. M., Kazakov, E. H., Tonevitsky, A., Kazakov, S. V., Vechorko, V. I., Nikulin, S. V., Makarova, J. A., & Gazaryan, I. G. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.621054 · Cited by 27 · see citing works

Regulation of the HIF switch in human endothelial and cancer cells

Slawski, J., Jaśkiewicz, M., Barton, A., Kozioł, S., Collawn, J. F., & Bartoszewski, R. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151386 · Cited by 26 · see citing works

Osteoclasts adapt to physioxia perturbation through DNA demethylation

Nishikawa, K., Seno, S., Yoshihara, T., Narazaki, A., Sugiura, Y., Shimizu, R., Kikuta, J., Sakaguchi, R., Suzuki, N., Takeda, N., et al. (2021) · EMBO Reports · doi:10.15252/embr.202153035 · Cited by 24 · see citing works

Catabolism of Hydroxyproline in Vertebrates: Physiology, Evolution, Genetic Diseases and New siRNA Approach for Treatment

Belostotsky, R., & Frishberg, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23021005 · Cited by 25 · see citing works

Interplay between Hypoxia and Extracellular Vesicles in Cancer and Inflammation

Venturella, M., Criscuoli, M., Carraro, F., Naldini, A., & Zocco, D. (2021) · Biology · doi:10.3390/biology10070606 · Cited by 24 · see citing works

Oxidative Stress Response’s Kinetics after 60 Minutes at Different (30% or 100%) Normobaric Hyperoxia Exposures

Lévêque, C., Mrakic‐Sposta, S., Lafère, P., Vezzoli, A., Germonpré, P., Beer, A., Mievis, S., Virgili, F., Lambrechts, K., Theunissen, S., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010664 · Cited by 22 · see citing works

Functional crosstalk between chromatin and hypoxia signalling

Collier, H., Albanese, A., Kwok, C.-S., Kou, J., & Rocha, S. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110660 · Cited by 22 · see citing works

Specific inhibition of HIF activity: can peptides lead the way?

Mylonis, I., Chachami, G., & Simos, G. (2021) · Cancers · doi:10.3390/cancers13030410 · Cited by 21 · see citing works

Redox Imbalance in Neurological Disorders in Adults and Children

Rey, F., Berardo, C., Maghraby, E., Mauri, A., Messa, L., Esposito, L., Casili, G., Ottolenghi, S., Bonaventura, E., Cuzzocrea, S., et al. (2023) · Antioxidants · doi:10.3390/antiox12040965 · Cited by 23 · see citing works

Different dissolved oxygen effects on growth and O2-sensing pathway in juvenile bighead carp (Hypophthalmichthys nobilis)

Zhou, X., Wu, Y., Zhou, Y., Zhang, Z., Chen, G., Yu, X., & Tong, J. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740672 · Cited by 19 · see citing works

Physioxia-induced downregulation of Tet2 in hematopoietic stem cells contributes to enhanced self-renewal

Aljoufi, A., Zhang, C., Ropa, J. P., Chang, W., Palam, L. R., Cooper, S. H., Ramdas, B., Capitano, M. L., Broxmeyer, H. E., & Kapur, R. (2022) · Blood · doi:10.1182/blood.2022015499 · Cited by 17 · see citing works

Hydroxylation of the NOTCH1 intracellular domain regulates Notch signaling dynamics

Ferrante, F., Giaimo, B. D., Friedrich, T., Sugino, T., Mertens, D., Kugler, S. J., Gahr, B. M., Just, S., Pan, L., Bartkuhn, M., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05052-9 · Cited by 17 · see citing works

NF-κB is a central regulator of hypoxia-induced gene expression

Shakir, D., Batie, M., Kwok, C.-S., Cook, S. J., Kenneth, N. S., & Rocha, S. (2025) · EMBO Reports · doi:10.1038/s44319-025-00651-x · Cited by 18 · see citing works

Hypoxic regulation of extracellular vesicles: Implications for cancer therapy

Yoo, S., Choi, S., Kim, I., & Kim, I. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.09.034 · Cited by 15 · see citing works

Oxygen‐regulated post‐translation modifications as master signalling pathway in cells

Batie, M., Fasanya, T., Kenneth, N. S., & Rocha, S. (2023) · EMBO Reports · doi:10.15252/embr.202357849 · Cited by 22 · see citing works

Histone H3K4me3 breadth in hypoxia reveals endometrial core functions and stress adaptation linked to endometriosis

