A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis

Targeting HIF-1 for cancer therapy

Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717 · see citing works

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,974 · 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

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180 · 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

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

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

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

Regulation of angiogenesis by hypoxia: role of the HIF system

Pugh, C. W., & Ratcliffe, P. J. (2003) · Nature Medicine · doi:10.1038/nm0603-677 · Cited by 2,520 · see citing works

Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel–Lindau protein

Ohh, M., Park, C. W., Ivan, M., Hoffman, M. A., Kim, T.-Y., Huang, L. E., Pavletich, N., Chau, V., & Kaelin, W. G. (2000) · Nature Cell Biology · doi:10.1038/35017054 · Cited by 1,577 · 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

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

Hypoxia Inducible Factor-α Binding and Ubiquitylation by the von Hippel-Lindau Tumor Suppressor Protein

Cockman, M. E., Masson, N., Mole, D. R., Jaakkola, P., Chang, G.-W., Clifford, S. C., Maher, E. R., Pugh, C. W., Ratcliffe, P. J., & Maxwell, P. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002740200 · Cited by 1,053 · 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-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene.

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

Mechanism of regulation of the hypoxia‐inducible factor‐1α by the von Hippel‐Lindau tumor suppressor protein

Tanimoto, K., Makino, Y., Pereira, T., & Poellinger, L. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4298 · Cited by 928 · 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

Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

Kamura, T., Sato, S., Iwaï, K., Czyzyk-Krzeska, M., Conaway, R. C., & Conaway, J. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.190332597 · Cited by 652 · see citing works

Impaired physiological responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1α

Yu, A. Y., Shimoda, L. A., Iyer, N. V., Huso, D. L., Sun, X., McWilliams, R. M., Beaty, T. H., Sham, J. S. K., Wiener, C. M., Sylvester, J. T., et al. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5912 · Cited by 645 · see citing works

Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor

Ivan, M., Haberberger, T., Gervasi, D. C., Michelson, K. S., Günzler, V., Kondo, K., Yang, H., Sorokina, I., Conaway, R. C., Conaway, J. W., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192342099 · Cited by 561 · see citing works

Hearts From Rodents Exposed to Intermittent Hypoxia or Erythropoietin Are Protected Against Ischemia-Reperfusion Injury

Cai, Z. P., Manalo, D. J., Wei, G., Rodríguez, E. R., Fox-Talbot, K., Lu, H., Zweier, J. L., & Semenza, G. L. (2003) · Circulation · doi:10.1161/01.cir.0000078635.89229.8a · Cited by 557 · see citing works

Characterization of a Subset of the Basic-Helix-Loop-Helix-PAS Superfamily That Interacts with Components of the Dioxin Signaling Pathway

Hogenesch, J. B., Chan, W. K., Jackiw, V., Brown, R. C., Gu, Y.-Z., Pray-Grant, M. G., Perdew, G. H., & Bradfield, C. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8581 · Cited by 514 · see citing works

Disruption 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

Differentiating the functional role of hypoxia‐inducible factor (HIF)‐1α and HIF‐2α (EPAS‐1) by the use of RNA interference: erythropoietin is a HIF‐2α target gene in Hep3B and Kelly cells

Warnecke, C., Zaborowska, Z., Kurreck, J., Erdmann, V. A., Frei, U. A., Wiesener, M. S., & Eckardt, K. (2004) · The FASEB Journal · doi:10.1096/fj.04-1640fje · 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

Sequence determinants in hypoxia-inducible factor-1α for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3

Huang, J., Zhao, Q., Mooney, S. M., & Lee, F. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206955200 · Cited by 307 · see citing works

Congenital disorder of oxygen sensing: association of the homozygous Chuvash polycythemia VHL mutation with thrombosis and vascular abnormalities but not tumors

Gordeuk, V. R., Sergueeva, A. I., Miasnikova, G. Y., Okhotin, D., Voloshin, Y., Choyke, P. L., Butman, J. A., Jedlickova, K., Prchal, J. T., & Polyakova, L. A. (2004) · Blood · doi:10.1182/blood-2003-07-2535 · Cited by 273 · see citing works

Functional analysis of an oxygen-regulated transcriptional enhancer lying 3' to the mouse erythropoietin gene.

