메뉴 건너뛰기




Volumn 12, Issue 3, 2016, Pages 157-168

HIF prolyl hydroxylase inhibitors for the treatment of renal anaemia and beyond

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROPOIETIN; HYPOXIA INDUCIBLE FACTOR 2ALPHA; HYPOXIA INDUCIBLE FACTOR PROLYL HYDROXYLASE INHIBITOR; PHD2 PROTEIN; PROTEIN; UNCLASSIFIED DRUG; HYPOXIA INDUCIBLE FACTOR PROLINE DIOXYGENASE;

EID: 84958920828     PISSN: 17595061     EISSN: 1759507X     Source Type: Journal    
DOI: 10.1038/nrneph.2015.193     Document Type: Article
Times cited : (230)

References (146)
  • 1
    • 84897019542 scopus 로고    scopus 로고
    • Oxygen sensing, hypoxia-inducible factors, and disease pathophysiology
    • Semenza, G. L. Oxygen sensing, hypoxia-inducible factors, and disease pathophysiology. Annu. Rev. Pathol. 9, 47-71 (2014
    • (2014) Annu. Rev. Pathol , vol.9 , pp. 47-71
    • Semenza, G.L.1
  • 2
    • 84880534866 scopus 로고    scopus 로고
    • Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases
    • Chowdhury, R., et al. Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases. ACS Chem. Biol. 8, 1488-1496 (2013
    • (2013) ACS Chem. Biol , vol.8 , pp. 1488-1496
    • Chowdhury, R.1
  • 3
    • 84890449252 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor prolyl hydroxylase domain oxygen sensors: Tricking the body into mounting orchestrated survival and repair responses
    • Rabinowitz, M. H. Inhibition of hypoxia-inducible factor prolyl hydroxylase domain oxygen sensors: tricking the body into mounting orchestrated survival and repair responses. J. Med. Chem. 56, 9369-9402 (2013
    • (2013) J. Med. Chem , vol.56 , pp. 9369-9402
    • Rabinowitz, M.H.1
  • 4
    • 84877940214 scopus 로고    scopus 로고
    • How important is transfusion avoidance in 2013?
    • Macdougall, I. C., & Obrador, G. T. How important is transfusion avoidance in 2013? Nephrol. Dial. Transplant. 28, 1092-1099 (2013
    • (2013) Nephrol. Dial. Transplant , vol.28 , pp. 1092-1099
    • Macdougall, I.C.1    Obrador, G.T.2
  • 5
    • 0022980521 scopus 로고
    • Effect of human erythropoietin derived from recombinant DNA on the anaemia of patients maintained by chronic haemodialysis
    • Winearls, C. G., et al. Effect of human erythropoietin derived from recombinant DNA on the anaemia of patients maintained by chronic haemodialysis. Lancet 2, 1175-1178 (1986
    • (1986) Lancet , vol.2 , pp. 1175-1178
    • Winearls, C.G.1
  • 6
    • 84925223869 scopus 로고    scopus 로고
    • Erythropoiesis-stimulating agents for anaemia in adults with chronic kidney disease: A network meta-Analysis
    • Palmer, S. C., et al. Erythropoiesis-stimulating agents for anaemia in adults with chronic kidney disease: a network meta-Analysis. Cochrane Database Syst. Rev. 12, CD010590 (2014
    • (2014) Cochrane Database Syst. Rev , vol.12 , pp. CD010590
    • Palmer, S.C.1
  • 8
    • 84872808811 scopus 로고    scopus 로고
    • Peginesatide for anemia in patients with chronic kidney disease not receiving dialysis
    • Macdougall, I. C., et al. Peginesatide for anemia in patients with chronic kidney disease not receiving dialysis. N. Engl. J. Med. 368, 320-332 (2013
    • (2013) N. Engl. J. Med , vol.368 , pp. 320-332
    • Macdougall, I.C.1
  • 9
    • 84872782188 scopus 로고    scopus 로고
    • Peginesatide in patients with anemia undergoing hemodialysis
    • Fishbane, S., et al. Peginesatide in patients with anemia undergoing hemodialysis. N. Engl. J. Med. 368, 307-319 (2013
    • (2013) N. Engl. J. Med , vol.368 , pp. 307-319
    • Fishbane, S.1
  • 10
    • 70350774297 scopus 로고    scopus 로고
    • A peptide-based erythropoietin-receptor agonist for pure red-cell aplasia
    • Macdougall, I. C., et al. A peptide-based erythropoietin-receptor agonist for pure red-cell aplasia. N. Engl. J. Med. 361, 1848-1855 (2009
    • (2009) N. Engl. J. Med , vol.361 , pp. 1848-1855
    • Macdougall, I.C.1
  • 11
    • 84887450702 scopus 로고    scopus 로고
    • Lessons learned from peginesatide in the treatment of anemia associated with chronic kidney disease in patients on dialysis
    • Kaushik, T., & Yaqoob, M. M. Lessons learned from peginesatide in the treatment of anemia associated with chronic kidney disease in patients on dialysis. Biologics 7, 243-246 (2013
    • (2013) Biologics , vol.7 , pp. 243-246
    • Kaushik, T.1    Yaqoob, M.M.2
  • 12
    • 84875711713 scopus 로고    scopus 로고
    • Anaemia: The safety and efficacy of peginesatide in patients with CKD
    • Eckardt, K. U. Anaemia: the safety and efficacy of peginesatide in patients with CKD. Nat. Rev. Nephrol. 9, 192-193 (2013
    • (2013) Nat. Rev. Nephrol , vol.9 , pp. 192-193
    • Eckardt, K.U.1
  • 13
    • 84867178552 scopus 로고    scopus 로고
    • Mechanisms of anemia in CKD
    • Babitt, J. L., & Lin, H. Y. Mechanisms of anemia in CKD. J. Am. Soc. Nephrol. 23, 1631-1634 (2012
    • (2012) J. Am. Soc. Nephrol , vol.23 , pp. 1631-1634
    • Babitt, J.L.1    Lin, H.Y.2
  • 14
    • 0942287103 scopus 로고    scopus 로고
    • Anti-erythropoietin antibodies and pure red cell aplasia
    • Rossert, J., Casadevall, N., & Eckardt, K. U. Anti-erythropoietin antibodies and pure red cell aplasia. J. Am. Soc. Nephrol. 15, 398-406 (2004
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 398-406
    • Rossert, J.1    Casadevall, N.2    Eckardt, K.U.3
  • 15
    • 84924404728 scopus 로고    scopus 로고
    • Incidence of erythropoietin antibody-mediated pure red cell aplasia: The prospective immunogenicity surveillance registry (prims
    • Macdougall, I. C., et al. Incidence of erythropoietin antibody-mediated pure red cell aplasia: the Prospective Immunogenicity Surveillance Registry (PRIMS). Nephrol. Dial. Transplant. 30, 451-460 (2015
    • (2015) Nephrol. Dial. Transplant , vol.30 , pp. 451-460
    • Macdougall, I.C.1
  • 16
    • 70949108082 scopus 로고    scopus 로고
    • A trial of darbepoetin alfa in type 2 diabetes and chronic kidney disease
    • Pfeffer, M. A., et al. A trial of darbepoetin alfa in type 2 diabetes and chronic kidney disease. N. Engl. J. Med. 361, 2019-2032 (2009
    • (2009) N. Engl. J. Med , vol.361 , pp. 2019-2032
    • Pfeffer, M.A.1
  • 17
    • 33750983605 scopus 로고    scopus 로고
    • Correction of anemia with epoetin alfa in chronic kidney disease
    • Singh, A. K., et al. Correction of anemia with epoetin alfa in chronic kidney disease. N. Engl. J. Med. 355, 2085-2098 (2006
    • (2006) N. Engl. J. Med , vol.355 , pp. 2085-2098
    • Singh, A.K.1
  • 18
    • 49749092336 scopus 로고    scopus 로고
    • Anemia of chronic disease: A harmful disorder or an adaptive beneficial response?
