메뉴 건너뛰기




Volumn 116, Issue 24, 2010, Pages 5357-5367

Transferrin receptor 2 is a component of the erythropoietin receptor complex and is required for efficient erythropoiesis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE RECEPTOR; ERYTHROPOIETIN RECEPTOR; GROWTH DIFFERENTIATION FACTOR 15; HEPCIDIN; HOMODIMER; IRON; TRANSFERRIN RECEPTOR 2;

EID: 78650037490     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-04-281360     Document Type: Article
Times cited : (119)

References (47)
  • 1
    • 0028880455 scopus 로고
    • Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor
    • Wu H, Liu X, Jaenish R, Lodish HF. Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor. Cell. 1995;83(1):59-67.
    • (1995) Cell , vol.83 , Issue.1 , pp. 59-67
    • Wu, H.1    Liu, X.2    Jaenish, R.3    Lodish, H.F.4
  • 2
    • 0023656554 scopus 로고
    • The erythropoietin receptor of rat erythroid progenitor cell: Characterization and affinity cross-linkage
    • Mayeux P, Billat C, Jacquot R. The erythropoietin receptor of rat erythroid progenitor cell: characterization and affinity cross-linkage. J Biol Chem. 1987;262(29):13985-13990.
    • (1987) J Biol Chem , vol.262 , Issue.29 , pp. 13985-13990
    • Mayeux, P.1    Billat, C.2    Jacquot, R.3
  • 3
    • 0035694582 scopus 로고    scopus 로고
    • The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor
    • Huang LJ, Constantinescu SN, Lodish HF. The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor. Mol Cell. 2001;8(6):1327-1338.
    • (2001) Mol Cell , vol.8 , Issue.6 , pp. 1327-1338
    • Huang, L.J.1    Constantinescu, S.N.2    Lodish, H.F.3
  • 4
    • 0025368581 scopus 로고
    • Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism
    • DOI 10.1073/pnas.87.11.4139
    • Yoshimura A, D'Andrea AD, Lodish HF. Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism. Proc Natl Acad Sci U S A. 1990;87(11):4139-4143. (Pubitemid 20217997)
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.11 , pp. 4139-4143
    • Yoshimura, A.1    D'Andrea, A.D.2    Lodish, H.F.3
  • 5
    • 0023199248 scopus 로고
    • Identification of the receptor for erythropoietin by cross-linking to Friend virus-infected erythroid cells
    • Sawyer ST, Krantz SB, Luna J. Identification of the receptor for erythropoietin by cross-linking to Friend virus-infected erythroid cells. Proc Natl Acad Sci U S A. 1987;84(11):3690-3694.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , Issue.11 , pp. 3690-3694
    • Sawyer, S.T.1    Krantz, S.B.2    Luna, J.3
  • 6
    • 0027533763 scopus 로고
    • Subunit structure of the erythropoietin receptor analyzed by 125I-Epo cross-linking in cells expressing wild-type or mutant receptors
    • Miura O, Ihle JN. Subunit structure of the erythropoietin receptor analyzed by 125I-Epo cross-linking in cells expressing wild-type or mutant receptors. Blood. 1993;81(7):1739-1744.
    • (1993) Blood , vol.81 , Issue.7 , pp. 1739-1744
    • Miura, O.1    Ihle, J.N.2
  • 7
    • 0026976944 scopus 로고
    • Subunit structure and transmembrane signaling of the erythropoietin receptor
    • Showers MO, D'Andrea AD. Subunit structure and transmembrane signaling of the erythropoietin receptor. Int Rev Cytol. 1992;137B:99-120.
    • (1992) Int Rev Cytol , vol.137 B , pp. 99-120
    • Showers, M.O.1    D'Andrea, A.D.2
  • 8
    • 0030909362 scopus 로고    scopus 로고
    • Cell surface organization of the erythropoietin receptor complex differs depending on its mode of activation
    • DOI 10.1074/jbc.272.14.9099
    • Tarr K, Watowich SS, Longmore GD. Cell surface organization of the erythropoietin receptor complex differs depending on its mode of activation. J Biol Chem. 1997;272(14):9099-9107. (Pubitemid 27154913)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9099-9107
    • Tarr, K.1    Watowich, S.S.2    Longmore, G.D.3
  • 9
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy JE, Jin O, Fujiwara Y, Kuo F, Andrews NC. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat Genet. 1999;21(4):396-399.