Pugh, C. W., Tan, C., Jones, R. W., & Ratcliffe, P. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10553 · Cited by 255 · see citing works

HIF-2α regulates murine hematopoietic development in an erythropoietin-dependent manner

Scortegagna, M., Ding, K., Zhang, Q., Oktay, Y., Bennett, M. J., Bennett, M., Shelton, J. M., Richardson, J. A., Moe, O. W., & Garcia, J. A. (2004) · Blood · doi:10.1182/blood-2004-05-1695 · Cited by 233 · see citing works

Enhancer element at the 3'-flanking region controls transcriptional response to hypoxia in the human erythropoietin gene

Beck, I., Ramirez, S., Weinmann, R. S., & Caro, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98438-3 · Cited by 206 · see citing works

The HIF family member EPAS1/HIF-2α is required for normal hematopoiesis in mice

Scortegagna, M., Morris, M. A., Oktay, Y., Bennett, M., & Garcia, J. A. (2003) · Blood · doi:10.1182/blood-2003-02-0448 · Cited by 203 · see citing works

VHL protein‐interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF‐1α

Li, Z., Wang, D., Messing, E. M., & Wu, G. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400377 · Cited by 196 · see citing works

The von Hippel-Lindau Tumor Suppressor Protein Mediates Ubiquitination of Activated Atypical Protein Kinase C

Okuda, H., Saitoh, K., Hirai, S.-I., Iwaï, K., Takaki, Y., Baba, M., Minato, N., Ohno, S., & Shuin, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107880200 · Cited by 176 · see citing works

Characterization and comparative analysis of the EGLN gene family

Taylor, M. S. (2001) · Gene · doi:10.1016/s0378-1119(01)00633-3 · Cited by 145 · see citing works

Inactivation of the Arylhydrocarbon Receptor Nuclear Translocator (Arnt) Suppresses von Hippel-Lindau Disease-Associated Vascular Tumors in Mice

Rankin, E. B., Higgins, D. F., Walisser, J. A., Johnson, R. S., Bradfield, C. A., & Haase, V. H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3163-3172.2005 · Cited by 137 · see citing works

Mutations in the VHL gene in sporadic apparently congenital polycythemia

Pastore, Y. D., Jelinek, J., Ang, S., Guan, Y., Liu, E., Jedlickova, K., Krishnamurti, L., & Prchal, J. T. (2003) · Blood · doi:10.1182/blood-2002-06-1843 · Cited by 136 · see citing works

Congenital polycythemias/erythrocytoses.

Gordeuk, V. R., Stockton, D. W., & Prchal, J. T. (2005) · PubMed · Cited by 104 · see citing works

Chuvash-type congenital polycythemia in 4 families of Asian and Western European ancestry

Percy, M. J., McMullin, M. F., Jowitt, S. N., Potter, M., Treacy, M., Watson, W. H., & Lappin, T. R. J. (2003) · Blood · doi:10.1182/blood-2002-10-3246 · Cited by 90 · see citing works

Dynamic, site-specific interaction of hypoxia-inducible factor-1alpha with the von Hippel-Lindau tumor suppressor protein.

Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · PubMed · Cited by 87 · see citing works

Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel–Lindau protein

Corn, P. G., McDonald, E. R., Herman, J. G., & El‐Deiry, W. S. (2003) · Nature Genetics · doi:10.1038/ng1254 · Cited by 78 · see citing works

The VHL protein recruits a novel KRAB‐A domain protein to repress HIF‐1α transcriptional activity

Li, Z., Wang, D., Na, X., Schoen, S. R., Messing, E. M., & Wu, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg173 · Cited by 77 · see citing works

Induction of human endometrial cancer cell senescence through modulation of HIF‐1α activity by EGLN1

Kato, H., Inoue, T., Asanoma, K., Nishimura, C., Matsuda, T., & Wake, N. (2005) · International Journal of Cancer · doi:10.1002/ijc.21488 · Cited by 74 · see citing works

Untitled work

(2005) · PubMed · Cited by 72 · see citing works

A common polymorphism in the oxygen-dependent degradation (ODD) domain of hypoxia inducible factor-1alpha (HIF-1alpha) does not impair Pro-564 hydroxylation.

