Anaemia in kidney disease: harnessing hypoxia responses for therapy

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

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

Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization

Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803 · 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

Anemia of Chronic Disease

Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800 · 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

Correction of anemia with epoetin alfa in chronic kidney disease

Singh, A. K., Szczech, L., Tang, K. L., Barnhart, H., Sapp, S., Wolfson, M., & Reddan, D. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa065485 · Cited by 2,762 · see citing works

IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin

Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650 · 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

A trial of darbepoetin alfa in type 2 diabetes and chronic kidney disease

Pfeffer, M. A., Burdmann, E. A., Chen, C.-Y., Cooper, M. E., de Zeeuw, D., Eckardt, K.-U., Feyzi, J. M., Ivanovich, P., Kewalramani, R., Levey, A. S., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0907845 · Cited by 2,096 · see citing works

Normalization of Hemoglobin Level in Patients with Chronic Kidney Disease and Anemia

Drüeke, T. B., Locatelli, F., Clyne, N., Eckardt, K., Macdougall, I. C., Tsakiris, D., Burger, H.-U., & Scherhag, A. W. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa062276 · Cited by 2,094 · see citing works

The Effects of Normal as Compared with Low Hematocrit Values in Patients with Cardiac Disease Who Are Receiving Hemodialysis and Epoetin

Besarab, A., Bolton, W. K., Browne, J. K., Egrie, J. C., Nissenson, A. R., Okamoto, D. M., Schwab, S. J., & Goodkin, D. A. (1998) · New England Journal of Medicine · doi:10.1056/nejm199808273390903 · Cited by 1,930 · see citing works

Regulation of Mammalian O ₂ Homeostasis by Hypoxia-Inducible Factor 1

Semenza, G. L. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.551 · Cited by 1,914 · see citing works

Impact of epoetin alfa on clinical end points in patients with chronic renal failure: A meta-analysis

Jones, M., Ibels, L. S., Schenkel, B., & Zagari, M. J. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00450.x · Cited by 1,812 · see citing works

HIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progression

Keith, B., Johnson, R. S., & Simon, M. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3183 · Cited by 1,693 · see citing works

General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia.

Wang, G. L., & Semenza, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4304 · Cited by 1,468 · see citing works

Fate Tracing Reveals the Pericyte and Not Epithelial Origin of Myofibroblasts in Kidney Fibrosis

Humphreys, B. D., Lin, S., Kobayashi, A., Hudson, T. E., Nowlin, B. T., Bonventre, J. V., Valerius, M. T., McMahon, A. P., & Duffield, J. S. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090517 · Cited by 1,447 · see citing works

The impact of O2 availability on human cancer

Bertout, J. A., Patel, S. A., & Simon, M. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2540 · Cited by 1,365 · see citing works

Dysmetabolic Hyperferritinemia: All Iron Overload Is Not Hemochromatosis

Makker, J. S., Hanif, A., Bajantri, B., & Chilimuri, S. S. (2015) · Case Reports in Gastroenterology · doi:10.1159/000373883 · Cited by 1,353 · see citing works

HIF-1 mediates metabolic responses to intratumoral hypoxia and oncogenic mutations

Semenza, G. L. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67230 · Cited by 1,335 · see citing works

HIF-1 and mechanisms of hypoxia sensing

Semenza, G. L. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00194-0 · Cited by 1,267 · see citing works

The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation

Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214 · see citing works

JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin

Witthuhn, B. A., Quelle, F. W., Silvennoinen, O., Yi, T., Tang, B., Miura, O., & Ihle, J. N. (1993) · Cell · doi:10.1016/0092-8674(93)90414-l · Cited by 1,184 · see citing works

Hypoxia-Induced Angiogenesis: Good and Evil

Krock, B. L., Skuli, N., & Simon, M. C. (2011) · Genes & Cancer · doi:10.1177/1947601911423654 · Cited by 1,179 · see citing works

Erythropoietin: structure, control of production, and function

JELKMANN, W. E. B. (1992) · Physiological Reviews · doi:10.1152/physrev.1992.72.2.449 · Cited by 1,167 · see citing works

Oxygen Sensing, Hypoxia-Inducible Factors, and Disease Pathophysiology

Semenza, G. L. (2013) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104720 · Cited by 1,159 · see citing works

Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1

Manalo, D. J., Rowan, A., Lavoie, T., Natarajan, L., Kelly, B. D., Ye, S. Q., Garcia, J. G. N., & Semenza, G. L. (2005) · Blood · doi:10.1182/blood-2004-07-2958 · Cited by 1,154 · see citing works

History of Erythropoiesis-Stimulating Agents, the Development of Biosimilars, and the Future of Anemia Treatment in Nephrology

Kalantar‐Zadeh, K. (2017) · American Journal of Nephrology · doi:10.1159/000455387 · Cited by 1,149 · see citing works

Identification of erythroferrone as an erythroid regulator of iron metabolism

Kautz, L., Jung, G., Valore, E. V., Rivella, S., Nemeth, E., & Ganz, T. (2014) · Nature Genetics · doi:10.1038/ng.2996 · Cited by 1,127 · see citing works

The role of iron regulatory proteins in mammalian iron homeostasis and disease

Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055 · see citing works

Integration of Oxygen Signaling at the Consensus HRE

Wenger, R. H., Stiehl, D. P., & Camenisch, G. (2005) · Science's STKE · doi:10.1126/stke.3062005re12 · Cited by 1,032 · see citing works

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

Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor

Wu, H., Liu, X., Jaenisch, R., & Lodish, H. F. (1995) · Cell · doi:10.1016/0092-8674(95)90234-1 · Cited by 1,007 · see citing works

Role of the kidney in erythropoiesis

JACOBSON, L. O., GOLDWASSER, E., FRIED, W., & PLZAK, L. (1957) · Nature · doi:10.1038/179633a0 · Cited by 862 · see citing works

Erythropoietin Retards DNA Breakdown and Prevents Programmed Death in Erythroid Progenitor Cells

Koury, M. J., & Bondurant, M. C. (1990) · Science · doi:10.1126/science.2326648 · Cited by 841 · see citing works

Pericytes and Perivascular Fibroblasts Are the Primary Source of Collagen-Producing Cells in Obstructive Fibrosis of the Kidney

Lin, S., Kisseleva, T., Brenner, D. A., & Duffield, J. S. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080433 · Cited by 834 · 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

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

Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia

Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782 · see citing works

Desferrioxamine induces erythropoietin gene expression and hypoxia- inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction

Wang, G., & Semenza, G. (1993) · Blood · doi:10.1182/blood.v82.12.3610.3610 · Cited by 766 · 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

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

Schödel, J., Oikonomopoulos, S., Ragoussis, J., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2011) · Blood · doi:10.1182/blood-2010-10-314427 · Cited by 724 · see citing works

Decreased Erythropoietin Response in Patients with the Anemia of Cancer

Miller, C. B., Jones, R. J., Piantadosi, S., Abeloff, M. D., & Spivak, J. L. (1990) · New England Journal of Medicine · doi:10.1056/nejm199006143222401 · Cited by 655 · see citing works

The Heart and Pulmonary Circulation at High Altitudes: Healthy Highlanders and Chronic Mountain Sickness

Penaloza, D., & Arias-Stella, J. (2007) · Circulation · doi:10.1161/circulationaha.106.624544 · Cited by 643 · see citing works

Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)

Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639 · see citing works

Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation

Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A. (1999) · Science · doi:10.1126/science.283.5404.987 · Cited by 598 · 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

The mammalian basic helix–loop–helix/PAS family of transcriptional regulators

Kewley, R. J., Whitelaw, M. L., & Chapman‐Smith, A. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00211-5 · Cited by 590 · see citing works

The serine protease TMPRSS6 is required to sense iron deficiency

Du, X., She, E., Gelbart, T., Truksa, J., Lee, P., Xia, Y., Khovananth, K., Mudd, S., Mann, N., Moresco, E. M. Y., et al. (2008) · Science · doi:10.1126/science.1157121 · Cited by 578 · see citing works

The Serine Protease Matriptase-2 (TMPRSS6) Inhibits Hepcidin Activation by Cleaving Membrane Hemojuvelin

Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., & Camaschella, C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.012 · Cited by 555 · see citing works

Erythropoietin Gene Expression in Human, Monkey and Murine Brain

Marti, H. H., Wenger, R. H., Rivas, L. A., Straumann, U., Oigicaylioglu, M., Henn, V. S., Yonekawa, Y., Bauer, C., & Gassmann, M. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01252.x · Cited by 553 · see citing works

Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells

Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544 · see citing works

Erythroblastic islands: niches for erythropoiesis

Chasis, J. A., & Mohandas, N. (2008) · Blood · doi:10.1182/blood-2008-03-077883 · Cited by 506 · see citing works

Iron Metabolism and the IRE/IRP Regulatory System: An Update

Pantopoulos, K. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.001 · Cited by 505 · see citing works

HIF-2α, but not HIF-1α, promotes iron absorption in mice

Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502 · see citing works

Expanding chemical biology of 2-oxoglutarate oxygenases

Loenarz, C., & Schofield, C. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio0308-152 · Cited by 498 · see citing works

Mammalian Kidney Development: Principles, Progress, and ProjectionsPreprint

Little, M. H., & McMahon, A. P. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008300 · Cited by 479 · see citing works

Localization of erythropoietin synthesizing cells in murine kidneys by in situ hybridization

Koury, S., Bondurant, M. C., & Koury, M. (1988) · Blood · doi:10.1182/blood.v71.2.524.524 · Cited by 469 · see citing works

Acute postnatal ablation of <i>Hif-2</i> α results in anemia

Gruber, M., Hu, C.-J., Johnson, R. S., Brown, E. J., Keith, B., & Simon, M. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608382104 · Cited by 457 · see citing works

Peritubular cells are the site of erythropoietin synthesis in the murine hypoxic kidney.