Rytkönen, K. T., Faux, T., Mahmoudian, M., Heinosalo, T., Nnamani, M. C., Perheentupa, A. H., POUTANEN, M. H., Elo, L. L., & Wagner, G. P. (2022) · iScience · doi:10.1016/j.isci.2022.104235 · Cited by 14 · see citing works

Hypoxic vasodilatory defect and pulmonary hypertension in mice lacking hemoglobin β-cysteine93 S-nitrosylation

Zhang, R., Hausladen, A., Qian, Z., Liao, X., Premont, R. T., & Stamler, J. S. (2021) · JCI Insight · doi:10.1172/jci.insight.155234 · Cited by 14 · see citing works

miR-451 protects against ischemic stroke by targeting Phd3

Wang, M., Bai, Y., Chi, H., Lin, P., Wu, Y., Cui, J., Wang, Y., Sun, J., & Lang, M. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113777 · Cited by 13 · see citing works

Evaluating Oxygen Tensions Related to Bone Marrow and Matrix for MSC Differentiation in 2D and 3D Biomimetic Lamellar Scaffolds

Sayın, E., Baran, E. T., Elsheikh, A., Mudera, V., Cheema, U., & Hasırcı, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084010 · Cited by 13 · see citing works

Exploring the pathogenesis of pulmonary vascular disease

EJIKEME, C. P., & Safdar, Z. (2024) · Frontiers in Medicine · doi:10.3389/fmed.2024.1402639 · Cited by 12 · see citing works

FG-4592 alleviates radiation-induced intestinal injury by facilitating recovery of intestinal stem cell and reducing damage of intestinal epithelial

Xia, P., Yang, Y., Liu, R., Feng, Z., Lin, Y., Tang, H., Du, J., Cheng, Y., Cai, J., Hu, H., et al. (2021) · Toxicology Letters · doi:10.1016/j.toxlet.2021.12.011 · Cited by 12 · see citing works

Oxygen sensing and transcriptional regulation under hypoxia exposure in the mollusk Crassostrea gigas

Meng, J., Wang, T., Li, B., Li, L., & Zhang, G. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.158557 · Cited by 10 · see citing works

Oxygen is an essential gasotransmitter directly sensed via protein gasoreceptors

Anbalagan, S. (2024) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12400 · Cited by 11 · see citing works

Vitamin B3-Based Biologically Active Compounds as Inhibitors of Human Cholinesterases

Zandona, A., Lihtar, G., Maraković, N., Miš, K., Bušić, V., Gašo-Sokač, D., Pirkmajer, S., & Katalinić, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218088 · Cited by 12 · see citing works

Oxygen Sensing in Neurodegenerative Diseases: Current Mechanisms, Implication of Transcriptional Response, and Pharmacological Modulation

Rey, F., Messa, L., Maghraby, E., Casili, G., Ottolenghi, S., Barzaghini, B., Raimondi, M. T., Cereda, C., Cuzzocrea, S., Zuccotti, G., et al. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0046 · Cited by 11 · see citing works

Hypoxia-driven deSUMOylation of EXOSC10 promotes adaptive changes in the transcriptome profile

Filippopoulou, C., Thomé, C. C., Perdikari, S., Ntini, E., Simos, G., Bohnsack, K. E., & Chachami, G. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05035-9 · Cited by 10 · see citing works

Advances in plant oxygen sensing: endogenous and exogenous mechanisms

Yan, Z., Yang, S., Chen, L., Yan, J., Liu, M., Tang, S., Jia, W., Liu, J., & Liu, H. (2024) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2024.11.014 · Cited by 9 · see citing works

Role of prolyl hydroxylase domain proteins in bone metabolism

Wolf, D., Muralidharan, A., & Mohan, S. (2022) · Osteoporosis and Sarcopenia · doi:10.1016/j.afos.2022.03.001 · Cited by 9 · see citing works

A synthetic synthesis to explore animal evolution and development

Perkins, M. L., Gándara, L., & Crocker, J. (2022) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2020.0517 · Cited by 9 · see citing works

Bioenergetic mapping of ‘healthy microbiomes’ via compound processing potential imprinted in gut and soil metagenomes

Liddicoat, C., Edwards, R. A., Roach, M. J., Robinson, J. M., Wallace, K. J., Barnes, A. D., Brame, J. E., Heintz‐Buschart, A., Cavagnaro, T. R., Dinsdale, E. A., et al. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.173543 · Cited by 9 · see citing works

Hypoxia signalling in the regulation of innate immune training

Eades, L., Drozd, M., & Cubbon, R. M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210857 · Cited by 9 · see citing works