    • Zarychanski, R., & Houston, D. S. Anemia of chronic disease: a harmful disorder or an adaptive, beneficial response? CMAJ 179, 333-337 (2008
    • (2008) CMAJ , vol.179 , pp. 333-337
    • Zarychanski, R.1    Houston, D.S.2
  • 19
    • 84857153506 scopus 로고    scopus 로고
    • The new FDA labeling for ESA-implications for patients and providers
    • Manns, B. J., & Tonelli, M. The new FDA labeling for ESA-implications for patients and providers. Clin. J. Am. Soc. Nephrol. 7, 348-353 (2012
    • (2012) Clin. J. Am. Soc. Nephrol , vol.7 , pp. 348-353
    • Manns, B.J.1    Tonelli, M.2
  • 20
    • 84884333035 scopus 로고    scopus 로고
    • KDIGO clinical practice guideline for anemia in chronic kidney disease
    • KDIGO clinical practice guideline for anemia in chronic kidney disease. Kidney Int. Suppl. 2, 279-335 (2012
    • (2012) Kidney Int. Suppl , vol.2 , pp. 279-335
  • 21
    • 17944375360 scopus 로고    scopus 로고
    • C elegans EGL 9 and mammalian homologues define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein, A. C., et al. C. elegans EGL 9 and mammalian homologues define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54 (2001
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1
  • 22
    • 84868104099 scopus 로고    scopus 로고
    • Transmembrane prolyl 4 hydroxylase is a fourth prolyl 4 hydroxylase regulating EPO production and erythropoiesis
    • Laitala, A., et al. Transmembrane prolyl 4 hydroxylase is a fourth prolyl 4 hydroxylase regulating EPO production and erythropoiesis. Blood 120, 3336-3344 (2012
    • (2012) Blood , vol.120 , pp. 3336-3344
    • Laitala, A.1
  • 24
    • 84895460591 scopus 로고    scopus 로고
    • The roles of Jumonji-Type oxygenases in human disease
    • Johansson, C., et al. The roles of Jumonji-Type oxygenases in human disease. Epigenomics 6, 89-120 (2014
    • (2014) Epigenomics , vol.6 , pp. 89-120
    • Johansson, C.1
  • 25
    • 84894247043 scopus 로고    scopus 로고
    • Optimal translational termination requires C4 lysyl hydroxylation of eRF1
    • Feng, T., et al. Optimal translational termination requires C4 lysyl hydroxylation of eRF1. Mol. Cell 53, 645-654 (2014
    • (2014) Mol Cell , vol.53 , pp. 645-654
    • Feng, T.1
  • 26
    • 84896511439 scopus 로고    scopus 로고
    • OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation
    • Singleton, R. S., et al. OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. Proc. Natl Acad. Sci. USA 111, 4031-4036 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 4031-4036
    • Singleton, R.S.1
  • 27
    • 84903517759 scopus 로고    scopus 로고
    • Human UTY(KDM6C) is a male-specific N? Methyl lysyl demethylase
    • Walport, L. J., et al. Human UTY(KDM6C) is a male-specific N? methyl lysyl demethylase. J. Biol. Chem. 289, 18302-18313 (2014
    • (2014) J. Biol. Chem , vol.289 , pp. 18302-18313
    • Walport, L.J.1
  • 28
    • 84901048393 scopus 로고    scopus 로고
    • Hairless is a histone H3K9 demethylase
    • Liu, L., et al. Hairless is a histone H3K9 demethylase. FASEB J. 28, 1534-1542 (2014
    • (2014) FASEB J. , vol.28 , pp. 1534-1542
    • Liu, L.1
  • 29
    • 84890061632 scopus 로고    scopus 로고
    • JMJD1C demethylates MDC1 to regulate the RNF8 and BRCA1 mediated chromatin response to DNA breaks
    • Watanabe, S., et al. JMJD1C demethylates MDC1 to regulate the RNF8 and BRCA1 mediated chromatin response to DNA breaks. Nat. Struct. Mol. Biol. 20, 1425-1433 (2013
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 1425-1433
    • Watanabe, S.1
  • 30
    • 0035903468 scopus 로고    scopus 로고
    • 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. Independent function of two destruction domains in hypoxia-inducible factor α chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206 (2001
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 31
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4 hydroxylases that modify the hypoxia-inducible factor
    • Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I., & Myllyharju, J. Characterization of the human prolyl 4 hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278, 30772-30780 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 32
    • 0037097861 scopus 로고    scopus 로고
    • FIH 1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D., et al. FIH 1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471 (2002
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1
  • 33
    • 79959450883 scopus 로고    scopus 로고
    • High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
    • Schodel, J., et al. High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood 117, e207-e217 (2011
    • (2011) Blood , vol.117 , pp. e207-e217
    • Schodel, J.1
  • 34
    • 84887501809 scopus 로고    scopus 로고
    • Regulation of IL 1β induced NF ?B by hydroxylases links key hypoxic and inflammatory signaling pathways
    • Scholz, C. C., et al. Regulation of IL 1β induced NF ?B by hydroxylases links key hypoxic and inflammatory signaling pathways. Proc. Natl Acad. Sci. USA 110, 18490-18495 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 18490-18495
    • Scholz, C.C.1
  • 35
    • 34548239264 scopus 로고    scopus 로고
    • Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor
    • Coleman, M. L., et al. Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor. J. Biol. Chem. 282, 24027-24038 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 24027-24038
    • Coleman, M.L.1
  • 36
    • 79953180051 scopus 로고    scopus 로고
    • Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor
    • Yang, M., et al. Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor. J. Biol. Chem. 286, 7648-7660 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 7648-7660
    • Yang, M.1
  • 37
    • 0027367661 scopus 로고
    • Identification of the renal erythropoietin-producing cells using transgenic mice
    • Maxwell, P. H., et al. Identification of the renal erythropoietin-producing cells using transgenic mice. Kidney Int. 44, 1149-1162 (1993
    • (1993) Kidney Int , vol.44 , pp. 1149-1162
    • Maxwell, P.H.1
  • 38
    • 0027410945 scopus 로고
    • Co localization of erythropoietin messenger RNA and ecto 5?-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin
    • Bachmann, S., Le Hir, M., & Eckardt, K. U. Co localization of erythropoietin messenger RNA and ecto 5?-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin. J. Histochem. Cytochem. 41, 335-341 (1993
    • (1993) J. Histochem. Cytochem , vol.41 , pp. 335-341
    • Bachmann, S.1    Le Hir, M.2    Eckardt, K.U.3
  • 39
    • 46749127450 scopus 로고    scopus 로고
    • Repression via the GATA box is essential for tissue-specific erythropoietin gene expression
    • Obara, N., et al. Repression via the GATA box is essential for tissue-specific erythropoietin gene expression. Blood 111, 5223-5232 (2008
    • (2008) Blood , vol.111 , pp. 5223-5232
    • Obara, N.1
  • 40
    • 18444380862 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor 1α and-2α in hypoxic and ischemic rat kidneys