Lacombe, C., Silva, J. L. D., Bruneval, P., Fournier, J. G., Wendling, F., Casadevall, N., Camilleri, J.-P., Bariety, J., Varet, B. R., & Tambourin, P. E. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113363 · Cited by 437 · see citing works

Intestinal Hypoxia-Inducible Transcription Factors Are Essential for Iron Absorption following Iron Deficiency

Shah, Y. M., Matsubara, T., Ito, S., Yim, S.-H., & Gonzalez, F. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.012 · Cited by 431 · see citing works

How the Target Hemoglobin of Renal Anemia Should Be?

Mimura, I., Tanaka, T., & Nangaku, M. (2015) · The Nephron journals/Nephron journals · doi:10.1159/000440849 · Cited by 416 · see citing works

A randomized controlled study of iron supplementation in patients treated with erythropoietin

Macdougall, I. C., Tucker, B., Thompson, J., Tomson, C., Baker, L. R. I., & Raine, A. E. G. (1996) · Kidney International · doi:10.1038/ki.1996.487 · Cited by 415 · see citing works

Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1

Rolfs, A., Kvietikova, I., Gassmann, M., & Wenger, R. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20055 · Cited by 401 · see citing works

Identification of the renal erythropoietin-producing cells using transgenic mice

Maxwell, P. H., Osmond, M. K., Pugh, C. W., Heryet, A. R., Nicholls, L. G., Tan, C. C., Doe, B., Ferguson, D. J. P., Johnson, M. H., & Ratcliffe, P. J. (1993) · Kidney International · doi:10.1038/ki.1993.362 · Cited by 388 · see citing works

Identification of a hypoxia response element in the transferrin receptor gene

Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380 · see citing works

Transferrin Receptor Induction by Hypoxia

Tacchini, L., Bianchi, L., Bernelli-Zazzera, A., & Cairo, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24142 · Cited by 379 · 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

Heme regulates the dynamic exchange of Bach1 and NF-E2-related factors in the Maf transcription factor network

Sun, J., Brand, M., Zenke, Y., Tashiro, S., Groudine, M., & Igarashi, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308083100 · Cited by 364 · see citing works

The regulated expression of erythropoietin by two human hepatoma cell lines.

Goldberg, M. A., Glass, G. A., Cunningham, J. M., & Bunn, H. F. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.7972 · Cited by 358 · see citing works

Structure, function, and activation of the erythropoietin receptor

Youssoufian, H., Longmore, G. D., Neumann, D., Yoshimura, A., & Lodish, H. F. (1993) · Blood · doi:10.1182/blood.v81.9.2223.2223 · Cited by 353 · see citing works

Molecular control of iron transport

Ganz, T. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006070802 · Cited by 353 · see citing works

Turning cells red: signal transduction mediated by erythropoietin

Richmond, T. D., Chohan, M., & Barber, D. L. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.01.007 · Cited by 349 · see citing works

Dysfunction of fibroblasts of extrarenal origin underlies renal fibrosis and renal anemia in mice

Asada, N., Takase, M., Nakamura, J., Oguchi, A., Asada, M., Suzuki, N., Yamamura, K., Nagoshi, N., Shibata, S., Rao, T. N., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57301 · Cited by 348 · 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

Heme Induces Ubiquitination and Degradation of the Transcription Factor Bach1

Zenke-Kawasaki, Y., Dohi, Y., Katoh, Y., Ikura, T., Ikura, M., Asahara, T., Tokunaga, F., Iwaï, K., & Igarashi, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02415-06 · Cited by 330 · see citing works

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

Percy, M. J., Zhao, Q., Flores, A., Harrison, C., Lappin, T. R. J., Maxwell, P. H., McMullin, M. F., & Lee, F. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508423103 · Cited by 330 · 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

Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis

Liu, Q., Davidoff, O., Niss, K., & Haase, V. H. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63924 · Cited by 328 · see citing works

Erythropoietin

Erslev, A. J. (1991) · New England Journal of Medicine · doi:10.1056/nejm199105093241907 · Cited by 324 · see citing works

Co-localization of erythropoietin mRNA and ecto-5'-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin.

Bachmann, S., Hir, M. L., & Eckardt, K. (1993) · Journal of Histochemistry & Cytochemistry · doi:10.1177/41.3.8429197 · Cited by 322 · see citing works

The multifunctional role of EKLF/KLF1 during erythropoiesis

Siatecka, M., & Bieker, J. J. (2011) · Blood · doi:10.1182/blood-2011-03-331371 · Cited by 314 · 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

Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis

Silvestri, L., Pagani, A., & Camaschella, C. (2008) · Blood · doi:10.1182/blood-2007-07-100677 · Cited by 311 · see citing works

Hepatic HIF-2 regulates erythropoietic responses to hypoxia in renal anemia

Kapitsinou, P. P., Liu, Q., Unger, T. L., Rha, J., Davidoff, O., Keith, B., Epstein, J. A., Moores, S. L., Erickson-Miller, C. L., & Haase, V. H. (2010) · Blood · doi:10.1182/blood-2010-02-270322 · Cited by 307 · see citing works

Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias

Chen, J.-J. (2006) · Blood · doi:10.1182/blood-2006-08-041830 · Cited by 306 · see citing works

Diverse origins of the myofibroblast—implications for kidney fibrosis

Falke, L. L., Gholizadeh, S., Goldschmeding, R., Kok, R. J., & Nguyen, T. Q. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.246 · Cited by 297 · 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

The N-Terminal Domain of Janus Kinase 2 Is Required for Golgi Processing and Cell Surface Expression of Erythropoietin Receptor

Huang, L. J.-S., Constantinescu, S. N., & Lodish, H. F. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00401-4 · Cited by 294 · see citing works

The glucocorticoid receptor is required for stress erythropoiesisPreprint

Bauer, A., Tronche, F., Wessely, O., Kellendonk, C., Reichardt, H. M., Steinlein, P., Schütz, G., & Beug, H. (1999) · Genes & Development · doi:10.1101/gad.13.22.2996 · Cited by 291 · see citing works

A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression

Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281 · see citing works

Neurons and astrocytes express EPO mRNA: Oxygen-sensing mechanisms that involve the redox-state of the brain

Bernaudin, M., Bellail, A. C., Marti, H. H., Yvon, A., Vivien, D., Duchatelle, I., MacKenzie, E. T., & Petit, E. (2000) · Glia · doi:10.1002/(sici)1098-1136(200005)30:3 · Cited by 281 · see citing works

The HIF Signaling Pathway in Osteoblasts Directly Modulates Erythropoiesis through the Production of EPO

Rankin, E. B., Wu, C., Khatri, R., Wilson, T. L. S., Andersen, R., Araldi, E., Rankin, A. L., Yuan, J., Kuo, C. J., Schipani, E., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.051 · Cited by 278 · see citing works

Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency

Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274 · see citing works

Intrarenal oxygenation: unique challenges and the biophysical basis of homeostasis

Evans, R. G., Gardiner, B. S., Smith, D. W., & O'Connor, P. M. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90230.2008 · Cited by 274 · see citing works

Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases

Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274 · see citing works

Human marrow cells capable of erythropoietic differentiation in vitro: definition of three erythroid colony responses

Gregory, C., & Eaves, A. (1977) · Blood · doi:10.1182/blood.v49.6.855.855 · Cited by 274 · see citing works

Erythrocyte vesiculation: a self‐protective mechanism?

Willekens, F. L. A., Werre, J. M., Groenen‐Döpp, Y. A. M., Roerdinkholder‐Stoelwinder, B., de Pauw, B., & Bosman, G. J. C. G. M. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07055.x · Cited by 271 · see citing works

Apoptotic Role of Fas/Fas Ligand System in the Regulation of Erythropoiesis

Maria, R. D., Testa, U., Luchetti, L., Zeuner, A., Stassi, G., Pelosi, E., Riccioni, R., Felli, N., Samoggia, P., & Peschle, C. (1999) · Blood · doi:10.1182/blood.v93.3.796 · Cited by 267 · see citing works

Hypoxia-Inducible Factor-2α Mediates the Adaptive Increase of Intestinal Ferroportin During Iron Deficiency in Mice

Taylor, M., Qu, A., Anderson, E. R., Matsubara, T., Martin, A., Gonzalez, F. J., & Shah, Y. M. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.007 · Cited by 265 · 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

Estrogen-dependent Production of Erythropoietin in Uterus and Its Implication in Uterine Angiogenesis

Yasuda, Y., Masuda, S., Chikuma, M., Inoue, K., Nagao, M., & Sasaki, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25381 · Cited by 263 · see citing works

Quantitation of erythropoietin-producing cells in kidneys of mice by in situ hybridization: correlation with hematocrit, renal erythropoietin mRNA, and serum erythropoietin concentration

Koury, S. T., Koury, M., Bondurant, M. C., Caro, J., & Gräber, S. E. (1989) · Blood · doi:10.1182/blood.v74.2.645.645 · Cited by 252 · see citing works

Identification of a Multipotent Self-Renewing Stromal Progenitor Population during Mammalian Kidney Organogenesis

Kobayashi, A., Mugford, J. W., Krautzberger, A. M., Naiman, N., Liao, J., & McMahon, A. P. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.08.008 · Cited by 248 · see citing works

Cell-type-specific and hypoxia-inducible expression of the human erythropoietin gene in transgenic mice.