    • (1999) Nat Genet , vol.21 , Issue.4 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 10
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • Kawabata H, Yang R, Hirama T, et al. Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family. J Biol Chem. 1999;274(30):20826-20832.
    • (1999) J Biol Chem , vol.274 , Issue.30 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3
  • 11
    • 60649103774 scopus 로고    scopus 로고
    • Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression
    • Gao J, Chen J, Kramer M, Tsukamoto H, Zhang AS, Enns CA. Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression. Cell Metab. 2009;9(3):217-227.
    • (2009) Cell Metab , vol.9 , Issue.3 , pp. 217-227
    • Gao, J.1    Chen, J.2    Kramer, M.3    Tsukamoto, H.4    Zhang, A.S.5    Enns, C.A.6
  • 12
    • 0034022636 scopus 로고    scopus 로고
    • The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22
    • Camaschella C, Roetto A, Cali A, et al. The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22. Nat Genet. 2000;25(1):14-15.
    • (2000) Nat Genet , vol.25 , Issue.1 , pp. 14-15
    • Camaschella, C.1    Roetto, A.2    Cali, A.3
  • 13
    • 0036678091 scopus 로고    scopus 로고
    • Targeted mutagenesis of the murine transferrin receptor-2 gene produces hemochromatosis
    • Fleming RE, Ahmann JR, Migas MC, et al. Targeted mutagenesis of the murine transferrin receptor-2 gene produces hemochromatosis. Proc Natl Acad Sci U S A. 2002;99(16):10653-10658.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.16 , pp. 10653-10658
    • Fleming, R.E.1    Ahmann, J.R.2    Migas, M.C.3
  • 14
    • 21044434748 scopus 로고    scopus 로고
    • First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin
    • Wallace DF, Summerville L, Lusby PE, Subramaniam VN. First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin. Gut. 2005;54(7):980-986.
    • (2005) Gut , vol.54 , Issue.7 , pp. 980-986
    • Wallace, D.F.1    Summerville, L.2    Lusby, P.E.3    Subramaniam, V.N.4
  • 15
    • 33846225653 scopus 로고    scopus 로고
    • Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload
    • Wallace DF, Summerville L, Subramaniam VN. Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload. Gastroenterology. 2007;132(1):301-310.
    • (2007) Gastroenterology , vol.132 , Issue.1 , pp. 301-310
    • Wallace, D.F.1    Summerville, L.2    Subramaniam, V.N.3
  • 16
    • 34948904750 scopus 로고    scopus 로고
    • High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
    • Tanno T, Bhanu NV, Oneal PA, et al. High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin. Nat Med. 2007;13(9):1096-1101.
    • (2007) Nat Med , vol.13 , Issue.9 , pp. 1096-1101
    • Tanno, T.1    Bhanu, N.V.2    Oneal, P.A.3
  • 17
    • 0034674778 scopus 로고    scopus 로고
    • Proteasomes regulate the duration of erythropoietin receptor activation by controlling down-regulation of cell surface receptors
    • Verdier F, Walrafen P, Hubert N, et al. Proteasomes regulate the duration of erythropoietin receptor activation by controlling down-regulation of cell surface receptors. J Biol Chem. 2000;275(24):18375-18381.
    • (2000) J Biol Chem , vol.275 , Issue.24 , pp. 18375-18381
    • Verdier, F.1    Walrafen, P.2    Hubert, N.3
  • 18
    • 34250027624 scopus 로고    scopus 로고
    • Beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation
    • Meyer L, Deau B, Forejtnikova H, et al. beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation. Blood. 2007;109(12):5215-5222.
    • (2007) Blood , vol.109 , Issue.12 , pp. 5215-5222
    • Meyer, L.1    Deau, B.2    Forejtnikova, H.3
  • 19
    • 33746618762 scopus 로고    scopus 로고
    • Selected anti-Epo receptor antibodies predict Epo receptor expression
    • Verdier F, Gomez S, Lacombe C, Mayeux P. Selected anti-Epo receptor antibodies predict Epo receptor expression. Blood. 2006;108(3):1106.