Percy, M. J., Mooney, S. M., McMullin, M. F., Flores, A. G., Lappin, T. R. J., & Lee, F. S. (2003) · Molecular Cancer · doi:10.1186/1476-4598-2-31 · Cited by 60 · see citing works

The Transcriptional Activity of the APP Intracellular Domain−Fe65 Complex Is Inhibited by Activation of the NF-κB Pathway

Zhao, Q., & Lee, F. S. (2003) · Biochemistry · doi:10.1021/bi027117f · Cited by 32 · see citing works

Synthesis of acetals and ketals catalyzed by tungstosilicic acid supported on active carbon

Yang, S., Du, X.-X., He, L., & Sun, J. (2005) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.2005.b0373 · Cited by 17 · see citing works

Erythrocytosis and the Chuvash von Hippel-Lindau mutation

Percy, M. J., Beard, M. E. J., Carter, C., & Thein, S. L. (2003) · British Journal of Haematology · doi:10.1046/j.1365-2141.2003.04631.x · Cited by 8 · 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

Genetic Evidence for High-Altitude Adaptation in Tibet

Simonson, T. S., Yang, Y., Huff, C. D., Yun, H., Qin, G., Witherspoon, D. J., Bai, Z., Lorenzo, F. R., Xing, J., Jorde, L. B., et al. (2010) · Science · doi:10.1126/science.1189406 · Cited by 1,227 · see citing works

Oxygen Sensing, Homeostasis, and Disease

Semenza, G. L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1011165 · Cited by 989 · 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

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

Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation

Koivunen, P., Lee, S., Duncan, C. G., Lopez, G., Lu, G., Ramkissoon, S., Losman, J. A., Joensuu, P., Bergmann, U., Gross, S., et al. (2012) · Nature · doi:10.1038/nature10898 · Cited by 727 · see citing works

Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer

King, A., Selak, M. A., & Gottlieb, E. (2006) · Oncogene · doi:10.1038/sj.onc.1209594 · Cited by 672 · see citing works

Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo

Rankin, E. B., Biju, M. P., Liu, Q., Unger, T. L., Rha, J., Johnson, R. S., Simon, M. C., Keith, B., & Haase, V. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30117 · Cited by 596 · see citing works

Distribution and clinical impact of functional variants in 50,726 whole-exome sequences from the DiscovEHR study

Dewey, F. E., Murray, M. F., Overton, J. D., Habegger, L., Leader, J. B., Fetterolf, S. N., O’Dushlaine, C. T., Hout, C. V. V., Staples, J. C., Gonzaga-Jauregui, C. G., et al. (2016) · Science · doi:10.1126/science.aaf6814 · Cited by 533 · see citing works

A Lactate-Induced Response to Hypoxia

Lee, D. C., Sohn, H. A., Park, Z., Oh, S. H., Kang, Y. K., Lee, K.-M., Kang, M., Jang, Y. J., Yang, S., Hong, Y. K., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.011 · Cited by 523 · see citing works

The stimulation of thrombosis by hypoxia

Gupta, N., Zhao, Y., & Evans, C. E. (2019) · Thrombosis Research · doi:10.1016/j.thromres.2019.07.013 · Cited by 438 · see citing works

Role and regulation of prolyl hydroxylase domain proteins

Fong, G.-H., & Takeda, K. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.10 · Cited by 423 · see citing works

A genetic mechanism for Tibetan high-altitude adaptation

Lorenzo, F., Huff, C. D., Myllymäki, M., Olenchock, B. A., Swierczek, S. I., Tashi, T., Gordeuk, V. R., Wuren, T., Ge, R., McClain, D. A., et al. (2014) · Nature Genetics · doi:10.1038/ng.3067 · Cited by 422 · 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