Systems approaches to understand oxygen sensing: how multi-omics has driven advances in understanding oxygen-based signalling

Batie, M., Kenneth, N. S., & Rocha, S. (2022) · Biochemical Journal · doi:10.1042/bcj20210554 · Cited by 8 · see citing works

The origin and distribution of the main oxygen sensing mechanism across metazoans

Song, B., Modjewski, L., Kapust, N., Mizrahi, I., & Martin, W. F. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.977391 · Cited by 7 · see citing works

HOCI Probe CPP Induces the Differentiation of Human Dermal Fibroblasts into Vascular Endothelial Cells through PHD2/HIF-1α/HEY1 Signaling Pathway

Cui, X., Wen, J., Li, N., Hao, X., Zhang, S., Zhao, B., Wu, X., & Miao, J. (2022) · Cells · doi:10.3390/cells11193126 · Cited by 6 · see citing works

A Hypoxia-Epigenetics Axis Drives EMT in Pancreatic Cancer

Wirth, M., & Schneider, G. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-3578 · Cited by 6 · see citing works

Enhanced degradation of exogenetic citrinin by glycosyltransferases in the oleaginous yeast Saitozyma podzolica zwy-2-3

Yang, Q., Guo, S., Ran, Y., Zeng, J., Qiao, D., Xu, H., & Cao, Y. (2024) · Bioresource Technology · doi:10.1016/j.biortech.2024.131468 · Cited by 6 · see citing works

Hypoxia‐Mimicking Mediated Macrophage‐Elimination of Erythrocytes Promotes Bone Regeneration via Regulating Integrin α v β 3 /Fe 2+ ‐Glycolysis‐Inflammation

Ao, Y., Guo, Y., Zhang, Y., Xie, L., Xia, R., Xu, J., Shi, M., Gao, X., Yu, X., & Chen, Z. (2024) · Advanced Science · doi:10.1002/advs.202403921 · Cited by 6 · see citing works

Targeted therapies for myelodysplastic syndromes/neoplasms (MDS): current landscape and future directions

Bidikian, A., Bewersdorf, J. P., Shallis, R. M., Getz, T. M., Stempel, J. M., Kewan, T. Z., Stahl, M. F., & Zeidan, A. M. (2024) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2024.2414071 · Cited by 6 · see citing works

Genetic approaches to understand cellular responses to oxygen availability

Ortmann, B. M., & Nathan, J. A. (2021) · FEBS Journal · doi:10.1111/febs.16072 · Cited by 6 · see citing works

Hypoxia signalling in the regulation of innate immune training

Eades, L., Drozd, M., & Cubbon, R. (2022) · White Rose Research Online (University of Leeds, The University of Sheffield, University of York) · Cited by 5 · see citing works

Transducer Systems Integrated into Organ‐on‐a‐Chip Devices: From Detection to Fabrication

Ferreira, G. M., Sousa, P. C., Catarino, S. O., & Minas, G. M. H. (2025) · Small · doi:10.1002/smll.202510425 · Cited by 4 · see citing works

RNA Modifications in Cancer Stem Cell Biology

Cerneckis, J., Cui, Q., Liu, W., & Shi, Y. (2023) · Cancer treatment and research · doi:10.1007/978-3-031-45654-1_2 · Cited by 4 · see citing works

HIFs in hypoxic regulation of the extracellular matrix: focus on little-known player HIF-3

Gornostaeva, A. N., Buravkova, L. B., Lobanova, M. V., & Andreeva, E. R. (2024) · Biocell · doi:10.32604/biocell.2024.048873 · Cited by 5 · see citing works

Lingzhi or Reishi Medicinal Mushroom Ganoderma lucidum (Agaricomycetes) Aqueous Extract Reverses Hypoxia Induced Redox Imbalance and Inflammatory Response in Rat Thymocytes

Maithani, R., & Tulsawani, R. (2025) · International journal of medicinal mushrooms · doi:10.1615/intjmedmushrooms.2025059009 · Cited by 4 · see citing works

The Placental Circulations

Jones, D. S., Jauniaux, E. R. M., & Burton, G. J. (2021) · Springer eBooks · doi:10.1007/978-3-030-84725-8_9 · Cited by 4 · see citing works

Fe(2)OG: an integrated HMM profile-based web server to predict and analyze putative non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenase function in protein sequences

Kundu, S. (2021) · BMC Research Notes · doi:10.1186/s13104-021-05477-z · Cited by 4 · see citing works