    • (2006) Blood , vol.108 , Issue.3 , pp. 1106
    • Verdier, F.1    Gomez, S.2    Lacombe, C.3    Mayeux, P.4
  • 20
    • 0001660768 scopus 로고    scopus 로고
    • Purification, amplification and characterization of a population of human erythroid progenitors
    • Freyssinier JM, Lecoq-Lafon C, Amsellem S, et al. Purification, amplification and characterization of a population of human erythroid progenitors. Br J Haematol. 1999;106(4):912-922.
    • (1999) Br J Haematol , vol.106 , Issue.4 , pp. 912-922
    • Freyssinier, J.M.1    Lecoq-Lafon, C.2    Amsellem, S.3
  • 21
    • 77951442893 scopus 로고    scopus 로고
    • Comparison of three Tfr2-deficient murine models suggests distinct functions for TFR2 alpha and beta isoforms in different tissues
    • Roetto A, Di Cunto F, Pellegrino RM, et al. Comparison of three Tfr2-deficient murine models suggests distinct functions for TFR2 alpha and beta isoforms in different tissues. Blood. 2010;115(13):3382-3389.
    • (2010) Blood , vol.115 , Issue.13 , pp. 3382-3389
    • Roetto, A.1    Di Cunto, F.2    Pellegrino, R.M.3
  • 22
    • 0035862331 scopus 로고    scopus 로고
    • Caspase activation is required for terminal erythroid differentiation
    • Zermati Y, Garrido C, Amsellem S, et al. Caspase activation is required for terminal erythroid differentiation. J Exp Med. 2001;193(2):247-254.
    • (2001) J Exp Med , vol.193 , Issue.2 , pp. 247-254
    • Zermati, Y.1    Garrido, C.2    Amsellem, S.3
  • 23
    • 0026034133 scopus 로고
    • Establishment and characterization of a human leukemic cell line with megakaryocytic features: Dependency on granulocyte-macrophage colony stimulating factor, interleukin 3, or erythropoietin for growth and survival
    • Komatsu N, Nakauchi H, Miwa A, et al. Establishment and characterization of a human leukemic cell line with megakaryocytic features: dependency on granulocyte-macrophage colony stimulating factor, interleukin 3, or erythropoietin for growth and survival. Cancer Res. 1991;51(1):341-345.
    • (1991) Cancer Res , vol.51 , Issue.1 , pp. 341-345
    • Komatsu, N.1    Nakauchi, H.2    Miwa, A.3
  • 24
    • 0031783567 scopus 로고    scopus 로고
    • Large-scale sequencing of two regions in human chromosome 7q22: Analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes
    • Glockner G, Scherer S, Schattevoy R, et al. Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. Genome Res. 1998;8(10):1060-1073.
    • (1998) Genome Res , vol.8 , Issue.10 , pp. 1060-1073
    • Glockner, G.1    Scherer, S.2    Schattevoy, R.3
  • 25
    • 0037064136 scopus 로고    scopus 로고
    • Shedding of the transferrin receptor is mediated constitutively by an integral membrane metalloprotease sensitive to tumor necrosis factor alpha protease inhibitor-2
    • Kaup M, Dassler K, Weise C, Fuchs H. Shedding of the transferrin receptor is mediated constitutively by an integral membrane metalloprotease sensitive to tumor necrosis factor alpha protease inhibitor-2. J Biol Chem. 2002;277(41):38494-38502.
    • (2002) J Biol Chem , vol.277 , Issue.41 , pp. 38494-38502
    • Kaup, M.1    Dassler, K.2    Weise, C.3    Fuchs, H.4
  • 26
    • 0036786289 scopus 로고    scopus 로고
    • Internal tandem duplication of FLT3 in relapsed acute myeloid leukemia: A comparative analysis of bone marrow samples from 108 adult patients at diagnosis and relapse
    • Shih LY, Huang CF, Wu JH, et al. Internal tandem duplication of FLT3 in relapsed acute myeloid leukemia: a comparative analysis of bone marrow samples from 108 adult patients at diagnosis and relapse. Blood. 2002;100(7):2387-2392.