Semenza, G. L., Koury, S. T., Nejfelt, M. K., Gearhart, J. D., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8725 · Cited by 248 · see citing works

The liver as a source of extrarenal erythropoietin production

Fried, W. (1972) · Blood · doi:10.1182/blood.v40.5.671.671 · Cited by 235 · 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

Stress erythropoiesis: new signals and new stress progenitor cells

Paulson, R. F., Shi, L., & Wu, D.-C. (2011) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32834521c8 · Cited by 232 · see citing works

Hypoxia-inducible Factor-1 Deficiency Results in Dysregulated Erythropoiesis Signaling and Iron Homeostasis in Mouse Development

Yoon, D., Pastore, Y. D., Divoký, V., Liu, E., Mlodnicka, A., Rainey, K., Poňka, P., Semenza, G. L., Schumacher, A., & Prchal, J. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602329200 · Cited by 230 · see citing works

HLF/HIF‐2α is a key factor in retinopathy of prematurity in association with erythropoietin

Morita, M., Ohneda, O., Yamashita, T., Takahashi, S., Suzuki, N., Nakajima, O., Kawauchi, S., Ema, M., Shibahara, S., Udono, T., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg117 · Cited by 230 · see citing works

Localization of cells producing erythropoietin in murine liver by in situ hybridization [see comments]

Koury, S. T., Bondurant, M. C., Koury, M., & Semenza, G. (1991) · Blood · doi:10.1182/blood.v77.11.2497.bloodjournal77112497 · Cited by 220 · see citing works

Suppression of Fas-FasL coexpression by erythropoietin mediates erythroblast expansion during the erythropoietic stress response in vivo

Liu, Y. M., Pop, R., Sadegh, C., Brugnara, C., Haase, V. H., & Socolovsky, M. (2006) · Blood · doi:10.1182/blood-2005-11-4458 · Cited by 215 · see citing works

The IRP1-HIF-2α Axis Coordinates Iron and Oxygen Sensing with Erythropoiesis and Iron Absorption

Anderson, S. A., Nizzi, C. P., Chang, Y.-I., Deck, K. M., Schmidt, P. J., Galy, B., Damnernsawad, A., Broman, A. T., Kendziorski, C., Hentze, M. W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.007 · Cited by 211 · see citing works

Blunted erythropoietin response to anaemia in rheumatoid arthritis

Baer, A. N., Dessypris, E. N., Goldwasser, E., & Krantz, S. B. (1987) · British Journal of Haematology · doi:10.1111/j.1365-2141.1987.tb01344.x · Cited by 210 · see citing works

Maintenance by erythropoietin of viability and maturation of murine erythroid precursor cells

Koury, M. J., & Bondurant, M. C. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041370108 · Cited by 206 · see citing works

Repression via the GATA box is essential for tissue-specific erythropoietin gene expression

Obara, N., Suzuki, N., Kim, K., Nagasawa, T., Imagawa, S., & Yamamoto, M. P. (2008) · Blood · doi:10.1182/blood-2007-10-115857 · Cited by 206 · see citing works

In vivo and in vitro regulation of erythropoietin mRNA: measurement by competitive polymerase chain reaction

Fandrey, J., & Bunn, H. F. (1993) · Blood · doi:10.1182/blood.v81.3.617.617 · Cited by 204 · see citing works

Chronic IFN-γ production in mice induces anemia by reducing erythrocyte life span and inhibiting erythropoiesis through an IRF-1/PU.1 axis

Libregts, S. F., Gutiérrez, L., de Bruin, A. M., Wensveen, F. M., Papadopoulos, P., van Ijcken, W., Özgür, Z., Philipsen, S., & Nolte, M. A. (2011) · Blood · doi:10.1182/blood-2010-10-315218 · Cited by 204 · 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

Erythropoietin mRNA levels are governed by both the rate of gene transcription and posttranscriptional events

Goldberg, M., Gaut, C., & Bunn, H. F. (1991) · Blood · doi:10.1182/blood.v77.2.271.271 · Cited by 199 · see citing works

Pathogenesis of Renal Anemia

Nangaku, M., & Eckardt, K. (2006) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2006.06.001 · Cited by 196 · see citing works

Multilineage embryonic hematopoiesis requires hypoxic ARNT activity

Adelman, D. M., Maltepe, E., & Simon, M. C. (1999) · Genes &amp; Development · doi:10.1101/gad.13.19.2478 · Cited by 185 · see citing works

Plasticity of Renal Erythropoietin-Producing Cells Governs Fibrosis

Souma, T., Yamazaki, S., Moriguchi, T., Suzuki, N., Hirano, I., Pan, X., Minegishi, N., Abe, M., Kiyomoto, H., Ito, S., et al. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013010030 · Cited by 184 · 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

Cell-specific translational profiling in acute kidney injury

Liu, J., Krautzberger, A. M., Sui, S. H., Hofmann, O., Chen, Y., Baetscher, M., Grgic, I., Kumar, S., Humphreys, B. D., Hide, W. A., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci72126 · Cited by 181 · see citing works

Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling

Besson-Fournier, C., Latour, C., Kautz, L., Bertrand, J., Ganz, T., Roth, M.-P., & Coppin, H. (2012) · Blood · doi:10.1182/blood-2012-02-411470 · Cited by 179 · see citing works

Epidermal Sensing of Oxygen Is Essential for Systemic Hypoxic Response

Boutin, A. T., Weidemann, A., Fu, Z., Mesropian, L., Gradin, K., Jamora, C., Wiesener, M. S., Eckardt, K., Koch, C. J., Ellies, L. G., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.038 · Cited by 177 · see citing works

New insights into erythropoiesis

Koury, M. J., Sawyer, S. T., & Brandt, S. J. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200203000-00002 · Cited by 177 · 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

Stimulation of erythropoietin gene transcription during hypoxia and cobalt exposure

Schuster, S. J., Badiavas, E. V., Costa-Giomi, P., Weinmann, R. S., Erslev, A. J., & Caro, J. (1989) · Blood · doi:10.1182/blood.v73.1.13.13 · Cited by 174 · see citing works

Erythropoietin mRNA Expression in Human Fetal and Neonatal Tissue

Dame, C., Fahnenstich, H., Freitag, P., Hofmann, D., Abdul‐Nour, T., Bartmann, P., & Fandrey, J. (1998) · Blood · doi:10.1182/blood.v92.9.3218.421k11_3218_3225 · Cited by 172 · see citing works

Growth and Differentiation of Human Stem Cell Factor/Erythropoietin-Dependent Erythroid Progenitor Cells In Vitro

Panzenböck, B., Bartůněk, P., Mapara, M. Y., & Zenke, M. (1998) · Blood · doi:10.1182/blood.v92.10.3658 · Cited by 171 · see citing works

HIF prolyl hydroxylase inhibition results in endogenous erythropoietin induction, erythrocytosis, and modest fetal hemoglobin expression in rhesus macaques

Hsieh, M. M., Linde, N. S., Wynter, A., Metzger, M., Wong, C., Langsetmo, I., Lin, A., Smith, R., Rodgers, G. P., Donahue, R. E., et al. (2007) · Blood · doi:10.1182/blood-2007-02-073254 · Cited by 171 · see citing works

Hypoxia-enhanced Expression of the Proprotein Convertase Furin Is Mediated by Hypoxia-inducible Factor-1

McMahon, S., Grondin, F., McDonald, P. P., Richard, D. E., & Dubois, C. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413248200 · Cited by 170 · see citing works

Mimicking Hypoxia to Treat Anemia: HIF-Stabilizer BAY 85-3934 (Molidustat) Stimulates Erythropoietin Production without Hypertensive Effects

Flamme, I., Oehme, F., Ellinghaus, P., Jeske, M., Keldenich, J., & Thuß, U. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111838 · Cited by 170 · see citing works

Hypoxia-inducible factor-2α-expressing interstitial fibroblasts are the only renal cells that express erythropoietin under hypoxia-inducible factor stabilization

Paliege, A., Rosenberger, C., Bondke, A., Sciesielski, L. K., Shina, A., Heyman, S. N., Flippin, L. A., Arend, M., Klaus, S. J., & Bachmann, S. (2009) · Kidney International · doi:10.1038/ki.2009.460 · Cited by 169 · 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

Studies on Erythropoiesis

Goldwasser, E., Jacobson, L., Fried, W. I., & Plzak, L. F. (1958) · Blood · doi:10.1182/blood.v13.1.55.55 · Cited by 165 · see citing works

Reactivation of hepatic EPO synthesis in mice after PHD loss

Minamishima, Y. A., & Kaelin, W. G. (2010) · Science · doi:10.1126/science.1192811 · Cited by 163 · see citing works

Hepatic hypoxia-inducible factor-2 down-regulates hepcidin expression in mice through an erythropoietin-mediated increase in erythropoiesis