    • Rosenberger, C., et al. Expression of hypoxia-inducible factor 1α and-2α in hypoxic and ischemic rat kidneys. J. Am. Soc. Nephrol. 13, 1721-1732 (2002
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1721-1732
    • Rosenberger, C.1
  • 41
    • 84856486011 scopus 로고    scopus 로고
    • Renal tubular HIF 2α expression requires VHL inactivation and causes fibrosis and cysts
    • Schietke, R. E., et al. Renal tubular HIF 2α expression requires VHL inactivation and causes fibrosis and cysts. PLoS ONE 7, e31034 (2012
    • (2012) PLoS ONE , vol.7 , pp. e31034
    • Schietke, R.E.1
  • 42
    • 17044378251 scopus 로고    scopus 로고
    • HIF 2α regulates murine hematopoietic development in an erythropoietin-dependent manner
    • Scortegagna, M., et al. HIF 2α regulates murine hematopoietic development in an erythropoietin-dependent manner. Blood 105, 3133-3140 (2005
    • (2005) Blood , vol.105 , pp. 3133-3140
    • Scortegagna, M.1
  • 43
    • 38049173572 scopus 로고    scopus 로고
    • A gain of function mutation in the HIF2A gene in familial erythrocytosis
    • Percy, M. J., et al. A gain of function mutation in the HIF2A gene in familial erythrocytosis. N. Engl. J. Med. 358, 162-168 (2008
    • (2008) N. Engl. J. Med , vol.358 , pp. 162-168
    • Percy, M.J.1
  • 44
    • 50949133897 scopus 로고    scopus 로고
    • Autosomal dominant erythrocytosis and pulmonary arterial hypertension associated with an activating HIF2α mutation
    • Gale, D. P., Harten, S. K., Reid, C. D., Tuddenham, E. G., & Maxwell, P. H. Autosomal dominant erythrocytosis and pulmonary arterial hypertension associated with an activating HIF2α mutation. Blood 112, 919-921 (2008
    • (2008) Blood , vol.112 , pp. 919-921
    • Gale, D.P.1    Harten, S.K.2    Reid, C.D.3    Tuddenham, E.G.4    Maxwell, P.H.5
  • 45
    • 77954926596 scopus 로고    scopus 로고
    • Natural selection on EPAS1 (HIF2α) associated with low hemoglobin concentration in Tibetan highlanders
    • Beall, C. M., et al. Natural selection on EPAS1 (HIF2α) associated with low hemoglobin concentration in Tibetan highlanders. Proc. Natl Acad. Sci. USA 107, 11459-11464 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11459-11464
    • Beall, C.M.1
  • 46
    • 77954319020 scopus 로고    scopus 로고
    • Sequencing of 50 human exomes reveals adaptation to high altitude
    • Yi, X., et al. Sequencing of 50 human exomes reveals adaptation to high altitude. Science 329, 75-78 (2010
    • (2010) Science , vol.329 , pp. 75-78
    • Yi, X.1
  • 47
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF 1α in normoxia
    • Berra, E., et al. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF 1α in normoxia. EMBO J. 22, 4082-4090 (2003
    • (2003) EMBO J. , vol.22 , pp. 4082-4090
    • Berra, E.1
  • 48
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1 PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R. J., et al. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279, 38458-38465 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1
  • 49
    • 31444436640 scopus 로고    scopus 로고
    • A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis
    • Percy, M. J., et al. A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis. Proc. Natl Acad. Sci. USA 103, 654-659 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 654-659
    • Percy, M.J.1
  • 50
    • 77955284188 scopus 로고    scopus 로고
    • The asparaginyl hydroxylase factor inhibiting HIF 1α is an essential regulator of metabolism
    • Zhang, N., et al. The asparaginyl hydroxylase factor inhibiting HIF 1α is an essential regulator of metabolism. Cell. Metab. 11, 364-378 (2010
    • (2010) Cell. Metab , vol.11 , pp. 364-378
    • Zhang, N.1
  • 51
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defect is associated with elevated HIFα levels in mice lacking prolyl hydroxylase domain protein 2
    • Takeda, K., et al. Placental but not heart defect is associated with elevated HIFα levels in mice lacking prolyl hydroxylase domain protein 2. Mol. Cell. Biol. 26, 8336-8346 (2006
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8336-8346
    • Takeda, K.1
  • 52
    • 0026724983 scopus 로고
    • Novel inhibitors of prolyl 4 hydroxylase 3 Inhibition by the substrate analogue N oxaloglycine and its derivatives
    • Cunliffe, C. J., Franklin, T. J., Hales, N. J., & Hill, G. B. Novel inhibitors of prolyl 4 hydroxylase. 3. Inhibition by the substrate analogue N oxaloglycine and its derivatives. J. Med. Chem. 35, 2652-2658 (1992
    • (1992) J. Med. Chem , vol.35 , pp. 2652-2658
    • Cunliffe, C.J.1    Franklin, T.J.2    Hales, N.J.3    Hill, G.B.4
  • 53
    • 0023021512 scopus 로고
    • Partial identity of the 2 oxoglutarate and ascorbate binding sites of prolyl 4 hydroxylase
    • Majamaa, K., Gunzler, V., Hanauske-Abel, H. M., Myllyla, R., & Kivirikko, K. I. Partial identity of the 2 oxoglutarate and ascorbate binding sites of prolyl 4 hydroxylase. J. Biol. Chem. 261, 7819-7823 (1986
    • (1986) J. Biol. Chem , vol.261 , pp. 7819-7823
    • Majamaa, K.1    Gunzler, V.2    Hanauske-Abel, H.M.3    Myllyla, R.4    Kivirikko, K.I.5
  • 54
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola, P., et al. Targeting of HIF α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292, 468-472 (2001
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 55
    • 0037108807 scopus 로고    scopus 로고
    • Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor
    • Ivan, M., et al. Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc. Natl Acad. Sci. USA 99, 13459-13464 (2002
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13459-13464
    • Ivan, M.1
  • 56
    • 34548829081 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibition results in endogenous erythropoietin induction, erythrocytosis, and modest fetal hemoglobin expression in rhesus macaques
    • Hsieh, M. M., et al. HIF prolyl hydroxylase inhibition results in endogenous erythropoietin induction, erythrocytosis, and modest fetal hemoglobin expression in rhesus macaques. Blood 110, 2140-2147 (2007
    • (2007) Blood , vol.110 , pp. 2140-2147
    • Hsieh, M.M.1
  • 57
    • 84911895497 scopus 로고    scopus 로고
    • Mimicking hypoxia to treat anemia: HIF-stabilizer BAY 85-3934 (molidustat) stimulates erythropoietin production without hypertensive effects
    • Flamme, I., et al. Mimicking hypoxia to treat anemia: HIF-stabilizer BAY 85-3934 (molidustat) stimulates erythropoietin production without hypertensive effects. PLoS ONE 9, e111838 (2014
    • (2014) PLoS ONE , vol.9 , pp. e111838
    • Flamme, I.1
  • 58
    • 0030763207 scopus 로고    scopus 로고
    • The interstitial response to renal injury: Fibroblast-like cells show phenotypic changes and have reduced potential for erythropoietin gene expression
    • Maxwell, P. H., Ferguson, D. J., Nicholls, L. G., Johnson, M. H., & Ratcliffe, P. J. The interstitial response to renal injury: fibroblast-like cells show phenotypic changes and have reduced potential for erythropoietin gene expression. Kidney Int. 52, 715-724 (1997
