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Volumn , Issue , 2005, Pages 61-86

Erythropoietin and erythropoiesis

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EID: 33646539955     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (110)
  • 1
    • 0011364893 scopus 로고
    • Human erythropoietin gene: High level expression in stably transfected mammalian cells and chromosome localization
    • Powell JS, Berkner KL, Lebo RV, Adamson JW. Human erythropoietin gene: high level expression in stably transfected mammalian cells and chromosome localization. Proc Natl Acad Sci USA 1986; 83:6465-6469.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6465-6469
    • Powell, J.S.1    Berkner, K.L.2    Lebo, R.V.3    Adamson, J.W.4
  • 4
    • 0023550727 scopus 로고
    • Structural characterization of natural human urinary and recombinant DNA-derived erythropoietin. Identification of des-arginine 166 erythro poietin
    • Recny MA, Scoble HA, Kim Y. Structural characterization of natural human urinary and recombinant DNA-derived erythropoietin. Identification of des-arginine 166 erythro poietin. J Biol Chem 1987; 262:17156-17163.
    • (1987) J Biol Chem , vol.262 , pp. 17156-17163
    • Recny, M.A.1    Scoble, H.A.2    Kim, Y.3
  • 5
    • 0021908684 scopus 로고
    • The role of carbohydrate in erythropoietin action
    • Dordal MS, Wang FF, Goldwasser E. The role of carbohydrate in erythropoietin action. Endocrinology 1985; 116:2293-2299.
    • (1985) Endocrinology , vol.116 , pp. 2293-2299
    • Dordal, M.S.1    Wang, F.F.2    Goldwasser, E.3
  • 8
    • 0029763919 scopus 로고    scopus 로고
    • Lectin-binding assays for the isoforms of human erythropoietin:Comparison of urinary and four recombinant erythropoietins
    • Storring PL, Tiplady RJ, Gaines-Das RE, Rafferty B, Mistry YG. Lectin-binding assays for the isoforms of human erythropoietin:comparison of urinary and four recombinant erythropoietins. J Endocrinol 1996; 150:401-412.
    • (1996) J Endocrinol , vol.150 , pp. 401-412
    • Storring, P.L.1    Tiplady, R.J.2    Gaines-Das, R.E.3    Rafferty, B.4    Mistry, Y.G.5
  • 9
    • 0015353290 scopus 로고
    • Electrophoretic behavior of erythropoietin in polyacrylamide gel
    • Dorado M, Langton AA, Brandan NC, Espada J. Electrophoretic behavior of erythropoietin in polyacrylamide gel. Biochem Med 1972; 6:238-245.
    • (1972) Biochem Med , vol.6 , pp. 238-245
    • Dorado, M.1    Langton, A.A.2    Brandan, N.C.3    Espada, J.4
  • 10
    • 0025948397 scopus 로고
    • Comparisons of human, rat and mouse erythropoietins by isoelectric focusing: Differences between serum and urinary erythropoietins
    • Tam RC, Coleman SL, Tiplady RJ, Storring PL, Cotes PM. Comparisons of human, rat and mouse erythropoietins by isoelectric focusing: differences between serum and urinary erythropoietins. Br J Haematol 1991; 79:504-511.
    • (1991) Br J Haematol , vol.79 , pp. 504-511
    • Tam, R.C.1    Coleman, S.L.2    Tiplady, R.J.3    Storring, P.L.4    Cotes, P.M.5
  • 11
    • 0025123840 scopus 로고
    • Molecular charge heterogeneity of human serum erythropoietin
    • Wide L, Bengtsson C. Molecular charge heterogeneity of human serum erythropoietin. Br J Haematol 1990; 76:121-127.
    • (1990) Br J Haematol , vol.76 , pp. 121-127
    • Wide, L.1    Bengtsson, C.2
  • 14
    • 0036865723 scopus 로고    scopus 로고
    • The enigma of the metabolic fate of circulating erythropoietin (Epo) in view of the pharmacokinetics of the recombinant drugs rhEpo and NESP
    • Jelkmann W. The enigma of the metabolic fate of circulating erythropoietin (Epo) in view of the pharmacokinetics of the recombinant drugs rhEpo and NESP. Eur J Haematol 2002; 69:265-274.