Erythropoietin after a century of research: younger than ever

JELKMANN, W. E. B. (2007) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2007.00818.x · Cited by 365 · see citing works

The IRP/IRE system in vivo: insights from mouse models

Wilkinson, N., & Pantopoulos, K. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00176 · Cited by 366 · see citing works

Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)

McDonough, M. A., Li, V., Flashman, E., Chowdhury, R., Mohr, C., Liénard, B. M. R., Zondlo, J., Oldham, N. J., Clifton, I. J., Lewis, J. K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601283103 · Cited by 366 · see citing works

Genetics and clinical characteristics of hereditary pheochromocytomas and paragangliomas

Welander, J., Söderkvist, P., & Gimm, O. (2011) · Endocrine Related Cancer · doi:10.1530/erc-11-0170 · Cited by 356 · see citing works

Targeting iron metabolism in drug discovery and delivery

Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352 · 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

Hypoxic regulation of erythropoiesis and iron metabolism

Haase, V. H. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00174.2010 · Cited by 347 · 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

von Hippel-Lindau Disease

Kaelin, W. G. (2006) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.2.010506.092049 · Cited by 335 · see citing works

Hypoxia-inducible factors in the kidney

Haase, V. H. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00071.2006 · Cited by 329 · see citing works

Generating specificity and diversity in the transcriptional response to hypoxia

Lendahl, U., Lee, K. L., Yang, H. H., & Poellinger, L. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2665 · Cited by 330 · see citing works

Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease

Fraisl, P., Aragonés, J., & Carmeliet, P. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2761 · Cited by 326 · see citing works

<i>PHD2</i> Mutation and Congenital Erythrocytosis with Paraganglioma

Ladroue, C., Carcenac, R., Leporrier, M., Gad, S., Le Hello, C., Galateau-Salle, F., Feunteun, J., Pouysségur, J., Richard, S., & Gardie, B. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0806277 · Cited by 323 · 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

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

Oxygen homeostasis

Semenza, G. L. (2009) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.69 · Cited by 311 · 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

Oxygen Sensors at the Crossroad of Metabolism

Aragonés, J., Fraisl, P., Baes, M. I., & Carmeliet, P. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.001 · Cited by 290 · 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

Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets

Myllyharju, J. (2008) · Annals of Medicine · doi:10.1080/07853890801986594 · Cited by 264 · 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 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

Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing

Webb, J. D., Coleman, M. L., & Pugh, C. W. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0147-7 · Cited by 255 · see citing works

ErythropoietinPreprint

Bunn, H. F. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011619 · Cited by 247 · see citing works

Targeting hypoxia-inducible factors: therapeutic opportunities and challenges

Yuan, X., Ruan, W., Bobrow, B., Carmeliet, P., & Eltzschig, H. K. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00848-6 · Cited by 245 · 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

Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates

Hewitson, K. S., Liénard, B. M. R., McDonough, M. A., Clifton, I. J., Butler, D., Soares, A. S., Oldham, N. J., McNeill, L. A., & Schofield, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608337200 · Cited by 235 · see citing works

Involvement of oxygen-sensing pathways in physiologic and pathologic erythropoiesis

Semenza, G. L. (2009) · Blood · doi:10.1182/blood-2009-05-189985 · Cited by 225 · see citing works

Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?

Ozer, A., & Bruick, R. K. (2007) · Nature Chemical Biology · doi:10.1038/nchembio863 · Cited by 214 · see citing works

The Many Facets of Erythropoietin Physiologic and Metabolic Response

Suresh, S., Rajvanshi, P. K., & Noguchi, C. T. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2019.01534 · Cited by 207 · see citing works

Hypoxia-inducible factors link iron homeostasis and erythropoiesis

Shah, Y. M., & Xie, L. (2014) · Gastroenterology · doi:10.1053/j.gastro.2013.12.031 · Cited by 187 · see citing works

An overview of 20 years of genetic studies in pheochromocytoma and paraganglioma

Buffet, A., Burnichon, N., Favier, J., & Gimenez‐Roqueplo, A. (2020) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2020.101416 · Cited by 194 · see citing works