    • (1997) Kidney Int , vol.52 , pp. 715-724
    • Maxwell, P.H.1    Ferguson, D.J.2    Nicholls, L.G.3    Johnson, M.H.4    Ratcliffe, P.J.5
  • 59
    • 84885060233 scopus 로고    scopus 로고
    • Plasticity of renal erythropoietin-producing cells governs fibrosis
    • Souma, T., et al. Plasticity of renal erythropoietin-producing cells governs fibrosis. J. Am. Soc. Nephrol. 24, 1599-1616 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 1599-1616
    • Souma, T.1
  • 60
    • 80155151941 scopus 로고    scopus 로고
    • Indoxyl sulfate, a representative uremic toxin, suppresses erythropoietin production in a HIF-dependent manner
    • Chiang, C. K., Tanaka, T., Inagi, R., Fujita, T., & Nangaku, M. Indoxyl sulfate, a representative uremic toxin, suppresses erythropoietin production in a HIF-dependent manner. Lab. Invest. 91, 1564-1571 (2011
    • (2011) Lab. Invest , vol.91 , pp. 1564-1571
    • Chiang, C.K.1    Tanaka, T.2    Inagi, R.3    Fujita, T.4    Nangaku, M.5
  • 61
    • 84907417174 scopus 로고    scopus 로고
    • Oral adsorbent AST 120 potentiates the effect of erythropoietin-stimulating agents on stage 5 chronic kidney disease patients: A randomized crossover study
    • Wu, I. W., et al. Oral adsorbent AST 120 potentiates the effect of erythropoietin-stimulating agents on stage 5 chronic kidney disease patients: a randomized crossover study. Nephrol. Dial. Transplant. 29, 1719-1727 (2014
    • (2014) Nephrol. Dial. Transplant , vol.29 , pp. 1719-1727
    • Wu, I.W.1
  • 62
    • 0015594961 scopus 로고
    • Effect of altitude on erythropoiesis and oxygen affinity in anaemic patients on maintenance dialysis
    • Blumberg, A., Keller, H., & Marti, H. R. Effect of altitude on erythropoiesis and oxygen affinity in anaemic patients on maintenance dialysis. Eur. J. Clin. Invest. 3, 93-97 (1973
    • (1973) Eur. J. Clin. Invest , vol.3 , pp. 93-97
    • Blumberg, A.1    Keller, H.2    Marti, H.R.3
  • 63
    • 0024213759 scopus 로고
    • Relation of serum erythropoietin levels to renal excretory function: Evidence for lowered set point for erythropoietin production in chronic renal failure
    • Chandra, M., Clemons, G. K., & McVicar, M. I. Relation of serum erythropoietin levels to renal excretory function: evidence for lowered set point for erythropoietin production in chronic renal failure. J. Pediatr. 113, 1015-1021 (1988
    • (1988) J. Pediatr , vol.113 , pp. 1015-1021
    • Chandra, M.1    Clemons, G.K.2    McVicar, M.I.3
  • 64
    • 0023199353 scopus 로고
    • Erythropoietin-hematocrit feedback circuit in the anemia of end-stage renal disease
    • Walle, A. J., Wong, G. Y., Clemons, G. K., Garcia, J. F., & Niedermayer, W. Erythropoietin-hematocrit feedback circuit in the anemia of end-stage renal disease. Kidney Int. 31, 1205-1209 (1987
    • (1987) Kidney Int , vol.31 , pp. 1205-1209
    • Walle, A.J.1    Wong, G.Y.2    Clemons, G.K.3    Garcia, J.F.4    Niedermayer, W.5
  • 65
    • 48149088154 scopus 로고    scopus 로고
    • The effect of altitude on dosing and response to erythropoietin in ESRD
    • Brookhart, M. A., et al. The effect of altitude on dosing and response to erythropoietin in ESRD. J. Am. Soc. Nephrol. 19, 1389-1395 (2008
    • (2008) J. Am. Soc. Nephrol , vol.19 , pp. 1389-1395
    • Brookhart, M.A.1
  • 66
    • 0025000033 scopus 로고
    • Multiple site estimates of erythropoietin and renin in polycythemic kidney transplant patients
    • Aeberhard, J. M., Schneider, P. A., Vallotton, M. B., Kurtz, A., & Leski, M. Multiple site estimates of erythropoietin and renin in polycythemic kidney transplant patients. Transplantation 50, 613-616 (1990
    • (1990) Transplantation , vol.50 , pp. 613-616
    • Aeberhard, J.M.1    Schneider, P.A.2    Vallotton, M.B.3    Kurtz, A.4    Leski, M.5
  • 67
    • 84866305533 scopus 로고    scopus 로고
    • Anemia and erythrocytosis in patients after kidney transplantation
    • Malyszko, J., Oberbauer, R., & Watschinger, B. Anemia and erythrocytosis in patients after kidney transplantation. Transpl. Int. 25, 1013-1023 (2012
    • (2012) Transpl. Int , vol.25 , pp. 1013-1023
    • Malyszko, J.1    Oberbauer, R.2    Watschinger, B.3
  • 68
    • 0024446601 scopus 로고
    • Erythropoietin in polycystic kidneys
    • Eckardt, K. U., et al. Erythropoietin in polycystic kidneys. J. Clin. Invest. 84, 1160-1166 (1989
    • (1989) J. Clin. Invest , vol.84 , pp. 1160-1166
    • Eckardt, K.U.1
  • 70
    • 34247864018 scopus 로고    scopus 로고
    • Involvement of hypoxia-inducible transcription factors in polycystic kidney disease
    • Bernhardt, W. M., et al. Involvement of hypoxia-inducible transcription factors in polycystic kidney disease. Am. J. Pathol. 170, 830-842 (2007
    • (2007) Am. J. Pathol , vol.170 , pp. 830-842
    • Bernhardt, W.M.1
  • 71
    • 84896839333 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α causes renal cyst expansion through calcium-Activated chloride secretion
    • Buchholz, B., et al. Hypoxia-inducible factor 1α causes renal cyst expansion through calcium-Activated chloride secretion. J. Am. Soc. Nephrol. 25, 465-474 (2014
    • (2014) J. Am. Soc. Nephrol , vol.25 , pp. 465-474
    • Buchholz, B.1
  • 72
    • 0025912710 scopus 로고
    • Localization of cells producing erythropoietin in murine liver by in situ hybridization
    • Koury, S. T., Bondurant, M. C., Koury, M. J., & Semenza, G. L. Localization of cells producing erythropoietin in murine liver by in situ hybridization. Blood 77, 2497-2503 (1991
    • (1991) Blood , vol.77 , pp. 2497-2503
    • Koury, S.T.1    Bondurant, M.C.2    Koury, M.J.3    Semenza, G.L.4
  • 73
    • 0028086474 scopus 로고
    • Expression of a homologously recombined erythropoietin SV40 T antigen fusion gene in mouse liver: Evidence for erythropoietin production by Ito cells
    • Maxwell, P. H., et al. Expression of a homologously recombined erythropoietin SV40 T antigen fusion gene in mouse liver: evidence for erythropoietin production by Ito cells. Blood 84, 1823-1830 (1994
    • (1994) Blood , vol.84 , pp. 1823-1830
    • Maxwell, P.H.1
  • 74
    • 0026575755 scopus 로고
    • Age-dependent expression of the erythropoietin gene in rat liver and kidneys
    • Eckardt, K. U., Ratcliffe, P. J., Tan, C. C., Bauer, C., & Kurtz, A. Age-dependent expression of the erythropoietin gene in rat liver and kidneys. J. Clin. Invest. 89, 753-760 (1992
    • (1992) J. Clin. Invest , vol.89 , pp. 753-760
    • Eckardt, K.U.1    Ratcliffe, P.J.2    Tan, C.C.3    Bauer, C.4    Kurtz, A.5
  • 75
    • 0015221608 scopus 로고
    • Influence of serum hepatitis on haemoglobin level in patients on regular haemodialysis
    • Kolk-Vegter, A. J., Bosch, E., & van Leeuwen, A. M. Influence of serum hepatitis on haemoglobin level in patients on regular haemodialysis. Lancet 1, 526-528 (1971
    • (1971) Lancet , vol.1 , pp. 526-528
    • Kolk-Vegter, A.J.1    Bosch, E.2    Van Leeuwen, A.M.3
  • 76
    • 0017364489 scopus 로고
    • Hepatic regeneration and erythropoietin production in the rat