    • (2002) Eur J Haematol , vol.69 , pp. 265-274
    • Jelkmann, W.1
  • 16
    • 0023248840 scopus 로고
    • Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells
    • Davis JM, Arakawa T, Strickland TW, Yphantis DA. Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells. Biochemistry 1987; 26:2633-2638.
    • (1987) Biochemistry , vol.26 , pp. 2633-2638
    • Davis, J.M.1    Arakawa, T.2    Strickland, T.W.3    Yphantis, D.A.4
  • 17
    • 0029348847 scopus 로고
    • Effect of low dose recombinant human omega erythropoietin (rHuEPO) on anaemia in patients on hemodialysis
    • Acharya VN, Sinha DK, Almeida AF, Pathare AV. Effect of low dose recombinant human omega erythropoietin (rHuEPO) on anaemia in patients on hemodialysis. J Assoc Physicians India 1995; 43:539-542.
    • (1995) J Assoc Physicians India , vol.43 , pp. 539-542
    • Acharya, V.N.1    Sinha, D.K.2    Almeida, A.F.3    Pathare, A.V.4
  • 18
    • 0036125372 scopus 로고    scopus 로고
    • A comparison between epoetin omega and epoetin alfa in the correction of anemia in hemodialysis patients: A prospective, controlled crossover study
    • Bren A, Kandus A, Varl J, Buturovic J, Ponikvar R, Kveder R, Primozic S, Ivanovich P. A comparison between epoetin omega and epoetin alfa in the correction of anemia in hemodialysis patients: a prospective, controlled crossover study. Artif Organs 2002; 26:91-97.
    • (2002) Artif Organs , vol.26 , pp. 91-97
    • Bren, A.1    Kandus, A.2    Varl, J.3    Buturovic, J.4    Ponikvar, R.5    Kveder, R.6    Primozic, S.7    Ivanovich, P.8
  • 19
    • 0036197002 scopus 로고    scopus 로고
    • Epoetin omega for treatment of anemia in maintenance hemodialysis patients
    • Sikole A, Spasovski G, Zafirov D, Polenakovic M. Epoetin omega for treatment of anemia in maintenance hemodialysis patients. Clin Nephrol 2002; 57:237-245.
    • (2002) Clin Nephrol , vol.57 , pp. 237-245
    • Sikole, A.1    Spasovski, G.2    Zafirov, D.3    Polenakovic, M.4
  • 20
    • 0023645520 scopus 로고
    • Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA
    • Sasaki H, Bothner B, Dell A, Fukuda M. Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA. J Biol Chem 1987; 262:12059-12076.
    • (1987) J Biol Chem , vol.262 , pp. 12059-12076
    • Sasaki, H.1    Bothner, B.2    Dell, A.3    Fukuda, M.4
  • 21
    • 0025268959 scopus 로고
    • Physicochemical and biological comparison of recombinant human erythropoietin with human urinary erythropoietin
    • Imai N, Kawamura A, Higuchi M, Oh-eda M, Orita T, Kawaguchi T, Ochi N. Physicochemical and biological comparison of recombinant human erythropoietin with human urinary erythropoietin. J Biochem (Tokyo) 1990; 107:352-359.
    • (1990) J Biochem (Tokyo) , vol.107 , pp. 352-359
    • Imai, N.1    Kawamura, A.2    Higuchi, M.3    Oheda, M.4    Orita, T.5    Kawaguchi, T.6    Ochi, N.7
  • 22
    • 0035895071 scopus 로고    scopus 로고
    • Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin
    • Skibeli V, Nissen-Lie G, Torjesen P. Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin. Blood 2001; 98:3626-3634.
    • (2001) Blood , vol.98 , pp. 3626-3634
    • Skibeli, V.1    Nissen-Lie, G.2    Torjesen, P.3
  • 23
    • 0034997401 scopus 로고    scopus 로고
    • Development and characterization of novel erythropoiesis stimulating protein (NESP)
    • Egrie JK, Browne JK. Development and characterization of novel erythropoiesis stimulating protein (NESP). Br J Cancer 2001; 84:3-10.
    • (2001) Br J Cancer , vol.84 , pp. 3-10
    • Egrie, J.K.1    Browne, J.K.2
  • 25
    • 0027410945 scopus 로고
    • Co-localization of erythropoietin mRNA and ecto-50-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin
    • Bachmann S, Le Hir M, Eckardt KU. Co-localization of erythropoietin mRNA and ecto-50-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin. J Histochem Cytochem 1993; 41:335-341.