Mastrogiannaki, M., Matak, P., Mathieu, J. R. R., Delga, S., Mayeux, P., Vaulont, S., & Peyssonnaux, C. (2011) · Haematologica · doi:10.3324/haematol.2011.056119 · Cited by 161 · see citing works

Detection of erythropoietin in human liquor: Intrinsic erythropoietin production in the brain

Marti, H. H., Gassmann, M., Wenger, R. H., Kvietikova, I., Morganti-Kossmann, M. C., Kossmann, T., Trentz, O., & Bauer, C. (1997) · Kidney International · doi:10.1038/ki.1997.55 · Cited by 160 · see citing works

Indoxyl sulfate, a representative uremic toxin, suppresses erythropoietin production in a HIF-dependent manner

Chiang, C., Tanaka, T., Inagi, R., Fujita, T., & Nangaku, M. (2011) · Laboratory Investigation · doi:10.1038/labinvest.2011.114 · Cited by 155 · see citing works

Survival or death of individual proerythroblasts results from differing erythropoietin sensitivities: a mechanism for controlled rates of erythrocyte production

Kelley, L., Koury, M., Bondurant, M. C., Koury, S. T., Sawyer, S. T., & Wickrema, A. (1993) · Blood · doi:10.1182/blood.v82.8.2340.2340 · Cited by 154 · see citing works

Apoptosis of human erythroid colony‐forming cells is decreased by stem cell factor and insulin‐like growth factor I as well as erythropoietin

Muta, K., & Krantz, S. B. (1993) · Journal of Cellular Physiology · doi:10.1002/jcp.1041560207 · Cited by 151 · see citing works

Fas Ligand Is Present in Human Erythroid Colony-Forming Cells and Interacts With Fas Induced by Interferon γ to Produce Erythroid Cell Apoptosis

Dai, C., Price, J. O., Brunner, T., & Krantz, S. B. (1998) · Blood · doi:10.1182/blood.v91.4.1235 · Cited by 150 · see citing works

Cellular Trafficking and Degradation of Erythropoietin and Novel Erythropoiesis Stimulating Protein (NESP)

Gross, A. W., & Lodish, H. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510493200 · Cited by 149 · see citing works

Production and processing of erythropoietin receptor transcripts in brain

Chin, K., Yu, X., Beleslin‐Čokić, B. B., Liu, C., Shen, K., Mohrenweiser, H. W., & Noguchi, C. T. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00157-1 · Cited by 145 · see citing works

The von Hippel–Lindau Chuvash mutation promotes pulmonary hypertension and fibrosis in mice

Hickey, M. M., Richardson, T., Wang, T., Mosqueira, M., Arguiri, E., Yu, H. D., Yu, Q., Solomides, C., Morrisey, E. E., Khurana, T. S., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci36362 · Cited by 140 · see citing works

Iron supplementation to treat anemia in patients with chronic kidney disease

Besarab, A., & Coyne, D. W. (2010) · Nature Reviews Nephrology · doi:10.1038/nrneph.2010.139 · Cited by 139 · see citing works

Genetic determinants of Tibetan high-altitude adaptation

Simonson, T. S., McClain, D. A., Jorde, L. B., & Prchal, J. T. (2011) · Human Genetics · doi:10.1007/s00439-011-1109-3 · Cited by 137 · 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

Polycythemia in transgenic mice expressing the human erythropoietin gene.

Semenza, G. L., Traystman, M. D., Gearhart, J. D., & Antonarakis, S. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.7.2301 · Cited by 131 · see citing works

Normal and disordered reticulocyte maturation

Ney, P. A. (2011) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328345213e · Cited by 129 · see citing works

Erythropoietin production in kidney tubular cells

Maxwell, A. P., Lappin, T. R. J., Johnston, C. F., Bridges, J. M., & McGeown, M. G. (1990) · British Journal of Haematology · doi:10.1111/j.1365-2141.1990.tb06347.x · Cited by 126 · see citing works

Studies on erythropoiesis. VIII. The effect of nephrectomy on response to hypoxic anoxia.

Goldwasser, E., Fried, W. I., & Jacobson, L. (1958) · PubMed · Cited by 125 · see citing works

Human erythropoietin gene expression in transgenic mice: multiple transcription initiation sites and cis-acting regulatory elements.

Semenza, G. L., Dureza, R. C., Traystman, M. D., Gearhart, J. D., & Antonarakis, S. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.3.930 · Cited by 119 · see citing works

Hyperuricemia, hypertension, and proteinuria associated with high-altitude polycythemia

Jefferson, J. A., Escudero, E., Hurtado, M.-E., Kelly, J. P., Swenson, E. R., Wener, M. H., Burnier, M., Maillard, M. P., Schreiner, G. F., Schoene, R. B., et al. (2002) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2002.33380 · Cited by 117 · see citing works

FOG‐1 and GATA‐1 act sequentially to specify definitive megakaryocytic and erythroid progenitors

Mancini, E., Sanjuán-Pla, A., Luciani, L., Moore, S., Grover, A., Zay, A., Rasmussen, K. D., Luc, S., Bilbao, D., O’Carroll, D., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.390 · Cited by 117 · see citing works

Preischemic targeting of HIF prolyl hydroxylation inhibits fibrosis associated with acute kidney injury

Kapitsinou, P. P., Jaffe, J. T., Michael, M., Swan, C. E., Duffy, K. J., Erickson‐Miller, C. L., & Haase, V. H. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00667.2011 · Cited by 115 · see citing works

Hepcidin regulates ferroportin expression and intracellular iron homeostasis of erythroblasts

Zhang, D.-L., Senecal, T., Ghosh, M. C., Ollivierre-Wilson, H., Tu, T., & Rouault, T. A. (2011) · Blood · doi:10.1182/blood-2011-01-330241 · Cited by 113 · see citing works

Isolation and Characterization of Renal Erythropoietin-Producing Cells from Genetically Produced Anemia Mice

Pan, X., Suzuki, N., Hirano, I., Yamazaki, S., Minegishi, N., & Yamamoto, M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025839 · Cited by 113 · see citing works

ZFP36L2 is required for self-renewal of early burst-forming unit erythroid progenitors

Zhang, L., Prak, L., Rayon-Estrada, V., Thiru, P., Flygare, J., Lim, B., & Lodish, H. F. (2013) · Nature · doi:10.1038/nature12215 · Cited by 113 · see citing works

Regulation of Type II Transmembrane Serine Proteinase TMPRSS6 by Hypoxia-inducible Factors

Lakhal‐Littleton, S., Schödel, J., Townsend, A., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173096 · Cited by 113 · see citing works

Correction of Uremic Iron Deficiency Anemia in Hemodialyzed Patients: A Prospective Study

Fudin, R., Jaichenko, J., Shostak, A., Bennett, M., & Gotloib, L. (1998) · The Nephron journals/Nephron journals · doi:10.1159/000045053 · Cited by 109 · see citing works

Gene Expression Profiling of the Hypoxia Signaling Pathway in Hypoxia-Inducible Factor 1α Null Mouse Embryonic Fibroblasts

Vengellur, A., WOODS, B. G., Ryan, H. E., Johnson, R. S., & LaPres, J. J. (2003) · Gene Expression · doi:10.3727/000000003108749062 · Cited by 107 · see citing works

Regulation of erythropoietin production is related to proximal tubular function

Eckardt, K., Kurtz, A., & Bauer, C. (1989) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1989.256.5.f942 · Cited by 105 · see citing works

Erythropoietin gene expression in different areas of the developing human central nervous system

Dame, C., Bartmann, P., Wolber, E., Fahnenstich, H., Hofmann, D., & Fandrey, J. (2000) · Developmental Brain Research · doi:10.1016/s0165-3806(00)00118-8 · Cited by 102 · see citing works

The glial cell response is an essential component of hypoxia-induced erythropoiesis in mice

Weidemann, A., Kerdiles, Y. M., Knaup, K. X., Rafie, C. A., Boutin, A. T., Stockmann, C., Takeda, N., Scadeng, M., Shih, A. Y., Haase, V. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39378 · Cited by 100 · see citing works

Hepatic Erythropoietin Gene Regulation by GATA-4

Dame, C., Sola, M. C., Lim, K.-C., Leach, K. M., Fandrey, J., Ma, Y., Knöpfle, G., Engel, J. D., & Bungert, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310404200 · Cited by 99 · see citing works

Role of uremic toxins in exacerbating anemia in renal failure

Macdougall, I. C. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.59780067.x · Cited by 97 · see citing works

Multiple members of the TNF superfamily contribute to IFN-γ-mediated inhibition of erythropoiesis

Felli, N., Pedini, F., Zeuner, A., Petrucci, E., Testa, U., Conticello, C., Biffoni, M., Di Cataldo, A., Winkles, J. A., Peschle, C., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.3.1464 · Cited by 96 · see citing works

Abnormal erythropoiesis and the pathophysiology of chronic anemia

Koury, M. J. (2014) · Blood Reviews · doi:10.1016/j.blre.2014.01.002 · Cited by 96 · see citing works

HIF and pulmonary vascular responses to hypoxia

Shimoda, L. A., & Laurie, S. S. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00643.2013 · Cited by 95 · see citing works

Erythropoietin gene expression is suppressed after lipopolysaccharide or interleukin-1 beta injections in rats