Deletion of Iron Regulatory Protein 1 Causes Polycythemia and Pulmonary Hypertension in Mice through Translational Derepression of HIF2α

Ghosh, M. C., Zhang, D.-L., Jeong, S. Y., Kovtunovych, G., Ollivierre-Wilson, H., Noguchi, A., Tu, T., Senecal, T., Robinson, G., Crooks, D. R., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.016 · Cited by 183 · see citing works

pVHL Acts as an Adaptor to Promote the Inhibitory Phosphorylation of the NF-κB Agonist Card9 by CK2

Yang, H., Minamishima, Y. A., Yan, Q., Schlisio, S., Ebert, B. L., Zhang, X., Zhang, L., Kim, W. Y., Olumi, A. F., & Kaelin, W. G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.010 · Cited by 179 · see citing works

The HIF pathway and erythrocytosis

Lee, F. S., & Percy, M. J. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130321 · Cited by 177 · see citing works

Loss of Hypoxia-Inducible Factor Prolyl Hydroxylase Activity in Cardiomyocytes Phenocopies Ischemic Cardiomyopathy

Moslehi, J. J., Minamishima, Y. A., Shi, J., Neuberg, D. S., Charytan, D. M., Padera, R. F., Signoretti, S., Liao, R., & Kaelin, W. G. (2010) · Circulation · doi:10.1161/circulationaha.109.922427 · Cited by 168 · see citing works

Inhibition of Hypoxia-Inducible Factor Prolyl Hydroxylase Domain Oxygen Sensors: Tricking the Body into Mounting Orchestrated Survival and Repair Responses

Rabinowitz, M. H. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400386j · Cited by 165 · see citing works

A feedback loop involving the Phd3 prolyl hydroxylase tunes the mammalian hypoxic response in vivo

Minamishima, Y. A., Moslehi, J., Padera, R. F., Bronson, R. T., Liao, R., & Kaelin, W. G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00331-09 · Cited by 161 · see citing works

Human Genetic Adaptation to High Altitude: Evidence from the Andes

Julian, C. G., & MOORE, L. G. (2019) · Genes · doi:10.3390/genes10020150 · Cited by 160 · see citing works

Hypoxia-inducible factors and diabetes

Gunton, J. E. (2020) · Journal of Clinical Investigation · doi:10.1172/jci137556 · Cited by 159 · see citing works

Autosomal dominant erythrocytosis and pulmonary arterial hypertension associated with an activating HIF2α mutation

Gale, D. P., Harten, S. K., Reid, C. D. L., Tuddenham, E. G. D., & Maxwell, P. H. (2008) · Blood · doi:10.1182/blood-2008-04-153718 · Cited by 157 · see citing works

A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove

Percy, M. J., Furlow, P. W., Beer, P. A., Lappin, T. R. J., McMullin, M. F., & Lee, F. S. (2007) · Blood · doi:10.1182/blood-2007-04-084434 · Cited by 155 · see citing works

HYPOXIA‐INDUCED ERYTHROPOIETIN PRODUCTION: A PARADIGM FOR OXYGEN‐REGULATED GENE EXPRESSION

Stockmann, C., & Fandrey, J. (2006) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2006.04474.x · Cited by 154 · see citing works

Prolyl hydroxylase domain inhibitors as a novel therapeutic approach against anemia in chronic kidney disease

Sugahara, M., Tanaka, T., & Nangaku, M. (2017) · Kidney International · doi:10.1016/j.kint.2017.02.035 · Cited by 148 · see citing works

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

Chowdhury, R., Leung, I. K. H., Tian, Y.-M., Abboud, M. I., Ge, W., Domene, C., Cantrelle, F.-X., Landrieu, I., Hardy, A. P., Pugh, C. W., et al. (2016) · Nature Communications · doi:10.1038/ncomms12673 · Cited by 145 · see citing works

Emerging novel functions of the oxygen-sensing prolyl hydroxylase domain enzymes

Wong, B. W., Kuchnio, A., Brüning, U., & Carmeliet, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.10.004 · Cited by 141 · see citing works