    • (1993) J Histochem Cytochem , vol.41 , pp. 335-341
    • Bachmann, S.1    Le Hir, M.2    Eckardt, K.U.3
  • 30
    • 0026526168 scopus 로고
    • Erythropoietin: Structure, control of production, and function
    • Jelkmann W. Erythropoietin: structure, control of production, and function. Physiol Rev 1992; 72:449-489.
    • (1992) Physiol Rev , vol.72 , pp. 449-489
    • Jelkmann, W.1
  • 31
    • 0036037635 scopus 로고    scopus 로고
    • From erythropoietin to oxygen: Hypoxia-inducible factor hydroxylases and the hypoxia signal pathway
    • Ratcliffe P. From erythropoietin to oxygen: hypoxia-inducible factor hydroxylases and the hypoxia signal pathway. Blood Purif 2002; 20:445-450.
    • (2002) Blood Purif , vol.20 , pp. 445-450
    • Ratcliffe, P.1
  • 32
    • 0036320934 scopus 로고    scopus 로고
    • Cellular adaptation to hypoxia:O2-sensing protein hydroxylases, hypoxia-inducible transcription factors, and O2-regulated gene expression
    • Wenger RH. Cellular adaptation to hypoxia:O2-sensing protein hydroxylases, hypoxia-inducible transcription factors, and O2-regulated gene expression. FASEB J 2002; 16:1151-1162.
    • (2002) FASEB J , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 33
    • 0027210562 scopus 로고
    • General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia
    • Wang GL, Semenza GL. General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia. Proc Natl Acad Sci USA 1993; 90:4304-4308.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 34
    • 0029051439 scopus 로고
    • Hypoxiainducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, Semenza GL. Hypoxiainducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci USA 1995; 92:5510-5514.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 35
    • 0029859510 scopus 로고    scopus 로고
    • Hypoxia -inducible factor 1 levels vary exponentially over a physio logically relevant range of O2 tension
    • Jiang BH, Semenza GL, Bauer C, Marti HH. Hypoxia -inducible factor 1 levels vary exponentially over a physio logically relevant range of O2 tension. Am J Physiol 1996; 271:C1172-C1180.
    • (1996) Am J Physiol , vol.271 , pp. C1172-C1180
    • Jiang, B.H.1    Semenza, G.L.2    Bauer, C.3    Marti, H.H.4
  • 36
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxiainducible factor-a chains activated by prolyl hydroxylation
    • Masson N, William C, Maxwell PH, Pugh CW, Ratcliffe PJ. Independent function of two destruction domains in hypoxiainducible factor-a chains activated by prolyl hydroxylation. EMBO J 2001; 20:5197-5206.
    • (2001) EMBO J , vol.20 , pp. 5197-5206
    • Masson, N.1    William, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 40
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4- hydroxylases that modify HIF
    • Bruick RK, McKnight SL. A conserved family of prolyl-4- hydroxylases that modify HIF. Science 2001; 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 41
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1a and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon PC, Hirota K, Semenza GL. FIH-1: a novel protein that interacts with HIF-1a and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 2001; 15:2675-2686.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 43
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 2002; 16:1466-1471.
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 44
    • 0036846033 scopus 로고    scopus 로고
    • Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803
    • McNeill LA, Hewitson KS, Claridge TD, Seibel JF, Horsfall LE. Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. Biochem J 2003; 367:571-575.
    • (2003) Biochem J , vol.367 , pp. 571-575
    • McNeill, L.A.1    Hewitson, K.S.2    Claridge, T.D.3    Seibel, J.F.4    Horsfall, L.E.5
  • 49
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1a (HIF-1a) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda S, Caro J. Hypoxia-inducible factor 1a (HIF-1a) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J Biol Chem 1997; 272:22642-22647.
    • (1997) J Biol Chem , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 50
    • 0035478294 scopus 로고    scopus 로고
    • Transduction pathways involved in hypoxia-inducible factor-1 phosphorylation and activation
    • Minet E, Michel G, Mottet D, Raes M, Michiels C. Transduction pathways involved in hypoxia-inducible factor-1 phosphorylation and activation. Free Radic Biol Med 2001; 31:847-855.