Frede, S., Fandrey, J., Pagel, H., Hellwig, T., & JELKMANN, W. E. B. (1997) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1997.273.3.r1067 · Cited by 95 · see citing works

Expression of a homologously recombined erythopoietin-SV40 T antigen fusion gene in mouse liver: evidence for erythropoietin production by Ito cells

Maxwell, P. H., Ferguson, D. J. P., Osmond, M. K., Pugh, C. W., Heryet, A. R., Doe, B. G., Johnson, M., & Ratcliffe, P. J. (1994) · Blood · doi:10.1182/blood.v84.6.1823.1823 · Cited by 94 · see citing works

Excessive erythrocytosis, chronic mountain sickness, and serum cobalt levels

Jefferson, J. A., Escudero, E., Hurtado, A., Pando, J., Tapia, R., Swenson, E. R., Prchal, J. T., Schreiner, G. F., Schoene, R. B., Hurtoado, A., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07594-3 · Cited by 93 · see citing works

The oviduct produces erythropoietin in an estrogen- and oxygen-dependent manner

Masuda, S., Kobayashi, T., Chikuma, M., Nagao, M., & Sasaki, R. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.6.e1038 · Cited by 93 · see citing works

HIF-Prolyl Hydroxylases in the Rat Kidney

Schödel, J., Klanke, B., Weidemann, A., Buchholz, B., Bernhardt, W. M., Bertog, M., Amann, K., Korbmacher, C., Wiesener, M. S., Warnecke, C., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080687 · Cited by 89 · see citing works

Erythropoietin stimulates spleen BMP4-dependent stress erythropoiesis and partially corrects anemia in a mouse model of generalized inflammation

Millot, S., Andrieu, V., Lettéron, P., Lyoumi, S., Hurtado-Nédelec, M., Karim, Z., Thibaudeau, O., Bennada, S., Charrier, J.-L., Lasocki, S., et al. (2010) · Blood · doi:10.1182/blood-2010-04-281840 · Cited by 87 · 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

A mouse model of adult-onset anaemia due to erythropoietin deficiency

Yamazaki, S., Souma, T., Hirano, I., Pan, X., Minegishi, N., Suzuki, N., & Yamamoto, M. P. (2013) · Nature Communications · doi:10.1038/ncomms2950 · Cited by 81 · see citing works

Pathophysiological Consequences of HIF Activation

Haase, V. H. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05030.x · Cited by 81 · 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

Erythropoietin: the story of hypoxia and a finely regulated hematopoietic hormone

Koury, M. J. (2005) · Experimental Hematology · doi:10.1016/j.exphem.2005.06.031 · Cited by 78 · see citing works

Single-dose Pharmacokinetics of Recombinant Human Erythropoietin in Patients with Various Degrees of Renal Failure

Kindler, J., Eckardt, K., Ehmer, B., Jandeleit, K., Kurtz, A., Schreiber, A., Scigalla, P., & Sieberth, H. G. (1989) · Nephrology Dialysis Transplantation · doi:10.1093/oxfordjournals.ndt.a091888 · Cited by 78 · see citing works

Autoimmune diseases caused by defects in clearing dead cells and nuclei expelled from erythroid precursors

Nagata, S. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00571.x · Cited by 77 · see citing works

Erythropoietin expression in primary rat Sertoli and peritubular myoid cells

Magnanti, M., Gandini, O., Giuliani, L., Gazzaniga, P., Marti, H. H., Gradilone, A., Frati, L., Aglianò, A. M., & Gassmann, M. (2001) · Blood · doi:10.1182/blood.v98.9.2872 · Cited by 77 · see citing works

Endogenous Urate Production Augments Plasma Antioxidant Capacity in Healthy Lowland Subjects Exposed to High Altitude

Baillie, J. K., Bates, M. G. D., Thompson, A. A. R., Waring, W. S., Partridge, R. W., Schnopp, M. F., Simpson, A., Gulliver-Sloan, F., Maxwell, S. R. J., & Webb, D. J. (2007) · CHEST Journal · doi:10.1378/chest.06-2235 · Cited by 77 · see citing works

Gene expression profiling of hypoxia signaling in human hepatocellular carcinoma cells

Vengellur, A., Phillips, J. M., Hogenesch, J. B., & LaPres, J. J. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00045.2004 · Cited by 72 · see citing works

Human hair follicles are an extrarenal source and a nonhematopoietic target of erythropoietin

Bodó, E., Kromminga, A., Funk, W., Laugsch, M., Duske, U., JELKMANN, W. E. B., & Paus, R. (2007) · The FASEB Journal · doi:10.1096/fj.07-8628com · Cited by 71 · see citing works

Mechanism of the Erythropoietic Effect of Cobalt

Goldwasser, E., Jacobson, L., Fried, W. I., & Plzak, L. F. (1957) · Science · doi:10.1126/science.125.3257.1085 · Cited by 71 · see citing works

HIF isoforms in the skin differentially regulate systemic arterial pressure

Cowburn, A. S., Takeda, N., Boutin, A. T., Kim, J., Sterling, J. C., Nakasaki, M., Southwood, M. R., Goldrath, A. W., Jamora, C., Nizet, V., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306942110 · Cited by 68 · see citing works

Iron Requirements in Hemodialysis

SARGENT, J. A., & Acchiardo, S. R. (2004) · Blood Purification · doi:10.1159/000074931 · Cited by 66 · see citing works

Hypoxic up-regulation of erythroid 5-aminolevulinate synthase

Höfer, T., Wenger, R. H., Kramer, M. F., Ferreira, G. C., & Gassmann, M. (2002) · Blood · doi:10.1182/blood-2002-03-0773 · Cited by 65 · see citing works

Bcl-xL prevents apoptosis of late-stage erythroblasts but does not mediate the antiapoptotic effect of erythropoietin

Rhodes, M., Kopsombut, P., Bondurant, M. C., Price, J. O., & Koury, M. J. (2005) · Blood · doi:10.1182/blood-2004-11-4344 · Cited by 65 · see citing works

Specific contribution of the erythropoietin gene 3' enhancer to hepatic erythropoiesis after late embryonic stages

Suzuki, N., Obara, N., Pan, X., Watanabe, M., Jishage, K.-I., Minegishi, N., & Yamamoto, M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05463-11 · Cited by 65 · see citing works

Transgenic mice carrying the erythropoietin gene promoter linked to lacZ express the reporter in proximal convoluted tubule cells after hypoxia

Loya, F., Yang, Y., Lin, H., Goldwasser, E., & Albitar, M. X. (1994) · Blood · doi:10.1182/blood.v84.6.1831.1831 · Cited by 62 · see citing works

Intolerability of cobalt salt as erythropoietic agent

Ebert, B., & JELKMANN, W. E. B. (2013) · Drug Testing and Analysis · doi:10.1002/dta.1528 · Cited by 62 · see citing works

Erythropoietin production in neuroepithelial and neural crest cells during primitive erythropoiesis

Suzuki, N., Hirano, I., Pan, X., Minegishi, N., & Yamamoto, M. P. (2013) · Nature Communications · doi:10.1038/ncomms3902 · Cited by 61 · see citing works

The effect of HIF on metabolism and immunity

Taylor, C. T., & Scholz, C. C. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00587-8 · Cited by 517 · see citing works

Metalloimmunology: The metal ion-controlled immunity

Wang, C., Zhang, R., Wei, X., Lv, M., & Jiang, Z. (2019) · Advances in immunology · doi:10.1016/bs.ai.2019.11.007 · Cited by 300 · see citing works

The multifaceted role of iron in renal health and disease

van Swelm, R. P. L., Wetzels, J. F. M., & Swinkels, D. W. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0197-5 · Cited by 279 · see citing works

Hypoxia-induced signaling in the cardiovascular system: pathogenesis and therapeutic targets

Zhao, Y., Xiong, W., Li, C., Zhao, R., Lu, H., Song, S., Zhou, Y., Hu, Y., Shi, B., & Ge, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01652-9 · Cited by 264 · see citing works

Daprodustat for the Treatment of Anemia in Patients Undergoing Dialysis

Singh, A. K., Carroll, K., Perkovic, V., Solomon, S. D., Jha, V., Johansen, K. L., Lópes, R. D., Macdougall, I. C., Obrador, G. T., Waikar, S. S., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2113379 · Cited by 254 · see citing works

Vadadustat, a novel oral HIF stabilizer, provides effective anemia treatment in nondialysis-dependent chronic kidney disease

Pérgola, P. E., Spinowitz, B., Hartman, C., Maroni, B. J., & Haase, V. H. (2016) · Kidney International · doi:10.1016/j.kint.2016.07.019 · Cited by 239 · see citing works

Kidney disease and obesity: epidemiology, mechanisms and treatment

Câmara, N. O. S., Iseki, K., Kramer, H., Liu, Z.-H., & Sharma, K. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.191 · Cited by 238 · see citing works

Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials

Yeh, T., Leissing, T. M., Abboud, M. I., Thinnes, C. C., Atasoylu, O., Holt‐Martyn, J. P., Zhang, D., Tumber, A., Lippl, K., Lohans, C. T., et al. (2017) · Chemical Science · doi:10.1039/c7sc02103h · Cited by 244 · see citing works

Controversies in optimal anemia management: conclusions from a Kidney Disease: Improving Global Outcomes (KDIGO) Conference