Interaction of TFAP2A with the Ku70/80 complex is crucial for HIF ‐dependent activation of hypoxia‐inducible genes

Kanoura, A., Giakountis, A., Filippopoulou, C., Karagiota, A., Stamatakis, G. M., Samiotaki, M. K., Panayotou, G., Simos, G., & Chachami, G. (2025) · FEBS Journal · doi:10.1111/febs.70025 · Cited by 3 · see citing works

Cellular respiration in dendritic cells: Exploring oxygen-dependent pathways for potential therapeutic interventions

Peter, A., Berneman, Z. N., & Cools, N. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.12.014 · Cited by 3 · see citing works

2-Oxoglutarate-dependent dioxygenases as oxygen sensors: their importance in health and disease

Lee, P. W. T., Kobayashi, M., Dohkai, T., Takahashi, I., Yoshida, T., & Harada, H. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae087 · Cited by 4 · see citing works

A phenopushing platform to identify compounds that alleviate acute hypoxic stress by fast-tracking cellular adaptation

Li, L., Hammerlindl, H., Shen, S. Q., Bao, F., Hammerlindl, S., Altschuler, S., & Wu, L.-N. F. (2025) · Nature Communications · doi:10.1038/s41467-025-57754-1 · Cited by 2 · see citing works

Graph Structured Neural Networks for Perturbation BiologyPreprint

Evans, N. J., Mills, G. B., Wu, G., Song, X. B., & McWeeney, S. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.28.582164 · Cited by 3 · see citing works

HIF inhibition: Current strategies and clinical challenges

Więch-Walów, A., Bartoszewska, S., Barton, A., Czechowicz, P., Dudzik, J., Wielockx, B., Collawn, J. F., & Bartoszewski, R. (2026) · Redox biology · doi:10.1016/j.redox.2026.104220 · Cited by 3 · see citing works

PHD1-dependent hydroxylation of RepoMan (CDCA2) on P604 modulates the control of mitotic progression

Druker, J., Jiang, H., Shakir, D., Child, F., Álvarez, V., Platani, M., Corno, A., Alabert, C., Saurin, A. T., Swedlow, J. R., et al. (2026) · eLife · doi:10.7554/elife.108131.3 · Cited by 2 · see citing works

Bioprocess Engineering for Cultivated Meat

Bernfeld, J., Zschieschang, S., Kirsch, M., Morales-Dalmau, J., Liedtke, J., & Lavrentieva, A. V. (2025) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2025_292 · Cited by 2 · see citing works

A ceRNA Network Mediates Salinity Adaptation Via miR-novel-3-LNC_015168-SLC17A9 Axis in Sea Cucumber

Wei, X., Chen, J., Zhao, Y., Li, N., Wang, N., Xu, T., Yang, Y., Ya-qing, C., & Tian, Y. (2026) · Marine Biotechnology · doi:10.1007/s10126-025-10538-6 · Cited by 2 · see citing works

A mechanistic computational model of the HIF signaling pathway in endothelial cells

Oliveira, R. H. D. M., Pathak, A. P., & Popel, A. S. (2026) · iScience · doi:10.1016/j.isci.2026.116195 · Cited by 2 · see citing works

2‐Methoxyestradiol Inhibits the Oxygen‐Sensing Pathway in Keloid Fibroblasts by Targeting HIF ‐1α/ PHD

Zhang, M., Li, Z., Xia, W., Si, L., Yu, N., Wang, X., & Long, X. (2025) · International Wound Journal · doi:10.1111/iwj.70373 · Cited by 1 · see citing works

Local oxygen tension dictates hematopoietic cell growth and potency

Ropa, J. P., Gutch, S., Wathen, L., Kim, S. J., Park, J., Newton, J., Whitacre, G., Aljoufi, A., Cooper, S. H., Hof, W. V. ’., et al. (2026) · Leukemia · doi:10.1038/s41375-026-02971-w · Cited by 1 · see citing works

Stress-Induced Insulin Resistance: Role of Von Willebrand Factor

Khan, G. A., Khan, A. M. A., Singh, B., & Alqahtani, M. E. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1005260 · Cited by 1 · see citing works

Dexamethasone inhibits the LPS-induced activation of hypoxia-inducible factor 1 alpha (HIF-1α) in macrophages independently of the DUSP1-p38-TTP-HIF-1α regulatory axisPreprint

Lockwood, C., Daley, K. K., O’Neil, J. D., Heighes, K. J., Clayton, S. A., & Clark, A. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.19.677372 · Cited by 1 · see citing works