    • (2001) Free Radic Biol Med , vol.31 , pp. 847-855
    • Minet, E.1    Michel, G.2    Mottet, D.3    Raes, M.4    Michiels, C.5
  • 51
    • 0035880239 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain
    • Vaux EC, Metzen E, Yeates KM, Ratcliffe PJ. Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain. Blood 2001; 98:296-302.
    • (2001) Blood , vol.98 , pp. 296-302
    • Vaux, E.C.1    Metzen, E.2    Yeates, K.M.3    Ratcliffe, P.J.4
  • 52
    • 0035933716 scopus 로고    scopus 로고
    • Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway
    • Srinivas V, Leshchinsky I, Sang N, King MP, Minchenko A, Caro J. Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway. J Biol Chem 2001; 276:21995-21998.
    • (2001) J Biol Chem , vol.276 , pp. 21995-21998
    • Srinivas, V.1    Leshchinsky, I.2    Sang, N.3    King, M.P.4    Minchenko, A.5    Caro, J.6
  • 53
    • 0028244438 scopus 로고
    • Positive and negative regulation of the erythropoietin gene
    • Imagawa S, Izumi T, Miura Y. Positive and negative regulation of the erythropoietin gene. J Biol Chem 1994; 269:9038-9044.
    • (1994) J Biol Chem , vol.269 , pp. 9038-9044
    • Imagawa, S.1    Izumi, T.2    Miura, Y.3
  • 54
    • 0031043063 scopus 로고    scopus 로고
    • Negative regulation of the erythropoietin gene expression by the GATA transcription factors
    • Imagawa S, Yamamoto M, Miura Y. Negative regulation of the erythropoietin gene expression by the GATA transcription factors. Blood 1997; 89:1430-1439.
    • (1997) Blood , vol.89 , pp. 1430-1439
    • Imagawa, S.1    Yamamoto, M.2    Miura, Y.3
  • 55
    • 0027241363 scopus 로고
    • The human erythropoietin-encoding gene contains a CAAT box, TATA boxes and other transcriptional regulatory elements in its 50 flanking region
    • Lee HS, Lin JJ, Kung HF, Huang PL, Lee L, Huang PL. The human erythropoietin-encoding gene contains a CAAT box, TATA boxes and other transcriptional regulatory elements in its 50 flanking region. Gene 1993; 128:227-236.
    • (1993) Gene , vol.128 , pp. 227-236
    • Lee, H.S.1    Lin, J.J.2    Kung, H.F.3    Huang, P.L.4    Lee, L.5    Huang, P.L.6
  • 56
    • 0036832772 scopus 로고    scopus 로고
    • Inhibition of erythropoietin gene expression signaling involves the transcription factors GATA-2 and NF-kB
    • La Ferla K, Reimann C, Jelkmann W, Hellwig-Bürgel T. Inhibition of erythropoietin gene expression signaling involves the transcription factors GATA-2 and NF-kB. FASEB J 2002; 16:1811-1813.
    • (2002) FASEB J , vol.16 , pp. 1811-1813
    • La Ferla, K.1    Reimann, C.2    Jelkmann, W.3    Hellwig-Bürgel, T.4
  • 57
    • 0033001379 scopus 로고    scopus 로고
    • Tumor necrosis factor p55 receptor (TNF-RI) mediates the in vitro inhibition of hepatic erythropoietin production
    • Jelkmann W, Hellwig-Buergel T. Tumor necrosis factor p55 receptor (TNF-RI) mediates the in vitro inhibition of hepatic erythropoietin production. Exp Hematol 1999; 27:224-228.
    • (1999) Exp Hematol , vol.27 , pp. 224-228
    • Jelkmann, W.1    Hellwig-Buergel, T.2
  • 59
    • 0024322837 scopus 로고
    • Quantitation of erythropoietin-producing cells in kidneys of mice by in situ hybridization: Correlation with hematocrit, renal erythropoietin mRNA, and serum erythropoietin concentration
    • Koury ST, Koury MJ, Bondurant MC, Caro J, Graber SE. Quantitation of erythropoietin-producing cells in kidneys of mice by in situ hybridization: correlation with hematocrit, renal erythropoietin mRNA, and serum erythropoietin concentration. Blood 1989; 74:645-651.