Babitt, J. L., Eisenga, M. F., Haase, V. H., Kshirsagar, A. V., Levin, A., Locatelli, F., Małyszko, J., Swinkels, D. W., Tarng, D., Cheung, M., et al. (2021) · Kidney International · doi:10.1016/j.kint.2021.03.020 · Cited by 222 · see citing works

Safety and Efficacy of Vadadustat for Anemia in Patients Undergoing Dialysis

Eckardt, K., Agarwal, R., Aswad, A., Awad, A., Block, G. A., Bacci, M. R., Farag, Y. M. K., Fishbane, S. N., Hubert, H., Jardine, A. G., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2025956 · Cited by 222 · see citing works

Phase 2 studies of oral hypoxia-inducible factor prolyl hydroxylase inhibitor FG-4592 for treatment of anemia in China

Chen, N., Qian, J., Chen, J., Yu, X., Mei, C., Hao, C., Jiang, G., Lin, H., Zhang, X., Zuo, L., et al. (2017) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfx011 · Cited by 205 · see citing works

Hypoxia-inducible factor–prolyl hydroxylase inhibitors in the treatment of anemia of chronic kidney disease

Haase, V. H. (2021) · Kidney International Supplements · doi:10.1016/j.kisu.2020.12.002 · Cited by 203 · see citing works

Hypoxia-Inducible Factor Activators in Renal Anemia: Current Clinical Experience

Sanghani, N. S., & Haase, V. H. (2019) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2019.04.004 · Cited by 187 · see citing works

Chronic Kidney Disease: Role of Diet for a Reduction in the Severity of the Disease

Naber, T., & Purohit, S. B. (2021) · Nutrients · doi:10.3390/nu13093277 · Cited by 193 · see citing works

Hypoxia and chronic kidney disease

Wang, B., Li, Z., Zhang, Y., Wen, Y., Gao, Y.-M., & Liu, B. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103942 · Cited by 171 · see citing works

HIF‐prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism

Haase, V. H. (2017) · Hemodialysis International · doi:10.1111/hdi.12567 · Cited by 161 · see citing works

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

Roxadustat Versus Epoetin Alfa for Treating Anemia in Patients with Chronic Kidney Disease on Dialysis: Results from the Randomized Phase 3 ROCKIES Study

Fishbane, S., Pollock, C. A., El-Shahawy, M., Escudero, E. T., Rastogi, A., Van, B. P., Frison, L., Houser, M., Pola, M., Little, D. J., et al. (2022) · Journal of the American Society of Nephrology · doi:10.1681/asn.2020111638 · Cited by 155 · see citing works

Roxadustat for anemia in patients with end-stage renal disease incident to dialysis

Provenzano, R., Shutov, E. V., Еремеева, Л. Ф., Korneyeva, S., Poole, L., Saha, G. C., Bradley, C., Eyassu, M., Besarab, A., Leong, R., et al. (2021) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfab051 · Cited by 136 · see citing works

The Endothelial Prolyl-4-Hydroxylase Domain 2/Hypoxia-Inducible Factor 2 Axis Regulates Pulmonary Artery Pressure in Mice

Kapitsinou, P. P., Rajendran, G., Astleford, L., Michael, M., Schonfeld, M. P., Fields, T. A., Shay, S. D., French, J. L., West, J. D., & Haase, V. H. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.01055-15 · Cited by 131 · see citing works

Anemia in chronic kidney disease

Atkinson, M. A., & Warady, B. A. (2017) · Pediatric Nephrology · doi:10.1007/s00467-017-3663-y · Cited by 135 · see citing works

Pharmacological targeting of the HIF hydroxylases – A new field in medicine development

Chan, M. C., Holt‐Martyn, J. P., Schofield, C. J., & Ratcliffe, P. J. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.01.001 · Cited by 126 · see citing works

Iron and innate antimicrobial immunity-depriving the pathogen, defending the host

Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · see citing works

The Mesangial cell — the glomerular stromal cell

Avraham, S., Korin, B., Chung, J.-J., Oxburgh, L. H., & Shaw, A. S. (2021) · Nature Reviews Nephrology · doi:10.1038/s41581-021-00474-8 · Cited by 122 · see citing works

Hypoxia, HIF, and Associated Signaling Networks in Chronic Kidney Disease

Liu, J., Wei, Q., Guo, C., Dong, G., Liu, Y., Tang, C., & Dong, Z. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050950 · Cited by 115 · see citing works

Protective Role of Histidine Supplementation Against Oxidative Stress Damage in the Management of Anemia of Chronic Kidney Disease

Vera‐Aviles, M., Vantana, E., Kardinasari, E., Koh, N. L., & Latunde-Dada, G. O. (2018) · Pharmaceuticals · doi:10.3390/ph11040111 · Cited by 113 · see citing works

Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases

Chan, M. C., Ilott, N. E., Schödel, J., Sims, D., Tumber, A., Lippl, K., Mole, D. R., Pugh, C. W., Ratcliffe, P. J., Ponting, C. P., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.749291 · Cited by 111 · see citing works

The role of HIF proteins in maintaining the metabolic health of the intervertebral disc

Silagi, E. S., Schipani, E., Shapiro, I. M., & Risbud, M. V. (2021) · Nature Reviews Rheumatology · doi:10.1038/s41584-021-00621-2 · Cited by 108 · see citing works

Effects of Molidustat in the Treatment of Anemia in CKD

Macdougall, I. C., Akizawa, T., Berns, J. S., Bernhardt, T., & Krueger, T. (2018) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.02510218 · Cited by 106 · see citing works

Distinct subpopulations of FOXD1 stroma-derived cells regulate renal erythropoietin

Kobayashi, H., Liu, Q., Binns, T. C., Urrutia, A. A., Davidoff, O., Kapitsinou, P. P., Pfaff, A. S., Olauson, H., Wernerson, A. M., Fogo, A. B., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci83551 · Cited by 104 · see citing works

A Randomized Trial of Roxadustat in Anemia of Kidney Failure: SIERRAS Study

Charytan, C., Manllo-Karim, R., Martin, E. R., Steer, D. L., Bernardo, M. V., Dua, S., Moustafa, M. A., Saha, G. C., Bradley, C., Eyassu, M., et al. (2021) · Kidney International Reports · doi:10.1016/j.ekir.2021.04.007 · Cited by 102 · see citing works

The Role of Fibroblast Growth Factor 23 in Inflammation and Anemia

Czaya, B. A., & Faul, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174195 · Cited by 99 · see citing works

Managing Anemia across the Stages of Kidney Disease in Those Hyporesponsive to Erythropoiesis-Stimulating Agents

Weir, M. R. (2021) · American Journal of Nephrology · doi:10.1159/000516901 · Cited by 97 · see citing works

Efficacy and Cardiovascular Safety of Roxadustat for Treatment of Anemia in Patients with Non–Dialysis-Dependent CKD

Provenzano, R., Szczech, L. A. M., Leong, R., Saikali, K. G., Zhong, M., Lee, T. T., Little, D. J., Houser, M. T., Frison, L., Houghton, J., et al. (2021) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.16191020 · Cited by 94 · see citing works

Positive Iron Balance in Chronic Kidney Disease: How Much is Too Much and How to Tell?

Wish, J. B., Aronoff, G. R., Bacon, B. R., Brugnara, C., Eckardt, K., Ganz, T., Macdougall, I. C., Núñez, J. E., Perahia, A. J., & Wood, J. C. (2018) · American Journal of Nephrology · doi:10.1159/000486968 · Cited by 87 · see citing works

Oxygen‐sensing mechanisms in cells

Wilson, J. W., Shakir, D., Batie, M., Frost, M., & Rocha, S. (2020) · The FEBS Journal · doi:10.1111/febs.15374 · Cited by 86 · 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

Hypoxia Pathway Proteins are Master Regulators of Erythropoiesis

Watts, D., Gaete, D., Rodriguez, D., Hoogewijs, D., Rauner, M., Sormendi, S., & Wielockx, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218131 · Cited by 86 · see citing works

Inflammatory bone marrow microenvironment

Leimkühler, N. B., & Schneider, R. K. (2019) · Hematology · doi:10.1182/hematology.2019000045 · Cited by 82 · see citing works

Treatment of Renal Anemia with Roxadustat: Advantages and Achievement

Li, Z., Tu, Y., & Liu, B. (2020) · Kidney Diseases · doi:10.1159/000504850 · Cited by 83 · see citing works

miR-429 regulates the transition between hypoxia-inducible factor (HIF)1A and HIF3A expression in human endothelial cells

Janaszak-Jasiecka, A., Bartoszewska, S., Kochan, K., Piotrowski, A., Kalinowski, L., Kamysz, W., Ochocka, R. J., Bartoszewski, R., & Collawn, J. F. (2016) · Scientific Reports · doi:10.1038/srep22775 · Cited by 81 · see citing works

Molecular mechanisms of ischemic preconditioning in the kidney

Kapitsinou, P. P., & Haase, V. H. (2015) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00224.2015 · Cited by 81 · see citing works

Efficacy and Safety of Daprodustat for Treatment of Anemia of Chronic Kidney Disease in Incident Dialysis Patients

Singh, A. K., Čižman, B., Carroll, K., McMurray, J. J. V., Perkovic, V., Jha, V., Johansen, K. L., Lópes, R. D., Macdougall, I. C., Obrador, G. T., et al. (2022) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2022.0605 · Cited by 80 · see citing works