    • Naughton, B. A., et al. Hepatic regeneration and erythropoietin production in the rat. Science 196, 301-302 (1977
    • (1977) Science , vol.196 , pp. 301-302
    • Naughton, B.A.1
  • 77
    • 80052568370 scopus 로고    scopus 로고
    • Specific contribution of the erythropoietin gene 3? Enhancer to hepatic erythropoiesis after late embryonic stages
    • Suzuki, N., et al. Specific contribution of the erythropoietin gene 3? enhancer to hepatic erythropoiesis after late embryonic stages. Mol. Cell. Biol. 31, 3896-3905 (2011
    • (2011) Mol. Cell. Biol , vol.31 , pp. 3896-3905
    • Suzuki, N.1
  • 78
    • 84936082587 scopus 로고    scopus 로고
    • Hypoxia signaling cascade for erythropoietin production in hepatocytes
    • Tojo, Y., et al. Hypoxia signaling cascade for erythropoietin production in hepatocytes. Mol. Cell. Biol. 35, 2658-2672 (2015
    • (2015) Mol. Cell. Biol , vol.35 , pp. 2658-2672
    • Tojo, Y.1
  • 79
    • 77954837178 scopus 로고    scopus 로고
    • Reactivation of hepatic EPO synthesis in mice after PHD loss
    • Minamishima, Y. A., & Kaelin, W. G. Jr. Reactivation of hepatic EPO synthesis in mice after PHD loss. Science 329, 407 (2010
    • (2010) Science , vol.329 , pp. 407
    • Minamishima, Y.A.1    Kaelin, W.G.2
  • 80
    • 70449412497 scopus 로고    scopus 로고
    • The glial cell response is an essential component of hypoxia-induced erythropoiesis in mice
    • Weidemann, A., et al. The glial cell response is an essential component of hypoxia-induced erythropoiesis in mice. J. Clin. Invest. 119, 3373-3383 (2009
    • (2009) J. Clin. Invest , vol.119 , pp. 3373-3383
    • Weidemann, A.1
  • 81
    • 84859207905 scopus 로고    scopus 로고
    • The HIF signaling pathway in osteoblasts directly modulates erythropoiesis through the production of EPO
    • Rankin, E. B., et al. The HIF signaling pathway in osteoblasts directly modulates erythropoiesis through the production of EPO. Cell 149, 63-74 (2012
    • (2012) Cell , vol.149 , pp. 63-74
    • Rankin, E.B.1
  • 82
    • 0026526168 scopus 로고
    • Erythropoietin: Structure, control of production, and function
    • Jelkmann, W. Erythropoietin: structure, control of production, and function. Physiol. Rev. 72, 449-489 (1992
    • (1992) Physiol. Rev , vol.72 , pp. 449-489
    • Jelkmann, W.1
  • 83
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer, S., Kristensen, M. M., Jensen, K. S., Johansen, J. V., & Staller, P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 283, 36542-36552 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 84
    • 84934756768 scopus 로고    scopus 로고
    • MicroRNA 687 induced by hypoxia-inducible factor 1 targets phosphatase and tensin homolog in renal ischemia-reperfusion injury
    • Bhatt, K., et al. MicroRNA 687 induced by hypoxia-inducible factor 1 targets phosphatase and tensin homolog in renal ischemia-reperfusion injury. J. Am. Soc. Nephrol. 26, 1588-1596 (2015
    • (2015) J. Am. Soc. Nephrol , vol.26 , pp. 1588-1596
    • Bhatt, K.1
  • 85
    • 84862792124 scopus 로고    scopus 로고
    • Targeting the hepcidin-ferroportin axis to develop new treatment strategies for anemia of chronic disease and anemia of inflammation
    • Sun, C. C., Vaja, V., Babitt, J. L., & Lin, H. Y. Targeting the hepcidin-ferroportin axis to develop new treatment strategies for anemia of chronic disease and anemia of inflammation. Am. J. Hematol. 87, 392-400 (2012
    • (2012) Am. J. Hematol , vol.87 , pp. 392-400
    • Sun, C.C.1    Vaja, V.2    Babitt, J.L.3    Lin, H.Y.4
  • 86
    • 84928476752 scopus 로고    scopus 로고
    • New insights into iron regulation and erythropoiesis
    • Kim, A., & Nemeth, E. New insights into iron regulation and erythropoiesis. Curr. Opin. Hematol. 22, 199-205 (2015
    • (2015) Curr. Opin. Hematol , vol.22 , pp. 199-205
    • Kim, A.1    Nemeth, E.2
  • 87
    • 84894387582 scopus 로고    scopus 로고
    • Hypoxia-inducible factors link iron homeostasis and erythropoiesis
    • Shah, Y. M., & Xie, L. Hypoxia-inducible factors link iron homeostasis and erythropoiesis. Gastroenterology 146, 630-642 (2014
    • (2014) Gastroenterology , vol.146 , pp. 630-642
    • Shah, Y.M.1    Xie, L.2
  • 88
    • 34447120059 scopus 로고    scopus 로고
    • Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs
    • Peyssonnaux, C., et al. Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs). J. Clin. Invest. 117, 1926-1932 (2007
    • (2007) J. Clin. Invest , vol.117 , pp. 1926-1932
    • Peyssonnaux, C.1
  • 89
    • 84870566647 scopus 로고    scopus 로고
    • Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis
    • Liu, Q., Davidoff, O., Niss, K., & Haase, V. H. Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis. J. Clin. Invest. 122, 4635-4644 (2012
    • (2012) J. Clin. Invest , vol.122 , pp. 4635-4644
    • Liu, Q.1    Davidoff, O.2    Niss, K.3    Haase, V.H.4
  • 90
    • 70849095971 scopus 로고    scopus 로고
    • Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors
    • Volke, M., et al. Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors. PLoS ONE 4, e7875 (2009
    • (2009) PLoS ONE , vol.4 , pp. e7875
    • Volke, M.1
  • 91
    • 84896029483 scopus 로고    scopus 로고
    • Induction of erythropoiesis in anemic patients by prolylhydroxylase inhibitor in a repeat dose, randomized placebo controlled trial [poster SA PO117
    • Abstract suppl
    • Brigandi, R. A., et al. Induction of erythropoiesis in anemic patients by prolylhydroxylase inhibitor in a repeat dose, randomized placebo controlled trial [poster SA PO117]. J. Am. Soc. Nephrol. 23 (Abstract suppl.), 663A (2012
    • (2012) J Am. Soc. Nephrol , vol.23 , pp. 663A
    • Brigandi, R.A.1
  • 92
    • 84933181213 scopus 로고    scopus 로고
    • AKB 6548, a new hypoxia-inducible factor prolyl hydroxylase inhibitor, increases hemoglobin in chronic kidney disease patients without increasing basal erythropoietin levels [abstract FR OR116
    • Abstract suppl
    • Shalwitz, R., et al. AKB 6548, a new hypoxia-inducible factor prolyl hydroxylase inhibitor, increases hemoglobin in chronic kidney disease patients without increasing basal erythropoietin levels [abstract FR OR116]. J. Am. Soc. Nephrol. 23 (Abstract suppl.), 56A (2012
    • (2012) J Am. Soc. Nephrol , vol.23 , pp. 56A
    • Shalwitz, R.1
  • 93
    • 84933178484 scopus 로고    scopus 로고
    • Impact of iron regimen on iron indices and hepcidin during roxadustat anemia correction in incident dialysis patients [poster TH PO847
    • Abstract suppl
    • Besarab, A., Szczech, L., Yu, K. H. P., & Neff, T. B. Impact of iron regimen on iron indices and hepcidin during roxadustat anemia correction in incident dialysis patients [poster TH PO847]. J. Am. Soc. Nephrol. 25 (Abstract suppl.), 304A (2014
    • (2014) J Am. Soc. Nephrol , vol.25 , pp. 304A
    • Besarab, A.1    Szczech, L.2    Yu, K.H.P.3    Neff, T.B.4
  • 94
    • 77949707023 scopus 로고    scopus 로고
    • Erythropoietin administration in humans causes a marked and prolonged reduction in circulating hepcidin