    • (1989) Blood , vol.74 , pp. 645-651
    • Koury, S.T.1    Koury, M.J.2    Bondurant, M.C.3    Caro, J.4    Graber, S.E.5
  • 60
    • 0024253443 scopus 로고
    • A comparison of the effects of renal artery constriction and anemia on the production of erythropoietin
    • Pagel H, Jelkmann W, Weiss C. A comparison of the effects of renal artery constriction and anemia on the production of erythropoietin. Pflugers Arch 1988; 413:62-66.
    • (1988) Pflugers Arch , vol.413 , pp. 62-66
    • Pagel, H.1    Jelkmann, W.2    Weiss, C.3
  • 61
    • 0013877501 scopus 로고
    • The central nervous system in regulation of erythropoiesis
    • Halvorsen S. The central nervous system in regulation of erythropoiesis. Acta Haematol 1966; 35:65-79.
    • (1966) Acta Haematol , vol.35 , pp. 65-79
    • Halvorsen, S.1
  • 62
    • 0014433970 scopus 로고
    • Extra-renal and renal control of erythropoietin production
    • Mirand EA. Extra-renal and renal control of erythropoietin production. Ann N Y Acad Sci 1968; 149:94-106.
    • (1968) Ann N Y Acad Sci , vol.149 , pp. 94-106
    • Mirand, E.A.1
  • 63
    • 0024515126 scopus 로고
    • Circadian rhythm of erythropoietin in human serum
    • Wide L, Bengtsson C, Birgegard G. Circadian rhythm of erythropoietin in human serum. Br J Haematol 1989; 72:85-90.
    • (1989) Br J Haematol , vol.72 , pp. 85-90
    • Wide, L.1    Bengtsson, C.2    Birgegard, G.3
  • 65
    • 0030734731 scopus 로고    scopus 로고
    • Erythropoietin: Physiology and pharmacology update
    • Fisher JW. Erythropoietin: physiology and pharmacology update. Proc Soc Exp Biol Med 2003; 216:358-369.
    • (2003) Proc Soc Exp Biol Med , vol.216 , pp. 358-369
    • Fisher, J.W.1
  • 66
    • 0032520980 scopus 로고    scopus 로고
    • Red blood cell precursor mass as an independent determinant of serum erythropoietin level
    • Cazzola M, Guarnone R, Cerani P, Centenara E, Rovati A, Beguin Y. Red blood cell precursor mass as an independent determinant of serum erythropoietin level. Blood 1998; 91:2139-2145.
    • (1998) Blood , vol.91 , pp. 2139-2145
    • Cazzola, M.1    Guarnone, R.2    Cerani, P.3    Centenara, E.4    Rovati, A.5    Beguin, Y.6
  • 67
    • 0021270306 scopus 로고
    • Effects of oxygen inhalation on endogenous erythropoietin kinetics, erythropoiesis, and properties of blood cells in sickle-cell anemia
    • Embury SH, Garcia JF, Mohandas N, Pennathur DR, Clark MR. Effects of oxygen inhalation on endogenous erythropoietin kinetics, erythropoiesis, and properties of blood cells in sickle-cell anemia. N Engl J Med 1984; 311:291-295.
    • (1984) N Engl J Med , vol.311 , pp. 291-295
    • Embury, S.H.1    Garcia, J.F.2    Mohandas, N.3    Pennathur, D.R.4    Clark, M.R.5
  • 69
    • 0015491311 scopus 로고
    • The second international reference preparation of erythropoietin, human, urinary, for bioassay
    • Annable L, Cotes PM, Mussett MV. The second international reference preparation of erythropoietin, human, urinary, for bioassay. Bull World Health Organ 1972; 47:99-112.
    • (1972) Bull World Health Organ , vol.47 , pp. 99-112
    • Annable, L.1    Cotes, P.M.2    Mussett, M.V.3
  • 70
    • 0026786258 scopus 로고
    • The International Standard for Recombinant DNA-derived Erythropoietin: Collaborative study of four recombinant DNA-derived erythropoietins and two highly purified human urinary erythropoietins
    • Storring PL, Gaines DR. The International Standard for Recombinant DNA-derived Erythropoietin: collaborative study of four recombinant DNA-derived erythropoietins and two highly purified human urinary erythropoietins. J Endocrinol 1992; 134:459-484.