Understanding How Minerals Contribute to Optimal Immune Function

Ştefanache, A., Lungu, I. I., Butnariu, I.-A., Călin, G., Guțu, C., Marcu, C., Grierosu, C., Goroftei, E. R. B., Duceac, L.-D., Dabija, M. G., et al. (2023) · Journal of Immunology Research · doi:10.1155/2023/3355733 · Cited by 91 · see citing works

Metal-based nano-vaccines for cancer immunotherapy

Li, J., Ren, H., & Zhang, Y. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214345 · Cited by 79 · see citing works

Uremic Toxins Affect Erythropoiesis during the Course of Chronic Kidney Disease: A Review

Hamza, E., Metzinger, L., & Meuth, V. M. (2020) · Cells · doi:10.3390/cells9092039 · Cited by 77 · see citing works

Ferroptosis: an important player in the inflammatory response in diabetic nephropathy

Li, J., Li, L., Zhang, Z., Chen, P., Shu, H., Yang, C., Chu, Y., & Liu, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1294317 · Cited by 82 · see citing works

KDIGO 2026 Clinical Practice Guideline for the Management of Anemia in Chronic Kidney Disease (CKD)

Tonelli, M. A., Berns, J. B., Bozkurt, B., Cheung, R., Cuevas, Y., Effa, E. E., Eisenga, M. F., Fishbane, S., Ginzburg, Y. Z., Haase, V. H., et al. (2026) · Kidney International · doi:10.1016/j.kint.2025.06.006 · Cited by 96 · see citing works

Efficacy and safety of HIF prolyl-hydroxylase inhibitor vs epoetin and darbepoetin for anemia in chronic kidney disease patients not undergoing dialysis: A network meta-analysis

Zheng, Q., Yang, H., Sun, L., Wei, R., Fu, X., Wang, Y., Huang, Y., Liu, Y., & Liu, W. J. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105020 · Cited by 76 · see citing works

Iron-Deficiency Anemia in CKD: A Narrative Review for the Kidney Care Team

Hain, D. J., Bednarski, D., Cahill, M. L., Dix, A., Foote, B. S., Haras, M. S., Pace, R. C., & Gutiérrez, O. M. (2023) · Kidney Medicine · doi:10.1016/j.xkme.2023.100677 · Cited by 89 · see citing works

Effects of vadadustat on hemoglobin concentrations in patients receiving hemodialysis previously treated with erythropoiesis-stimulating agents

Haase, V. H., Chertow, G. M., Block, G. A., Pérgola, P. E., deGoma, E. M., Khawaja, Z., Sharma, A. K., Maroni, B. J., & McCullough, P. A. (2018) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfy055 · Cited by 72 · see citing works

The Role of Hypoxia-Inducible Factor-1 Alpha in Renal Disease

Liu, H., Li, Y., & Xiong, J. (2022) · Molecules · doi:10.3390/molecules27217318 · Cited by 73 · 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

Anemia of Inflammation with An Emphasis on Chronic Kidney Disease

Begum, S., & Latunde-Dada, G. O. (2019) · Nutrients · doi:10.3390/nu11102424 · Cited by 77 · see citing works

Renal epithelium regulates erythropoiesis via HIF-dependent suppression of erythropoietin

Farsijani, N., Liu, Q., Kobayashi, H., Davidoff, O., Sha, F., Fandrey, J., Ikizler, T. A., O'Connor, P. M., & Haase, V. H. (2016) · Journal of Clinical Investigation · doi:10.1172/jci74997 · Cited by 67 · see citing works

Efficacy and safety of vadadustat compared with darbepoetin alfa in Japanese anemic patients on hemodialysis: a Phase 3, multicenter, randomized, double-blind study

Nangaku, M., Kondo, K., Ueta, K., Kokado, Y., Kaneko, G., Matsuda, H., Kawaguchi, Y., & Komatsu, Y. (2021) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfab055 · Cited by 65 · see citing works

Therapeutic targeting of the HIF oxygen-sensing pathway: Lessons learned from clinical studies

Haase, V. H. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.004 · Cited by 64 · see citing works

Hypoxia-inducible factor stabilizers for treating anemia of chronic kidney disease

Hasegawa, S., Tanaka, T., & Nangaku, M. (2018) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000000431 · Cited by 62 · see citing works

Developmental differences between neonatal and adult human erythropoiesis

Yan, H., Hale, J., Jaffray, J., Li, J., Wang, Y., Huang, Y., An, X., Hillyer, C. D., Wang, N., Kinet, S., et al. (2017) · American Journal of Hematology · doi:10.1002/ajh.25015 · Cited by 61 · see citing works

Biological basis for efficacy of activin receptor ligand traps in myelodysplastic syndromes

Verma, A. K., Suragani, R. N. V. S., Aluri, S., Shah, N. N., Bhagat, T. D., Alexander, M. J., Komrokji, R. S., & Kumar, R. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133678 · Cited by 59 · see citing works

Desidustat in Anemia due to Dialysis-Dependent Chronic Kidney Disease: A Phase 3 Study (DREAM-D)

Gang, S. D., Khetan, P., Varade, D., Chinta, V. R., Mavani, S., Gupta, U. C., Reddy, S. V. K., Rajanna, S., Jeloka, T. K., Ruhela, V., et al. (2022) · American Journal of Nephrology · doi:10.1159/000523949 · Cited by 56 · see citing works

Chronic kidney disease in children: an update

Cirillo, L., Chiara, L. D., Innocenti, S., Errichiello, C., Romagnani, P., & Becherucci, F. (2023) · Clinical Kidney Journal · doi:10.1093/ckj/sfad097 · Cited by 65 · see citing works

Efficacy and Safety of Molidustat for Anemia in ESA-Naive Nondialysis Patients: A Randomized, Phase 3 Trial

Yamamoto, H., Nobori, K., Matsuda, Y., Hayashi, Y., Hayasaki, T., & Akizawa, T. (2021) · American Journal of Nephrology · doi:10.1159/000518071 · Cited by 56 · see citing works

A Phase 3 Study of Enarodustat (JTZ-951) in Japanese Hemodialysis Patients for Treatment of Anemia in Chronic Kidney Disease: SYMPHONY HD Study

Akizawa, T., Nangaku, M., Yamaguchi, T., Koretomo, R., Maeda, K., Miyazawa, Y., & Hirakata, H. (2021) · Kidney Diseases · doi:10.1159/000517053 · Cited by 54 · see citing works

Induction of erythropoiesis by hypoxia-inducible factor prolyl hydroxylase inhibitors without promotion of tumor initiation, progression, or metastasis in a VEGF-sensitive model of spontaneous breast cancer

Seeley, T. W., Sternlicht, M. D., Klaus, S. J., Neff, T. B., & Liu, D. Y. (2017) · Hypoxia · doi:10.2147/hp.s130526 · Cited by 54 · see citing works

Evaluation of the Carcinogenic Potential of Roxadustat (FG-4592), a Small Molecule Inhibitor of Hypoxia-Inducible Factor Prolyl Hydroxylase in CD-1 Mice and Sprague Dawley Rats

Beck, J., Henschel, C., Chou, J., Lin, A., & del Balzo, U. (2017) · International Journal of Toxicology · doi:10.1177/1091581817737232 · Cited by 51 · see citing works

The profibrotic effects of MK‐8617 on tubulointerstitial fibrosis mediated by the KLF5 regulating pathway

Li, Z., Lv, L., Wang, B., Tang, T., Ye, F., Cao, J., Jiang, L., Sun, Y., Liu, H. S., Zhang, X., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201901087rr · Cited by 50 · see citing works

Vitamin C: From nutrition to oxygen sensing and epigenetics

Kietzmann, T. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102753 · Cited by 51 · 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

Roxadustat (FG-4592) treatment for anemia in dialysis-dependent (DD) and not dialysis-dependent (NDD) chronic kidney disease patients: A systematic review and meta‐analysis

Liu, J., Zhang, A., Hayden, J. C., Bhagavathula, A. S., Alshehhi, F., Rinaldi, G., Kontogiannis, V., & Rahmani, J. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104747 · Cited by 45 · see citing works

VEGF expands erythropoiesis via hypoxia-independent induction of erythropoietin in noncanonical perivascular stromal cells

Greenwald, A., Licht, T., Kumar, S., Oladipupo, S. S., Iyer, S., Grunewald, M., & Keshet, E. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20180752 · Cited by 44 · see citing works

Hypoxia in Atherogenesis

Ferns, G. A., & Heikal, L. (2016) · Angiology · doi:10.1177/0003319716662423 · Cited by 44 · see citing works

Prolyl-4-hydroxylase 2 and 3 coregulate murine erythropoietin in brain pericytes

Urrutia, A. A., Afzal, A., Nelson, J., Davidoff, O., Gross, K. W., & Haase, V. H. (2016) · Blood · doi:10.1182/blood-2016-05-713545 · Cited by 44 · see citing works

Roxadustat in the treatment of anaemia in chronic kidney disease

Vecchio, L. D., & Locatelli, F. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1417386 · Cited by 43 · see citing works

The Use of Erythropoiesis-Stimulating Agents in Patients With CKD and Cancer: A Clinical Approach

Thavarajah, S., & Choi, M. J. (2019) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2019.04.022 · Cited by 43 · see citing works