    • Ashby, D. R., et al. Erythropoietin administration in humans causes a marked and prolonged reduction in circulating hepcidin. Haematologica 95, 505-508 (2010
    • (2010) Haematologica , vol.95 , pp. 505-508
    • Ashby, D.R.1
  • 95
    • 64949191416 scopus 로고    scopus 로고
    • Plasma hepcidin levels are elevated but responsive to erythropoietin therapy in renal disease
    • Ashby, D. R., et al. Plasma hepcidin levels are elevated but responsive to erythropoietin therapy in renal disease. Kidney Int. 75, 976-981 (2009
    • (2009) Kidney Int , vol.75 , pp. 976-981
    • Ashby, D.R.1
  • 96
    • 84923176656 scopus 로고    scopus 로고
    • Erythropoietins inhibiting impact on hepcidin expression occurs indirectly
    • Gammella, E., et al. Erythropoietins inhibiting impact on hepcidin expression occurs indirectly. Am. J. Physiol. Regul. Integr. Comp. Physiol. 308, R330-R335 (2015
    • (2015) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.308 , pp. R330-R335
    • Gammella, E.1
  • 97
    • 84914098806 scopus 로고    scopus 로고
    • Short-Term treatment with a novel HIF-prolyl hydroxylase inhibitor (GSK1278863) failed to improve measures of performance in subjects with claudication-limited peripheral artery disease
    • Olson, E., et al. Short-Term treatment with a novel HIF-prolyl hydroxylase inhibitor (GSK1278863) failed to improve measures of performance in subjects with claudication-limited peripheral artery disease. Vasc. Med. 19, 473-482 (2014
    • (2014) Vasc. Med , vol.19 , pp. 473-482
    • Olson, E.1
  • 98
    • 38149075003 scopus 로고    scopus 로고
    • Inhibition of hypoxia inducible factor hydroxylases protects against renal ischemia-reperfusion injury
    • Hill, P., et al. Inhibition of hypoxia inducible factor hydroxylases protects against renal ischemia-reperfusion injury. J. Am. Soc. Nephrol. 19, 39-46 (2008
    • (2008) J. Am. Soc. Nephrol , vol.19 , pp. 39-46
    • Hill, P.1
  • 99
    • 84925546346 scopus 로고    scopus 로고
    • VHL the story of a tumour suppressor gene
    • Gossage, L., Eisen, T., & Maher, E. R. VHL, the story of a tumour suppressor gene. Nat. Rev. Cancer 15, 55-64 (2015
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 55-64
    • Gossage, L.1    Eisen, T.2    Maher, E.R.3
  • 100
    • 0027954044 scopus 로고
    • Mutations of the VHL tumour suppressor gene in renal carcinoma
    • Gnarra, J. R., et al. Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat. Genet. 7, 85-90 (1994
    • (1994) Nat. Genet , vol.7 , pp. 85-90
    • Gnarra, J.R.1
  • 101
    • 20744445650 scopus 로고    scopus 로고
    • Contrasting properties of hypoxia-inducible factor 1 (HIF 1) and HIF 2 in von Hippel-Lindau-Associated renal cell carcinoma
    • Raval, R. R., et al. Contrasting properties of hypoxia-inducible factor 1 (HIF 1) and HIF 2 in von Hippel-Lindau-Associated renal cell carcinoma. Mol. Cell. Biol. 25, 5675-5686 (2005
    • (2005) Mol. Cell. Biol , vol.25 , pp. 5675-5686
    • Raval, R.R.1
  • 102
    • 17044452288 scopus 로고    scopus 로고
    • HIF activation identifies early lesions in VHL kidneys: Evidence for site-specific tumor suppressor function in the nephron
    • Mandriota, S. J., et al. HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron. Cancer Cell 1, 459-468 (2002
    • (2002) Cancer Cell , vol.1 , pp. 459-468
    • Mandriota, S.J.1
  • 103
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth
    • Kondo, K., Kim, W., Lechpammer, M., & Kaelin, W. Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth. PLoS Biol. 1, 439-444 (2003
    • (2003) PLoS Biol , vol.1 , pp. 439-444
    • Kondo, K.1    Kim, W.2    Lechpammer, M.3    Kaelin, W.4
  • 104
    • 84863393080 scopus 로고    scopus 로고
    • Intratumor heterogeneity and branched evolution revealed by multiregion sequencing
    • Gerlinger, M., et al. Intratumor heterogeneity and branched evolution revealed by multiregion sequencing. N. Engl. J. Med. 366, 883-892 (2012
    • (2012) N. Engl. J. Med , vol.366 , pp. 883-892
    • Gerlinger, M.1
  • 105
    • 47049090632 scopus 로고    scopus 로고
    • PVHL and PTEN tumour suppressor proteins cooperatively suppress kidney cyst formation
    • Frew, I. J., et al. pVHL and PTEN tumour suppressor proteins cooperatively suppress kidney cyst formation. EMBO J. 27, 1747-1757 (2008
    • (2008) EMBO J. , vol.27 , pp. 1747-1757
    • Frew, I.J.1
  • 106
    • 0035339044 scopus 로고    scopus 로고
    • Contrasting effects on HIF 1α regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease
    • Clifford, S. C., et al. Contrasting effects on HIF 1α regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Hum. Mol. Genet. 10, 1029-1038 (2001
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1029-1038
    • Clifford, S.C.1
  • 107
    • 84903774921 scopus 로고    scopus 로고
    • HIF signaling pathway in pheochromocytoma and other neuroendocrine tumors
    • Jochmanova, I., Zelinka, T., Widimsky, J. Jr & Pacak, K. HIF signaling pathway in pheochromocytoma and other neuroendocrine tumors. Physiol. Res. 63, S251-S262 (2014
    • (2014) Physiol. Res , vol.63 , pp. S251-S262
    • Jochmanova, I.1    Zelinka, T.2    Widimsky, J.3    Pacak, K.4
  • 108
    • 84926681391 scopus 로고    scopus 로고
    • Germ-line PHD1 and PHD2 mutations detected in patients with pheochromocytoma/paraganglioma-polycythemia
    • Yang, C., et al. Germ-line PHD1 and PHD2 mutations detected in patients with pheochromocytoma/paraganglioma-polycythemia. J. Mol. Med. (Berl.) 93, 93-104 (2015
    • (2015) J. Mol. Med. (Berl , vol.93 , pp. 93-104
    • Yang, C.1
  • 109
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • Pugh, C. W., & Ratcliffe, P. J. Regulation of angiogenesis by hypoxia: role of the HIF system. Nat. Med. 9, 677-684 (2003
    • (2003) Nat. Med , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 110
    • 84867420094 scopus 로고    scopus 로고
    • Cancer and altered metabolism: Potential importance of hypoxia-inducible factor and 2 oxoglutarate-dependent dioxygenases
    • Kaelin, W. G. Jr. Cancer and altered metabolism: potential importance of hypoxia-inducible factor and 2 oxoglutarate-dependent dioxygenases. Cold Spring Harb. Symp. Quant. Biol. 76, 335-345 (2011
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 335-345
    • Kaelin, W.G.1
  • 111
    • 84878544545 scopus 로고    scopus 로고
    • The hypoxia factor Hif 1α controls neural crest chemotaxis and epithelial to mesenchymal transition
    • Barriga, E. H., Maxwell, P. H., Reyes, A. E., & Mayor, R. The hypoxia factor Hif 1α controls neural crest chemotaxis and epithelial to mesenchymal transition. J. Cell Biol. 201, 759-776 (2013
    • (2013) J. Cell Biol , vol.201 , pp. 759-776
    • Barriga, E.H.1    Maxwell, P.H.2    Reyes, A.E.3    Mayor, R.4
  • 112
    • 33645748171 scopus 로고    scopus 로고
    • Regulation of e cadherin expression by VHL and hypoxia-inducible factor
    • Esteban, M. A., et al. Regulation of E cadherin expression by VHL and hypoxia-inducible factor. Cancer Res. 66, 3567-3575 (2006
    • (2006) Cancer Res , vol.66 , pp. 3567-3575
    • Esteban, M.A.1
  • 113
    • 36849021771 scopus 로고    scopus 로고