    • (1992) J Endocrinol , vol.134 , pp. 459-484
    • Storring, P.L.1    Gaines, D.R.2
  • 71
    • 4644229227 scopus 로고    scopus 로고
    • Biochemistry and assays of Epo
    • Jelkmann W, ed, Johnson City, TN: FP Graham Publishing Co
    • Jelkmann W. Biochemistry and assays of Epo. In: Jelkmann W, ed. Erythropoietin: Molecular Biology and Clinical Use. Johnson City, TN: FP Graham Publishing Co., 2003:35-63.
    • (2003) Erythropoietin: Molecular Biology and Clinical Use , pp. 35-63
    • Jelkmann, W.1
  • 72
    • 0025276054 scopus 로고
    • Treatment of the anemia of chronic renal failure with recombinant human erythropoietin
    • Adamson JW, Eschbach JW. Treatment of the anemia of chronic renal failure with recombinant human erythropoietin. Annu Rev Med 1990; 41:349-360.
    • (1990) Annu Rev Med , vol.41 , pp. 349-360
    • Adamson, J.W.1    Eschbach, J.W.2
  • 73
    • 0026760450 scopus 로고
    • Progress in understanding the pathogenesis of the anemia of chronic disease
    • Means RT, Krantz SB. Progress in understanding the pathogenesis of the anemia of chronic disease. Blood 1992; 80:1639-1647.
    • (1992) Blood , vol.80 , pp. 1639-1647
    • Means, R.T.1    Krantz, S.B.2
  • 74
    • 0031821059 scopus 로고    scopus 로고
    • Proinflammatory cytokines lowering erythropoietin production
    • Jelkmann W. Proinflammatory cytokines lowering erythropoietin production. J Interferon Cytokine Res 1998; 18:555-559.
    • (1998) J Interferon Cytokine Res , vol.18 , pp. 555-559
    • Jelkmann, W.1
  • 75
    • 0034643632 scopus 로고    scopus 로고
    • The blood in systemic disorders
    • Spivak JL. The blood in systemic disorders. Lancet 2000; 355:1707-1712.
    • (2000) Lancet , vol.355 , pp. 1707-1712
    • Spivak, J.L.1
  • 76
    • 0026561396 scopus 로고
    • New tools for clinical evaluation of erythron function in man
    • Cazzola M, Beguin Y. New tools for clinical evaluation of erythron function in man. Br J Haematol 1992; 80:278-284.
    • (1992) Br J Haematol , vol.80 , pp. 278-284
    • Cazzola, M.1    Beguin, Y.2
  • 77
    • 0027524551 scopus 로고
    • Early prediction of response to recombinant human erythropoietin in patients with the anemia of renal failure by serum transferrin receptor and fibrinogen
    • Beguin Y, Loo M, R’Zik S, Sautois B, Lejeune F, Rorive G, Fillet G. Early prediction of response to recombinant human erythropoietin in patients with the anemia of renal failure by serum transferrin receptor and fibrinogen. Blood 1993; 82:2010-2016.
    • (1993) Blood , vol.82 , pp. 2010-2016
    • Beguin, Y.1    Loo, M.2    R’Zik, S.3    Sautois, B.4    Lejeune, F.5    Rorive, G.6    Fillet, G.7
  • 78
    • 0025123918 scopus 로고
    • Erythropoietin receptor. Subunit structure and activation
    • D’Andrea AD, Zon LI. Erythropoietin receptor. Subunit structure and activation. J Clin Invest 1990; 86:681-687.
    • (1990) J Clin Invest , vol.86 , pp. 681-687
    • D’Andrea, A.D.1    Zon, L.I.2
  • 80
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 1999; 283:987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 81
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy I, Wilson IA, Michnick SW. Erythropoietin receptor activation by a ligand-induced conformation change. Science 1999; 283:990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 82
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, Ihle JN. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 1993; 74:227-236.
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3    Yi, T.4    Tang, B.5    Miura, O.6    Ihle, J.N.7
  • 83
    • 0030709473 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation in proliferation and maturation of erythroid progenitor cells-signals emanating from the erythropoietin receptor
    • Klingmuller U. The role of tyrosine phosphorylation in proliferation and maturation of erythroid progenitor cells-signals emanating from the erythropoietin receptor. Eur J Biochem 1997; 249:637-647.