The prolyl hydroxylase inhibitor roxadustat: Paradigm in drug discovery and prospects for clinical application beyond anemia

Su, K., Li, Z., Yu, Y.-C., & Zhang, X. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.04.017 · Cited by 42 · see citing works

Three Times Weekly Dosing of Daprodustat versus Conventional Epoetin for Treatment of Anemia in Hemodialysis Patients

Coyne, D. W., Singh, A. K., Lópes, R. D., Bailey, C. K., Dimino, T. L., Huang, C., Connaire, J. J., Rastogi, A., Kim, S.-G., Orías, M., et al. (2022) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.00550122 · Cited by 42 · see citing works

Iron attenuates erythropoietin production by decreasing hypoxia-inducible transcription factor 2α concentrations in renal interstitial fibroblasts

Suzuki, N., Matsuo-Tezuka, Y., Sasaki, Y., Sato, K., Miyauchi, K., Kato, K., Saito, S., Shimonaka, Y., Hirata, M., & Yamamoto, M. P. (2018) · Kidney International · doi:10.1016/j.kint.2018.06.028 · Cited by 37 · see citing works

EPO synthesis induced by HIF‐PHD inhibition is dependent on myofibroblast transdifferentiation and colocalizes with non‐injured nephron segments in murine kidney fibrosis

Kobayashi, H., Davidoff, O., Pujari‐Palmer, S., Drevin, M., & Haase, V. H. (2022) · Acta Physiologica · doi:10.1111/apha.13826 · Cited by 36 · see citing works

Nanoengineered injectable hydrogels derived from layered double hydroxides and alginate for sustained release of protein therapeutics in tissue engineering applications

Phan, V. H. G., Duong, H. S., Le, Q.-G. T., Janarthanan, G., Vijayavenkataraman, S., Nguyen, H.-N. H., Nguyen, B.-P. T., Manivasagan, P., Jang, E., Li, Y., et al. (2023) · Journal of Nanobiotechnology · doi:10.1186/s12951-023-02160-2 · Cited by 34 · see citing works

Kinetic parameters of human aspartate/asparagine–β-hydroxylase suggest that it has a possible function in oxygen sensing

Brewitz, L., Tumber, A., & Schofield, C. J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012202 · Cited by 34 · see citing works

Investigational therapies for renal disease-induced anemia

Schmid, H., & JELKMANN, W. E. B. (2016) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2016.1182981 · Cited by 33 · see citing works

Iron Regulation by Molidustat, a Daily Oral Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitor, in Patients with Chronic Kidney Disease

Akizawa, T., Macdougall, I. C., Berns, J. S., Yamamoto, H., Taguchi, M., Iekushi, K., & Bernhardt, T. (2019) · The Nephron journals/Nephron journals · doi:10.1159/000502012 · Cited by 33 · see citing works

Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors

Brewitz, L., Tumber, A., Pfeffer, I., McDonough, M. A., & Schofield, C. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-65123-9 · Cited by 33 · see citing works

Tracking erythroid progenitor cells in times of need and times of plenty

Koury, M. J. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.10.007 · Cited by 33 · see citing works

Intestinal oxygen utilisation and cellular adaptation during intestinal ischaemia–reperfusion injury

Barakakis, P. A., Mavridis, T., Chlorogiannis, D., Barakakis, G., Laou, E., Sessler, D. I., Gkiokas, G., & Chalkias, A. F. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.70136 · Cited by 32 · see citing works

HIF hydroxylase inhibitors decrease cellular oxygen consumption depending on their selectivity

Sulser, P., Pickel, C., Günter, J., Leissing, T. M., Crean, D., Schofield, C. J., Wenger, R. H., & Scholz, C. C. (2019) · The FASEB Journal · doi:10.1096/fj.201902240r · Cited by 30 · see citing works

Kidney pericyte hypoxia-inducible factor regulates erythropoiesis but not kidney fibrosis

Pan, S., Tsai, P., Chou, Y., Chang, Y., Chang, F., Chiu, Y., Chiang, W., Hsu, T., Chen, Y., Chu, T., et al. (2021) · Kidney International · doi:10.1016/j.kint.2021.01.017 · Cited by 30 · see citing works

A network meta-analysis of the efficacy of hypoxia-inducible factor prolyl-hydroxylase inhibitors in dialysis chronic kidney disease

Chen, J., Shou, X., Xu, Y., Jin, L., Zhu, C., Ye, X., Mei, Z., & Chen, P. (2023) · Aging · doi:10.18632/aging.204611 · Cited by 30 · see citing works

Fount, fate, features, and function of renal erythropoietin-producing cells

Dahl, S. L., Bapst, A. M., Khodo, S. N., Scholz, C. C., & Wenger, R. H. (2022) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-022-02714-7 · Cited by 29 · see citing works

Discovery of a Potent and Orally Bioavailable Hypoxia-Inducible Factor 2α (HIF-2α) Agonist and Its Synergistic Therapy with Prolyl Hydroxylase Inhibitors for the Treatment of Renal Anemia

Yu, Y.-C., Yang, F., Yu, Q., Liu, S., Wu, C., Su, K., Yang, L., Bao, X., Li, Z., Li, X., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01479 · Cited by 28 · see citing works

Fate‐mapping of erythropoietin‐producing cells in mouse models of hypoxaemia and renal tissue remodelling reveals repeated recruitment and persistent functionality

Dahl, S. L., Pfundstein, S., Hunkeler, R., Dong, X., Knöpfel, T., Spielmann, P., Scholz, C. C., Nolan, K. A., & Wenger, R. H. (2022) · Acta Physiologica · doi:10.1111/apha.13768 · Cited by 28 · see citing works

VHL-recruiting PROTAC attenuates renal fibrosis and preserves renal function via simultaneous degradation of Smad3 and stabilization of HIF-2α

Yang, J., Ruan, Y., Wang, D., Fan, J., Luo, N., Chen, H., Li, X., Chen, W., & Wang, X. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00936-x · Cited by 27 · see citing works

Stabilization of hypoxia‐inducible factor 1α by cobalt chloride impairs podocyte morphology and slit‐diaphragm function

Nakuluri, K., Mukhi, D., Mungamuri, S. K., & Pasupulati, A. K. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28041 · Cited by 27 · see citing works

Effect of hypoxia-inducible factor-prolyl hydroxylase inhibitors on anemia in patients with CKD: a meta-analysis of randomized controlled trials including 2804 patients

Wang, B., Yin, Q., Han, Y., Wu, M., Li, Z., Tu, Y., Zhou, L., Wei, Q., Liu, H., Tang, R., et al. (2020) · Renal Failure · doi:10.1080/0886022x.2020.1811121 · Cited by 26 · see citing works

Lineage tracing analysis defines erythropoietin-producing cells as a distinct subpopulation of resident fibroblasts with unique behaviors

Kaneko, K., Sato, Y., Uchino, E., Toriu, N., Shigeta, M., Kiyonari, H., Endo, S., Fukuma, S., & Yanagita, M. (2022) · Kidney International · doi:10.1016/j.kint.2022.04.026 · Cited by 27 · see citing works

Anemia and Hypoxia Impact on Chronic Kidney Disease Onset and Progression: Review and Updates

Habas, E. M., Adab, A. A., Arryes, M., Alfitori, G. B., Farfar, K. L., Habas, A. M., Akbar, R. A., Rayani, A., Habas, E., & Elzouki, A. (2023) · Cureus · doi:10.7759/cureus.46737 · Cited by 35 · see citing works

Integrative view on how erythropoietin signaling controls transcription patterns in erythroid cells

Perreault, A. A., & Venters, B. J. (2018) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000415 · Cited by 27 · see citing works

Orchestrated regulation of iron trafficking proteins in the kidney during iron overload facilitates systemic iron retention

Weiss, A., Spektor, L., Cohen, L. A., Lifshitz, L., Magid-Gold, I., Zhang, D., Truman-Rosentsvit, M., Leichtmann‐Bardoogo, Y., Nyska, A., Addadi, Y., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204471 · Cited by 26 · see citing works

ANEMIA OF CHRONIC KIDNEY DISEASE: NOVEL PHYSIOLOGICAL APPROACHES TO THERAPY BASED ON SIMULATION OF HYPOXIC RESPONSE

Айтбаев, К. А., Murkamilov, I. T., & Fomin, V. V. (2017) · Almanac of Clinical Medicine · doi:10.18786/2072-0505-2017-45-7-565-574 · Cited by 1 · 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

Novel Masters of Erythropoiesis: Hypoxia Inducible Factors and Recent Advances in Anemia of Renal Disease

Solak, Y., Cetiner, M., Siriopol, D. C., Tarım, K., Afşar, B., Covic, A. C., & Kanbay, M. (2016) · Blood Purification · doi:10.1159/000446273 · Cited by 17 · see citing works

[Current insights into the role of HIF-PHD axis in renal anemia].

Cao, J.-Y., & Liu, B. (2018) · PubMed · Cited by 1 · see citing works

Erythropoiesis and chronic kidney disease–related anemia: From physiology to new therapeutic advancements

Cernaro, V., Coppolino, G., Visconti, L., Rivoli, L., Lacquaniti, A., Santoro, D., Buemi, A., Loddo, S., & Buemi, M. (2018) · Medicinal Research Reviews · doi:10.1002/med.21527 · Cited by 48 · see citing works