    • (2002) Blood , vol.100 , Issue.7 , pp. 2387-2392
    • Shih, L.Y.1    Huang, C.F.2    Wu, J.H.3
  • 27
    • 11244273938 scopus 로고    scopus 로고
    • Both proteasomes and lysosomes degrade the activated erythropoietin receptor
    • Walrafen P, Verdier F, Kadri Z, Chretien S, Lacombe C, Mayeux P. Both proteasomes and lysosomes degrade the activated erythropoietin receptor. Blood. 2005;105(2):600-608.
    • (2005) Blood , vol.105 , Issue.2 , pp. 600-608
    • Walrafen, P.1    Verdier, F.2    Kadri, Z.3    Chretien, S.4    Lacombe, C.5    Mayeux, P.6
  • 28
    • 0035525741 scopus 로고    scopus 로고
    • Expression of transferrin receptor 2 in normal and neoplastic hematopoietic cells
    • Kawabata H, Nakamaki T, Ikonomi P, Smith RD, Germain RS, Koeffler HP. Expression of transferrin receptor 2 in normal and neoplastic hematopoietic cells. Blood. 2001;98(9):2714-2719.
    • (2001) Blood , vol.98 , Issue.9 , pp. 2714-2719
    • Kawabata, H.1    Nakamaki, T.2    Ikonomi, P.3    Smith, R.D.4    Germain, R.S.5    Koeffler, H.P.6
  • 29
    • 36349010744 scopus 로고    scopus 로고
    • Transcriptional dysregulation mediated by RUNX1-RUNX1T1 in normal human progenitor cells and in acute myeloid leukaemia
    • Tonks A, Pearn L, Musson M, et al. Transcriptional dysregulation mediated by RUNX1-RUNX1T1 in normal human progenitor cells and in acute myeloid leukaemia. Leukemia. 2007;21(12):2495-2505.
    • (2007) Leukemia , vol.21 , Issue.12 , pp. 2495-2505
    • Tonks, A.1    Pearn, L.2    Musson, M.3
  • 30
    • 8644228649 scopus 로고    scopus 로고
    • Global regulation of erythroid gene expression by transcription factor GATA-1
    • Welch JJ,Watts JA, Vakoc CR, et al. Global regulation of erythroid gene expression by transcription factor GATA-1. Blood. 2004;104(10):3136-3147.
    • (2004) Blood , vol.104 , Issue.10 , pp. 3136-3147
    • Welch, J.J.1    Watts, J.A.2    Vakoc, C.R.3
  • 31
    • 4344576977 scopus 로고    scopus 로고
    • Transferrin receptor 2 protein is not expressed in normal erythroid cells
    • Calzolari A, Deaglio S, Sposi NM, et al. Transferrin receptor 2 protein is not expressed in normal erythroid cells. Biochem J. 2004;381(Pt 3):629-634.
    • (2004) Biochem J , vol.381 , Issue.PART 3 , pp. 629-634
    • Calzolari, A.1    Deaglio, S.2    Sposi, N.M.3
  • 32
    • 0026344547 scopus 로고
    • Structure of the murine erythropoietin receptor complex. Characterization of the erythropoietin cross-linked proteins
    • Mayeux P, Lacombe C, Casadevall N, Chretien S, Dusanter I, Gisselbrecht S. Structure of the murine erythropoietin receptor complex. Characterization of the erythropoietin cross-linked proteins. J Biol Chem. 1991;266(34):23380-23385.
    • (1991) J Biol Chem , vol.266 , Issue.34 , pp. 23380-23385
    • Mayeux, P.1    Lacombe, C.2    Casadevall, N.3    Chretien, S.4    Dusanter, I.5    Gisselbrecht, S.6
  • 33
    • 0033574449 scopus 로고    scopus 로고
    • The advantage of being uncompetitive
    • Chardin P, McCormick F. Brefeldin A: the advantage of being uncompetitive. Cell. 1999;97(2):153-155.
    • (1999) Cell , vol.97 , Issue.2 , pp. 153-155
    • Chardin, P.1    McCormick, F.2    Brefeldin, A.3
  • 34
    • 0344826470 scopus 로고    scopus 로고
    • Role of Ras signaling in erythroid differentiation of mouse fetal liver cells: Functional analysis by a flow cytometry-based novel culture system
    • Zhang J, Socolovsky M, Gross AW, Lodish HF. Role of Ras signaling in erythroid differentiation of mouse fetal liver cells: functional analysis by a flow cytometry-based novel culture system. Blood. 2003;102(12):3938-3946.