    • (1997) Eur J Biochem , vol.249 , pp. 637-647
    • Klingmuller, U.1
  • 84
    • 0035102191 scopus 로고    scopus 로고
    • The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif
    • Constantinescu SN, Huang LJ, Nam H, Lodish HF. The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif. Mol Cell 2001; 7:377-385.
    • (2001) Mol Cell , vol.7 , pp. 377-385
    • Constantinescu, S.N.1    Huang, L.J.2    Nam, H.3    Lodish, H.F.4
  • 85
    • 0028852393 scopus 로고
    • Hematopoietic cell phosphatase associates with erythropoietin (Epo) receptor after Epo-induced receptor tyrosine phosphorylation: Identification of potential binding sites
    • Yi T, Zhang J, Miura O, Ihle JN. Hematopoietic cell phosphatase associates with erythropoietin (Epo) receptor after Epo-induced receptor tyrosine phosphorylation: identification of potential binding sites. Blood 1995; 85:87-95.
    • (1995) Blood , vol.85 , pp. 87-95
    • Yi, T.1    Zhang, J.2    Miura, O.3    Ihle, J.N.4
  • 86
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmuller U, Lorenz U, Cantley LC, Neel BG, Lodish HF. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 1995; 80:729-738.
    • (1995) Cell , vol.80 , pp. 729-738
    • Klingmuller, U.1    Lorenz, U.2    Cantley, L.C.3    Neel, B.G.4    Lodish, H.F.5
  • 87
    • 0034839931 scopus 로고    scopus 로고
    • Genetic heterogeneity of primary familial and congenital polycythemia
    • Kralovics R, Prchal JT. Genetic heterogeneity of primary familial and congenital polycythemia. Am J Hematol 2001; 68:115-121.
    • (2001) Am J Hematol , vol.68 , pp. 115-121
    • Kralovics, R.1    Prchal, J.T.2
  • 88
    • 0036786352 scopus 로고    scopus 로고
    • Erythroid-specific expression of the erythropoietin receptor rescued its null mutant mice from lethality
    • Suzuki N, Ohneda O, Takahashi S, Higuchi M, Mukai HY, Nakahata T, Imagawa S, Yamamoto M. Erythroid-specific expression of the erythropoietin receptor rescued its null mutant mice from lethality. Blood 2002; 100:2279-2288.
    • (2002) Blood , vol.100 , pp. 2279-2288
    • Suzuki, N.1    Ohneda, O.2    Takahashi, S.3    Higuchi, M.4    Mukai, H.Y.5    Nakahata, T.6    Imagawa, S.7    Yamamoto, M.8
  • 89
    • 0027436101 scopus 로고
    • Serum form of the erythropoietin receptor identified by a sequencespecific peptide antibody
    • Baynes RD, Reddy GK, Shih YJ, Skikne BS, Cook JD. Serum form of the erythropoietin receptor identified by a sequencespecific peptide antibody. Blood 1993; 82:2088-2095.
    • (1993) Blood , vol.82 , pp. 2088-2095
    • Baynes, R.D.1    Reddy, G.K.2    Shih, Y.J.3    Skikne, B.S.4    Cook, J.D.5
  • 90
    • 0029914394 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay detects a potential soluble form of the erythropoietin receptor in human plasma
    • Harris KW, Winkelmann JC. Enzyme-linked immunosorbent assay detects a potential soluble form of the erythropoietin receptor in human plasma. Am J Hematol 1996; 52:8-13.
    • (1996) Am J Hematol , vol.52 , pp. 8-13
    • Harris, K.W.1    Winkelmann, J.C.2
  • 91
    • 0027049472 scopus 로고
    • The molecular mechanism of erythropoietin action
    • Koury MJ, Bondurant MC. The molecular mechanism of erythropoietin action. Eur J Biochem 1992; 210:649-663.
    • (1992) Eur J Biochem , vol.210 , pp. 649-663
    • Koury, M.J.1    Bondurant, M.C.2
  • 93
    • 0037114625 scopus 로고    scopus 로고
    • Polycythemia vera: Myths, mechanisms, and management
    • Spivak JL. Polycythemia vera: myths, mechanisms, and management. Blood 2002; 100:4272-4290.