Roxadustat (FG4592) alleviates Radiation-Induced Intestinal Injury by facilitating recovery of intestinal stem cell and reducing damage of intestinal epithelial cellPreprint

Xia, P., Yang, Y., Liu, R., Tang, H., Du, J., Cheng, Y., Cai, J., Liu, C., Xu, X., & Liu, H. (2020) · doi:10.21203/rs.3.rs-39385/v1

Analyzing Iron and Oxygen-Regulated Protein Complex Formation Using Proteomic Mass Spectrometry

Pandey, V., Mayank, A. K., & Wohlschlegel, J. A. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3080-8_10

Hypoxia-Regulated Gene Expression and Metastasis

Karlıtepe, A., Pi̇levneli̇, H., & Eren, M. K. (2023) · Springer eBooks · doi:10.1007/978-981-99-0313-9_6

PHD1-dependent hydroxylation of RepoMan (CDCA2) on P604 modulates the control of mitotic progressionPreprint

Druker, J., Jiang, H., Shakir, D., Child, F., Álvarez, V., Platani, M., Corno, A., Alabert, C., Saurin, A. T., Swedlow, J. R., et al. (2025) · eLife · doi:10.7554/elife.108131

PHD1-dependent hydroxylation of RepoMan (CDCA2) on P604 modulates the control of mitotic progressionPreprint

Druker, J., Jiang, H., Shakir, D., Child, F., Álvarez, V., Platani, M., Corno, A., Alabert, C., Saurin, A. T., Swedlow, J. R., et al. (2025) · eLife · doi:10.7554/elife.108131.1

Lipopolysaccharide induces HIF-1α accumulation via MAPK p38–mediated mRNA stabilization and dexamethasone-sensitive protein stabilization

Lockwood, C., Daley, K. K., O’Neil, J. D., Heighes, K. J., Clayton, S. A., & Clark, A. R. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111094

PHD1-dependent hydroxylation of RepoMan (CDCA2) on P604 modulates the control of mitotic progressionPreprint

Druker, J., Jiang, H., Shakir, D., Child, F., Álvarez, V., Platani, M., Corno, A., Alabert, C., Saurin, A. T., Swedlow, J. R., et al. (2026) · eLife · doi:10.7554/elife.108131.2

Protist oxygen-sensing and the role of prolyl hydroxylase-regulation of E3(SCF) ubiquitin ligases

Cantrell, D. A., Blader, I. J., & West, C. M. (2026) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2026.130928

Mechanisms controlling transcription in hypoxia; an unexpected role of NF-κB

Shakir, D., Batie, M., & Rocha, S. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.03.030

Etude des variations de pressions partielles d'oxygène sur les réactions cellulaires chez le sujet sain

Lévêque, C. (2024) · doi:10.70675/0d961065ze6e6z464fz8e74zd9c653b2325f

Characterization of Novel Metabolites of the HIF Stabilizer JNJ‐42041935 in Rats Using LC‐HRMS for Doping Control Purposes: A Pilot Study

Hou, J., & Yang, S. (2026) · Drug Testing and Analysis · doi:10.1002/dta.70086

Inhibition of Jumonji C domain histone demethylases by JIB-04 exacerbates ischemia-reperfusion injury and maladaptive repair in females lacking ovarian hormones

Buen, E. P., Gutiérrez-Mercado, Y. K., Munguía-Galaviz, F. J., González-González, R., & Echavarría, R. (2026) · Tissue and Cell · doi:10.1016/j.tice.2026.104016

Oxygen sensing decoded: a Nobel concept in biology

Griffioen, A. W., & Bischoff, J. E. (2019) · Angiogenesis · doi:10.1007/s10456-019-09692-y · Cited by 18 · see citing works

Oxygen Sensing: After the Nobel

(2019) · Cell · doi:10.1016/j.cell.2019.12.008 · Cited by 2 · see citing works

The 2016 Albert Lasker Basic Medical Research Award: Oxygen sensing—a mysterious process essential for survival

Li, Z., & Zhang, W. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-0314-3 · Cited by 1 · see citing works

Sensing and Signalling in Response to Oxygen Deprivation in Plants and Other Organisms

Bailey-Serres, J. N., & Chang, R. (2005) · Annals of Botany · doi:10.1093/aob/mci206 · Cited by 274 · see citing works

A Genetic Approach to the Analysis of Cellular Oxygen Sensing

Vaux, E. (2001) · Clinical Science · doi:10.1042/cs101015p