    • Hypoxia promotes fibrogenesis in vivo via HIF 1 stimulation of epithelial-To mesenchymal transition
    • Higgins, D. F., et al. Hypoxia promotes fibrogenesis in vivo via HIF 1 stimulation of epithelial-To mesenchymal transition. J. Clin. Invest. 117, 3810-3820 (2007
    • (2007) J. Clin. Invest , vol.117 , pp. 3810-3820
    • Higgins, D.F.1
  • 114
    • 84865575592 scopus 로고    scopus 로고
    • Molecular mechanisms mediating metastasis of hypoxic breast cancer cells
    • Semenza, G. L. Molecular mechanisms mediating metastasis of hypoxic breast cancer cells. Trends Mol. Med. 18, 534-543 (2012
    • (2012) Trends Mol. Med , vol.18 , pp. 534-543
    • Semenza, G.L.1
  • 115
    • 18744373593 scopus 로고    scopus 로고
    • Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia
    • Ang, S. O., et al. Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia. Nat. Genet. 32, 614-621 (2002
    • (2002) Nat. Genet , vol.32 , pp. 614-621
    • Ang, S.O.1
  • 116
    • 45949112024 scopus 로고    scopus 로고
    • Novel exon 12 mutations in the HIF2A gene associated with erythrocytosis
    • Percy, M. J., et al. Novel exon 12 mutations in the HIF2A gene associated with erythrocytosis. Blood 111, 5400-5402 (2008
    • (2008) Blood , vol.111 , pp. 5400-5402
    • Percy, M.J.1
  • 117
    • 79953695043 scopus 로고    scopus 로고
    • Dysregulation of the HIF pathway due to VHL mutation causing severe erythrocytosis and pulmonary arterial hypertension
    • Bond, J., et al. Dysregulation of the HIF pathway due to VHL mutation causing severe erythrocytosis and pulmonary arterial hypertension. Blood 117, 3699-3701 (2011
    • (2011) Blood , vol.117 , pp. 3699-3701
    • Bond, J.1
  • 118
    • 33746398489 scopus 로고    scopus 로고
    • Mutation of von Hippel-Lindau tumour suppressor and human cardiopulmonary physiology
    • Smith, T. G., et al. Mutation of von Hippel-Lindau tumour suppressor and human cardiopulmonary physiology. PLoS Med. 3, e290 (2006
    • (2006) PLoS Med , vol.3 , pp. e290
    • Smith, T.G.1
  • 119
    • 77949725833 scopus 로고    scopus 로고
    • The von hippel-lindau chuvash mutation promotes pulmonary hypertension and fibrosis in mice
    • Hickey, M. M., et al. The von Hippel-Lindau Chuvash mutation promotes pulmonary hypertension and fibrosis in mice. J. Clin. Invest. 120, 827-839 (2010
    • (2010) J. Clin. Invest , vol.120 , pp. 827-839
    • Hickey, M.M.1
  • 120
    • 2342631195 scopus 로고    scopus 로고
    • Congenital disorder of oxygen sensing: Association of the homozygous Chuvash polycythemia VHL mutation with thrombosis and vascular abnormalities but not tumors
    • Gordeuk, V. R., et al. Congenital disorder of oxygen sensing: association of the homozygous Chuvash polycythemia VHL mutation with thrombosis and vascular abnormalities but not tumors. Blood 103, 3924-3932 (2004
    • (2004) Blood , vol.103 , pp. 3924-3932
    • Gordeuk, V.R.1
  • 121
    • 84901457818 scopus 로고    scopus 로고
    • Smooth muscle cell-specific Hif 1α deficiency suppresses angiotensin II induced vascular remodelling in mice
    • Imanishi, M., et al. Smooth muscle cell-specific Hif 1α deficiency suppresses angiotensin II induced vascular remodelling in mice. Cardiovasc. Res. 102, 460-468 (2014
    • (2014) Cardiovasc. Res , vol.102 , pp. 460-468
    • Imanishi, M.1
  • 122
    • 80255131449 scopus 로고    scopus 로고
    • Hypoxia is present in murine atherosclerotic plaques and has multiple adverse effects on macrophage lipid metabolism
    • Parathath, S., et al. Hypoxia is present in murine atherosclerotic plaques and has multiple adverse effects on macrophage lipid metabolism. Circ. Res. 109, 1141-1152 (2011
    • (2011) Circ. Res , vol.109 , pp. 1141-1152
    • Parathath, S.1
  • 123
    • 25144475141 scopus 로고    scopus 로고
    • Cobalt promotes angiogenesis via hypoxia-inducible factor and protects tubulointerstitium in the remnant kidney model
    • Tanaka, T., et al. Cobalt promotes angiogenesis via hypoxia-inducible factor and protects tubulointerstitium in the remnant kidney model. Lab. Invest. 85, 1292-1307 (2005
    • (2005) Lab. Invest , vol.85 , pp. 1292-1307
    • Tanaka, T.1
  • 124
    • 32844456187 scopus 로고    scopus 로고
    • Induction of protective genes by cobalt ameliorates tubulointerstitial injury in the progressive Thy1 nephritis
    • Tanaka, T., et al. Induction of protective genes by cobalt ameliorates tubulointerstitial injury in the progressive Thy1 nephritis. Kidney Int. 68, 2714-2725 (2005
    • (2005) Kidney Int , vol.68 , pp. 2714-2725
    • Tanaka, T.1
  • 125
    • 72949106456 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor attenuates renal injury in rat remnant kidney
    • Song, Y. R., et al. Activation of hypoxia-inducible factor attenuates renal injury in rat remnant kidney. Nephrol. Dial. Transplant. 25, 77-85 (2010
    • (2010) Nephrol. Dial. Transplant , vol.25 , pp. 77-85
    • Song, Y.R.1
  • 126
    • 84861128230 scopus 로고    scopus 로고
    • Myeloid cell-derived hypoxia-inducible factor attenuates inflammation in unilateral ureteral obstruction-induced kidney injury
    • Kobayashi, H., et al. Myeloid cell-derived hypoxia-inducible factor attenuates inflammation in unilateral ureteral obstruction-induced kidney injury. J. Immunol. 188, 5106-5115 (2012
    • (2012) J. Immunol , vol.188 , pp. 5106-5115
    • Kobayashi, H.1
  • 127
    • 84923880080 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factors prevents diabetic nephropathy
    • Nordquist, L., et al. Activation of hypoxia-inducible factors prevents diabetic nephropathy. J. Am. Soc. Nephrol. 26, 328-338 (2015
    • (2015) J. Am. Soc. Nephrol , vol.26 , pp. 328-338
    • Nordquist, L.1
  • 128
    • 78649876180 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylases increases erythropoietin production in ESRD
    • Bernhardt, W. M., et al. Inhibition of prolyl hydroxylases increases erythropoietin production in ESRD. J. Am. Soc. Nephrol. 21, 2151-2156 (2010
    • (2010) J. Am. Soc. Nephrol , vol.21 , pp. 2151-2156
    • Bernhardt, W.M.1
  • 129
    • 84943401141 scopus 로고    scopus 로고
    • Randomized placebo-controlled dose-ranging and pharmacodynamics study of roxadustat (FG 4592) to treat anemia in nondialysis-dependent chronic kidney disease (NDD CKD) patients
    • Besarab, A., et al. Randomized placebo-controlled dose-ranging and pharmacodynamics study of roxadustat (FG 4592) to treat anemia in nondialysis-dependent chronic kidney disease (NDD CKD) patients. Nephrol. Dial. Transplant. 30, 1665-1673 (2015
    • (2015) Nephrol. Dial. Transplant , vol.30 , pp. 1665-1673
    • Besarab, A.1
  • 130
    • 85016925358 scopus 로고    scopus 로고
    • Roxadustat (FG 4592): Correction of anemia in incident dialysis patients
    • Besarab, A., et al. Roxadustat (FG 4592): correction of anemia in incident dialysis patients. J. Am. Soc. Nephrol. http://dx.doi.org/10.1681/ASN.2015030241 (2015
    • (2015) J. Am. Soc. Nephrol
    • Besarab, A.1
  • 131
    • 84904359493 scopus 로고    scopus 로고