Regulation of angiogenesis by oxygen sensing mechanisms

Fong, G. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0458-z · Cited by 140 · see citing works

High-Altitude Adaptation: Mechanistic Insights from Integrated Genomics and Physiology

Storz, J. F. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab064 · Cited by 136 · see citing works

Genetics of human origin and evolution: high-altitude adaptations

Bigham, A. W. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.06.018 · 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

In vivo and in vitro oncogenic effects of HIF2A mutations in pheochromocytomas and paragangliomas

Toledo, R. A., Qin, Y., Srikantan, S., Morales, N. P., Li, Q., Deng, Y., Kim, S.-W., Pereira, M. A. A., Toledo, S. P. A., Su, X., et al. (2013) · Endocrine Related Cancer · doi:10.1530/erc-13-0101 · Cited by 133 · see citing works

IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2α mRNA translation

Wilkinson, N., & Pantopoulos, K. (2013) · Blood · doi:10.1182/blood-2013-03-492454 · Cited by 133 · see citing works

CYSL-1 Interacts with the O2-Sensing Hydroxylase EGL-9 to Promote H2S-Modulated Hypoxia-Induced Behavioral Plasticity in C. elegans

Dengke, K., Vozdek, R., Bhatla, N., & Horvitz, H. R. (2012) · Neuron · doi:10.1016/j.neuron.2011.12.037 · Cited by 129 · 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

Novel exon 12 mutations in the HIF2A gene associated with erythrocytosis

Percy, M. J., Beer, P. A., Campbell, G., Dekker, A. W., Green, A. R., Oscier, D., Rainey, M. G., van Wijk, R., Wood, M., Lappin, T. R. J., et al. (2008) · Blood · doi:10.1182/blood-2008-02-137703 · Cited by 127 · see citing works

Erythropoietin Action in Stress Response, Tissue Maintenance and Metabolism

Zhang, Y., Wang, L., Dey, S., Alnaeeli, M., Suresh, S., Rogers, H. M., Teng, R., & Noguchi, C. T. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150610296 · Cited by 130 · see citing works

The complete evaluation of erythrocytosis: congenital and acquired

Patnaik, M. M., & Tefferi, A. (2009) · Leukemia · doi:10.1038/leu.2009.54 · Cited by 124 · see citing works

Genetic Basis of Congenital Erythrocytosis: Mutation Update and Online Databases

Bento, C., Percy, M. J., Gardie, B., Maia, T. M., van Wijk, R., Perrotta, S., Ragione, F. D., Almeida, H., Rossi, C., Girodon, F., et al. (2013) · Human Mutation · doi:10.1002/humu.22448 · Cited by 123 · see citing works

Prolyl 4‐hydroxylases, master regulators of the hypoxia response

Myllyharju, J. (2013) · Acta Physiologica · doi:10.1111/apha.12096 · Cited by 118 · see citing works

Regulated oxygen sensing by protein hydroxylation in renal erythropoietin-producing cells

Wenger, R. H., & Hoogewijs, D. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00736.2009 · Cited by 116 · see citing works

The classification and diagnosis of erythrocytosis

McMullin, M. F. (2008) · International Journal of Laboratory Hematology · doi:10.1111/j.1751-553x.2008.01102.x · Cited by 115 · see citing works

Erythrocytosis: the HIF pathway in control

Franke, K., Gassmann, M., & Wielockx, B. (2013) · Blood · doi:10.1182/blood-2013-01-478065 · Cited by 112 · see citing works

Survival and proliferative roles of erythropoietin beyond the erythroid lineage

Noguchi, C. T., Wang, L., Rogers, H. M., Teng, R., & Jia, Y. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399408000860 · Cited by 113 · see citing works

HIF-α Prolyl Hydroxylase Inhibitors and Their Implications for Biomedicine: A Comprehensive Review

Hirota, K. (2021) · Biomedicines · doi:10.3390/biomedicines9050468 · Cited by 113 · see citing works

HIF prolyl hydroxylases in the rat; organ distribution and changes in expression following hypoxia and coronary artery ligation