    • (2002) Blood , vol.100 , pp. 4272-4290
    • Spivak, J.L.1
  • 94
    • 0035669505 scopus 로고    scopus 로고
    • Idiopathic erythrocytosis-a declining entity
    • Blacklock HA, Royle GA. Idiopathic erythrocytosis-a declining entity. Br J Haematol 2001; 115:774-781.
    • (2001) Br J Haematol , vol.115 , pp. 774-781
    • Blacklock, H.A.1    Royle, G.A.2
  • 95
    • 0037097562 scopus 로고    scopus 로고
    • Purification and characterization of the yeast-expressed erythropoietin mutant Epo (R103A), a specific inhibitor of human primary hematopoietic cell erythropoiesis
    • Burns S, Arcasoy MO, Li L, Kurian E, Selander K, Emanuel PD, Harris KW. Purification and characterization of the yeast-expressed erythropoietin mutant Epo (R103A), a specific inhibitor of human primary hematopoietic cell erythropoiesis. Blood 2002; 99:4400-4405.
    • (2002) Blood , vol.99 , pp. 4400-4405
    • Burns, S.1    Arcasoy, M.O.2    Li, L.3    Kurian, E.4    Selander, K.5    Emanuel, P.D.6    Harris, K.W.7
  • 96
    • 0036189341 scopus 로고    scopus 로고
    • Effects of losartan or enalapril on hemoglobin, circulating erythropoietin, and insulin-like growth factor-1 in patients with and without posttransplant erythrocytosis
    • Wang AY-M, Yu AW-Y, Lam CW-K, Yu LM, Li PK-T, Goh J, Lui SF. Effects of losartan or enalapril on hemoglobin, circulating erythropoietin, and insulin-like growth factor-1 in patients with and without posttransplant erythrocytosis. Am J Kidney Dis 2002; 39:600-608.
    • (2002) Am J Kidney Dis , vol.39 , pp. 600-608
    • Wang, A.Y.-M.1    Yu, A.W.-Y.2    Lam, C.W.-K.3    Yu, L.M.4    Li, P.K.-T.5    Goh, J.6    Lui, S.F.7
  • 98
    • 0034232059 scopus 로고    scopus 로고
    • Use of recombinant human erythropoietin as an antianemic and performance enhancing drug
    • Jelkmann W. Use of recombinant human erythropoietin as an antianemic and performance enhancing drug. Curr Pharmaceut Biotechnol 2000; 1:11-31.
    • (2000) Curr Pharmaceut Biotechnol , vol.1 , pp. 11-31
    • Jelkmann, W.1
  • 99
    • 0037102975 scopus 로고    scopus 로고
    • Relationship between changes in hemoglobin level and quality of life during chemotherapy in anemic cancer patients receiving epoetin alfa therapy
    • Crawford J, Cella D, Cleeland CS, Cremieux PY, Demetri GD, Sarokhan BJ, Slavin MB, Glaspy JA. Relationship between changes in hemoglobin level and quality of life during chemotherapy in anemic cancer patients receiving epoetin alfa therapy. Cancer 2002; 95:888-895.
    • (2002) Cancer , vol.95 , pp. 888-895
    • Crawford, J.1    Cella, D.2    Cleeland, C.S.3    Cremieux, P.Y.4    Demetri, G.D.5    Sarokhan, B.J.6    Slavin, M.B.7    Glaspy, J.A.8
  • 104
    • 0033894551 scopus 로고    scopus 로고
    • Effects of desferrioxamine on serum erythropoietin and ventilatory sensitivity to hypoxia in humans
    • Ren X, Dorrington KL, Maxwell PH, Robbins PA. Effects of desferrioxamine on serum erythropoietin and ventilatory sensitivity to hypoxia in humans. J Appl Physiol 2000; 89:680-686.
    • (2000) J Appl Physiol , vol.89 , pp. 680-686
    • Ren, X.1    Dorrington, K.L.2    Maxwell, P.H.3    Robbins, P.A.4
  • 109
    • 0024046959 scopus 로고
    • Hormones that stimulate the growth of blood cells
    • Golde DW, Gasson JC. Hormones that stimulate the growth of blood cells. Sci Am 1988; 259:62-71.
    • (1988) Sci Am , vol.259 , pp. 62-71
    • Golde, D.W.1    Gasson, J.C.2


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