    • First in Man study with BAY 85-3934-A new oral selective HIF PH inhibitor for the treatment of renal anemia [poster TH PO1090
    • Abstract suppl
    • Boettcher, M. F., Lentini, S., Flamme, I., Kubitza, D., & Wensing, G. First in Man study with BAY 85-3934-A new oral selective HIF PH inhibitor for the treatment of renal anemia [poster TH PO1090]. J. Am. Soc. Nephrol. 24 (Abstract suppl.), 347A (2013
    • (2013) J Am. Soc. Nephrol , vol.24 , pp. 347A
    • Boettcher, M.F.1    Lentini, S.2    Flamme, I.3    Kubitza, D.4    Wensing, G.5
  • 132
    • 85016924015 scopus 로고    scopus 로고
    • Four-week studies of oral hypoxia-inducible factor-prolyl hydroxylase inhibitor GSK1278863 for treatment of anemia
    • Holdstock, L., et al. Four-week studies of oral hypoxia-inducible factor-prolyl hydroxylase inhibitor GSK1278863 for treatment of anemia. J. Am. Soc. Nephrol. http://dx.doi.org/10.1681/ASN.2014111139 (2015
    • (2015) J. Am. Soc. Nephrol
    • Holdstock, L.1
  • 133
    • 84919685459 scopus 로고    scopus 로고
    • The challenge of translating ischemic conditioning from animal models to humans: The role of comorbidities
    • McCafferty, K., Forbes, S., Thiemermann, C., & Yaqoob, M. M. The challenge of translating ischemic conditioning from animal models to humans: the role of comorbidities. Dis. Model Mech. 7, 1321-1333 (2014
    • (2014) Dis. Model Mech , vol.7 , pp. 1321-1333
    • McCafferty, K.1    Forbes, S.2    Thiemermann, C.3    Yaqoob, M.M.4
  • 134
    • 84902665539 scopus 로고    scopus 로고
    • Hypoxic preconditioning protection is eliminated in HIF 1α knockout mice subjected to neonatal hypoxia-ischemia
    • Sheldon, R. A., Lee, C. L., Jiang, X., Knox, R. N., & Ferriero, D. M. Hypoxic preconditioning protection is eliminated in HIF 1α knockout mice subjected to neonatal hypoxia-ischemia. Pediatr. Res. 76, 46-53 (2014
    • (2014) Pediatr. Res , vol.76 , pp. 46-53
    • Sheldon, R.A.1    Lee, C.L.2    Jiang, X.3    Knox, R.N.4    Ferriero, D.M.5
  • 135
    • 84862991047 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 transcriptional activity in endothelial cells is required for acute phase cardioprotection induced by ischemic preconditioning
    • Sarkar, K., et al. Hypoxia-inducible factor 1 transcriptional activity in endothelial cells is required for acute phase cardioprotection induced by ischemic preconditioning. Proc. Natl Acad. Sci. USA 109, 10504-10509 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 10504-10509
    • Sarkar, K.1
  • 136
    • 84919393948 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibition prior to transient focal cerebral ischaemia is neuroprotective in mice
    • Chen, R. L., et al. HIF prolyl hydroxylase inhibition prior to transient focal cerebral ischaemia is neuroprotective in mice. J. Neurochem. 131, 177-189 (2014
    • (2014) J. Neurochem , vol.131 , pp. 177-189
    • Chen, R.L.1
  • 137
    • 84941357822 scopus 로고    scopus 로고
    • Pre-And post-conditional inhibition of prolyl-4 hydroxylase domain enzymes protects the heart from an ischemic insult
    • Vogler, M., et al. Pre-And post-conditional inhibition of prolyl-4 hydroxylase domain enzymes protects the heart from an ischemic insult. Pflugers Arch. 467, 2141-2149 (2015
    • (2015) Pflugers Arch , vol.467 , pp. 2141-2149
    • Vogler, M.1
  • 138
    • 84913555668 scopus 로고    scopus 로고
    • HIF 1 reduces ischaemia-reperfusion injury in the heart by targeting the mitochondrial permeability transition pore
    • Ong, S. G., et al. HIF 1 reduces ischaemia-reperfusion injury in the heart by targeting the mitochondrial permeability transition pore. Cardiovasc. Res. 104, 24-36 (2014
    • (2014) Cardiovasc. Res , vol.104 , pp. 24-36
    • Ong, S.G.1
  • 139
    • 84892842174 scopus 로고    scopus 로고
    • Short hairpin RNA gene silencing of prolyl hydroxylase 2 with a minicircle vector improves neovascularization of hindlimb ischemia
    • Lijkwan, M. A., et al. Short hairpin RNA gene silencing of prolyl hydroxylase 2 with a minicircle vector improves neovascularization of hindlimb ischemia. Hum. Gene Ther. 25, 41-49 (2014
    • (2014) Hum. Gene Ther , vol.25 , pp. 41-49
    • Lijkwan, M.A.1
  • 140
    • 38649143118 scopus 로고    scopus 로고
    • Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism
    • Aragones, J., et al. Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism. Nat. Genet. 40, 170-180 (2008
    • (2008) Nat. Genet , vol.40 , pp. 170-180
    • Aragones, J.1
  • 141
    • 0037530588 scopus 로고    scopus 로고
    • Induction of renoprotective gene expression by cobalt ameliorates ischemic injury of the kidney in rats
    • Matsumoto, M., et al. Induction of renoprotective gene expression by cobalt ameliorates ischemic injury of the kidney in rats. J. Am. Soc. Nephrol. 14, 1825-1832 (2003
    • (2003) J. Am. Soc. Nephrol , vol.14 , pp. 1825-1832
    • Matsumoto, M.1
  • 142
    • 33745820018 scopus 로고    scopus 로고
    • Preconditional activation of hypoxia-inducible factors ameliorates ischemic acute renal failure
    • Bernhardt, W. M., et al. Preconditional activation of hypoxia-inducible factors ameliorates ischemic acute renal failure. J. Am. Soc. Nephrol. 17, 1970-1978 (2006
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 1970-1978
    • Bernhardt, W.M.1
  • 143
    • 84860505643 scopus 로고    scopus 로고
    • The protective effect of prolyl-hydroxylase inhibition against renal ischaemia requires application prior to ischaemia but is superior to EPO treatment
    • Wang, Z., et al. The protective effect of prolyl-hydroxylase inhibition against renal ischaemia requires application prior to ischaemia but is superior to EPO treatment. Nephrol. Dial. Transplant. 27, 929-936 (2012
    • (2012) Nephrol. Dial. Transplant , vol.27 , pp. 929-936
    • Wang, Z.1
  • 144
    • 75849163295 scopus 로고    scopus 로고
    • Donor treatment with a PHD-inhibitor activating HIFs prevents graft injury and prolongs survival in an allogenic kidney transplant model
    • Bernhardt, W. M., et al. Donor treatment with a PHD-inhibitor activating HIFs prevents graft injury and prolongs survival in an allogenic kidney transplant model. Proc. Natl Acad. Sci. USA 106, 21276-21281 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21276-21281
    • Bernhardt, W.M.1
  • 145
    • 84910046131 scopus 로고    scopus 로고
    • Erythropoietin and organ protection: Lessons from negative clinical trials
    • Pearl, R. G. Erythropoietin and organ protection: lessons from negative clinical trials. Crit. Care 18, 526 (2014
    • (2014) Crit. Care , vol.18 , pp. 526
    • Pearl, R.G.1
  • 146
    • 84908349650 scopus 로고    scopus 로고
    • Hypoxic signaling during tissue repair and regenerative medicine
    • Nauta, T. D., van Hinsbergh, V. W., & Koolwijk, P. Hypoxic signaling during tissue repair and regenerative medicine. Int. J. Mol. Sci. 15, 19791-19815 (2014
    • (2014) Int. J. Mol. Sci , vol.15 , pp. 19791-19815
    • Nauta, T.D.1    Van Hinsbergh, V.W.2    Koolwijk, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.