Willam, C., Maxwell, P. H., Nichols, L., Lygate, C. A., Tian, Y., Bernhardt, W. M., Wiesener, M. S., Ratcliffe, P. J., Eckardt, K., & Pugh, C. W. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.04.009 · Cited by 111 · see citing works

Pathophysiology of anemia and erythrocytosis

Hodges, V. M., Rainey, S., Lappin, T. R. J., & Maxwell, A. P. (2007) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2007.06.006 · Cited by 107 · see citing works

Erythrocytosis and Pulmonary Hypertension in a Mouse Model of Human HIF2A Gain of Function Mutation

Tan, Q., Kerestes, H., Percy, M. J., Pietrofesa, R. A., Chen, L., Khurana, T. S., Christofidou‐Solomidou, M., Lappin, T. R. J., & Lee, F. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444059 · Cited by 104 · see citing works

The Peptidyl Prolyl cis/trans Isomerase FKBP38 Determines Hypoxia-Inducible Transcription Factor Prolyl-4-Hydroxylase PHD2 Protein Stability

Barth, S., Nesper, J., Hasgall, P. A., Wirthner, R., Nytko, K. J., Edlich, F., Katschinski, D. M., Stiehl, D. P., Wenger, R. H., & Camenisch, G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01324-06 · Cited by 103 · see citing works

Hypoxia-Inducible Factor and Its Role in the Management of Anemia in Chronic Kidney Disease

Kaplan, J., Sharma, N., & Dikdan, S. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020389 · Cited by 104 · see citing works

The role of HIF prolyl hydroxylases in tumour growth

Jokilehto, T., & Jaakkola, P. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01030.x · Cited by 102 · see citing works

Hypoxia-inducible factor-1α contributes to the profibrotic action of angiotensin II in renal medullary interstitial cells

Wang, Z., Tang, L., Zhu, Q., Yi, F., Zhang, F., Li, P., & Li, N. (2010) · Kidney International · doi:10.1038/ki.2010.326 · Cited by 101 · see citing works

Prolyl Hydroxylase Domain Inhibitors: A Route to HIF Activation and Neuroprotection

Harten, S. K., Ashcroft, M. A., & Maxwell, P. H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2870 · Cited by 99 · see citing works

Discovery and Preclinical Characterization of GSK1278863 (Daprodustat), a Small Molecule Hypoxia Inducible Factor–Prolyl Hydroxylase Inhibitor for Anemia

Ariazi, J. L., Duffy, K. J., Adams, D. F., Fitch, D. M., Luo, L., Pappalardi, M. B., Biju, M. P., DiFilippo, E. H., Shaw, T., Wiggall, K., et al. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.242503 · 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

Epigenetics: prenatal exposure to genistein leaves a permanent signature on the hematopoietic lineage

Vanhees, K., Coort, S. L., Ruijters, E. J. B., Godschalk, R., van Schooten, F., & van Doorn-Khosrovani, S. B. V. W. (2010) · The FASEB Journal · doi:10.1096/fj.10-172155 · Cited by 87 · see citing works

Prolyl hydroxylase 2 inactivation enhances glycogen storage and promotes excessive neutrophilic responses

Sadiku, P., Willson, J. A., Dickinson, R. S., Murphy, F. A., Harris, A. J., Lewis, A., Sammut, D., Mirchandani, A. S., Ryan, E. M., Watts, E., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90848 · Cited by 86 · see citing works

Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: small molecule-based therapeutics for anemia

Yan, L. Y., Colandrea, V. J., & Hale, J. J. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.510836 · Cited by 86 · see citing works

HIF-1α is a protective factor in conditional PHD2-deficient mice suffering from severe HIF-2α–induced excessive erythropoiesis

Franke, K., Kalucka, J. M., Mamlouk, S., Singh, R. P., Muschter, A., Weidemann, A., Iyengar, V., Jahn, S., Wieczorek, K. S., Geiger, K. D., et al. (2012) · Blood · doi:10.1182/blood-2012-08-449181 · Cited by 83 · see citing works

The frequency of JAK2 exon 12 mutations in idiopathic erythrocytosis patients with low serum erythropoietin levels

Percy, M. J., Scott, L. M., Erber, W. N., Harrison, C. N., Reilly, J. T., Jones, F. G. C., Green, A. R., & McMullin, M. F. (2007) · Haematologica · doi:10.3324/haematol.11643 · Cited by 85 · see citing works

Cellular Signal Transduction of the Hypoxia Response

Nakayama, K. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp167 · Cited by 82 · see citing works

Update on mutations in the HIF: EPO pathway and their role in erythrocytosis

Lappin, T. R. J., & Lee, F. S. (2019) · Blood Reviews · doi:10.1016/j.blre.2019.100590 · Cited by 82 · see citing works

Genetics and molecular pathogenesis of pheochromocytoma and paraganglioma

Galan, S., & Kann, P. H. (2012) · Clinical Endocrinology · doi:10.1111/cen.12071 · Cited by 83 · see citing works

Hypoxia-inducible factor prolyl-hydroxylase-2 mediates transforming growth factor beta 1-induced epithelial–mesenchymal transition in renal tubular cells

Han, W., Zhu, Q., Hu, J., Li, P., Zhang, F., & Li, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.029 · Cited by 82 · see citing works

The role of hypoxia, increased oxygen consumption, and hypoxia-inducible factor-1 alpha in progression of chronic kidney disease

Tanaka, T., & Nangaku, M. (2009) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e3283328eed · Cited by 79 · see citing works

Pharmacological Characterization of 1-(5-Chloro-6-(trifluoromethoxy)-1H-benzoimidazol-2-yl)-1H-pyrazole-4-carboxylic Acid (JNJ-42041935), a Potent and Selective Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitor

Barrett, T. D., Palomino, H. L., Brondstetter, T. I., Kanelakis, K. C., Wu, X., Haug, P. V., Yan, W., Young, A., Hua, H., Hart, J. C., et al. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070508 · Cited by 78 · see citing works

Loss of JAK2 regulation via a heterodimeric VHL-SOCS1 E3 ubiquitin ligase underlies Chuvash polycythemia

Russell, R. C., Sufan, R. I., Zhou, B. R., Heir, P., Bunda, S., Sybingco, S. S., Greer, S. N., Roche, O., Heathcote, S. A., Chow, V. W. K., et al. (2011) · Nature Medicine · doi:10.1038/nm.2370 · Cited by 78 · see citing works

Familial Erythrocytosis Associated with a Mutation in the HIF Prolyl Hydroxylase, PHD2.

Percy, M. J., Zhao, Q., Flores, A., Harrison, C. N., Lappin, T. R. J., Maxwell, P. H., McMullin, M. F., & Lee, F. (2005) · Blood · doi:10.1182/blood.v106.11.127.127 · Cited by 2 · see citing works

Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins

Cells, R., Lee, F. S., & Fong, G.-H. (2016)

Isolated erythrocytosis: study of 67 patients and identification of three novel germ-line mutations in the prolyl hydroxylase domain protein 2 (PHD2) gene

Albiero, E., Ruggeri, M., Fortuna, S., Finotto, S., Bernardi, M., Madeo, D., & Rodeghiero, F. (2012) · Haematologica · doi:10.3324/haematol.2010.039545 · Cited by 28 · see citing works

Prolyl hydroxylase domain proteins: Localization, regulation, function and their role in erythropoiesis (Review)

Hou, Y., Zhang, Z.-H., Li, W.-Q., Han, G., Shen, K., & Xie, Y. (2026) · Molecular Medicine Reports · doi:10.3892/mmr.2026.13792 · Cited by 4 · see citing works

Disturbance in the HIF-1α pathway associated with erythrocytosis: Further evidences brought by frameshift and nonsense mutations in the prolyl hydroxylase domain protein 2 (PHD2) gene

Al-Sheikh, M., Moradkhani, K., Lopez, M., Wajcman, H., & Préhu, C. (2008) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.07.017 · Cited by 50 · see citing works