    • (2003) Blood , vol.102 , Issue.12 , pp. 3938-3946
    • Zhang, J.1    Socolovsky, M.2    Gross, A.W.3    Lodish, H.F.4
  • 35
    • 0033000191 scopus 로고    scopus 로고
    • The Erythropoietin Receptor: Structure, Activation and Intracellular Signal Transduction
    • Constantinescu SN, Ghaffari S, Lodish HF. The Erythropoietin Receptor: Structure, Activation and Intracellular Signal Transduction. Trends Endocrinol Metab. 1999;10(1):18-23.
    • (1999) Trends Endocrinol Metab , vol.10 , Issue.1 , pp. 18-23
    • Constantinescu, S.N.1    Ghaffari, S.2    Lodish, H.F.3
  • 36
    • 77953582302 scopus 로고    scopus 로고
    • Covering a broad dynamic range: Information processing at the erythropoietin receptor
    • Becker V, Schilling M, Bachmann J, et al. Covering a broad dynamic range: information processing at the erythropoietin receptor. Science. 2010;328(5984):1404-1408.
    • (2010) Science , vol.328 , Issue.5984 , pp. 1404-1408
    • Becker, V.1    Schilling, M.2    Bachmann, J.3
  • 37
    • 0025784395 scopus 로고
    • Multimeric structure of the membrane erythropoietin receptor of murine erythroleukemia cells (Friend cells): Cross-linking of erythropoietin with the Spleen Focus-forming Virus envelope protein
    • Casadevall N, Lacombe C, Muller O, Gisselbrecht S, Mayeux P. Multimeric structure of the membrane erythropoietin receptor of murine erythroleukemia cells (Friend cells): cross-linking of erythropoietin with the Spleen Focus-forming Virus envelope protein. J Biol Chem. 1991;266(24):6952-6956.
    • (1991) J Biol Chem , vol.266 , Issue.24 , pp. 6952-6956
    • Casadevall, N.1    Lacombe, C.2    Muller, O.3    Gisselbrecht, S.4    Mayeux, P.5
  • 38
    • 10244265904 scopus 로고    scopus 로고
    • Diferric transferrin regulates transferrin receptor 2 protein stability
    • Johnson MB, Enns CA. Diferric transferrin regulates transferrin receptor 2 protein stability. Blood. 2004;104(13):4287-4293.
    • (2004) Blood , vol.104 , Issue.13 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 39
    • 70350644759 scopus 로고    scopus 로고
    • A genome-wide meta-analysis identifies 22 loci associated with eight hematological parameters in the HaemGen consortium
    • Soranzo N, Spector TD, Mangino M, et al. A genome-wide meta-analysis identifies 22 loci associated with eight hematological parameters in the HaemGen consortium. Nat Genet. 2009;41(11):1182-1190.
    • (2009) Nat Genet , vol.41 , Issue.11 , pp. 1182-1190
    • Soranzo, N.1    Spector, T.D.2    Mangino, M.3
  • 40
    • 0035353167 scopus 로고    scopus 로고
    • New mutations inactivating transferrin receptor 2 in hemochromatosis type 3
    • Roetto A, Totaro A, Piperno A, et al. New mutations inactivating transferrin receptor 2 in hemochromatosis type 3. Blood. 2001;97(9):2555-2560.
    • (2001) Blood , vol.97 , Issue.9 , pp. 2555-2560
    • Roetto, A.1    Totaro, A.2    Piperno, A.3
  • 41
    • 70349968176 scopus 로고    scopus 로고
    • Natural history of TFR2-related hereditary hemochromatosis in a 47-yr-old Italian patient
    • Ricerca BM, Radio FC, De Marinis L, et al. Natural history of TFR2-related hereditary hemochromatosis in a 47-yr-old Italian patient. Eur J Haematol. 2009;83(5):494-496.
    • (2009) Eur J Haematol , vol.83 , Issue.5 , pp. 494-496
    • Ricerca, B.M.1    Radio, F.C.2    De Marinis, L.3
  • 42
    • 58149092194 scopus 로고    scopus 로고
    • Growth differentiation factor 15 production is necessary for normal erythroid differentiation and is increased in refractory anaemia with ring-sideroblasts
    • Ramirez JM, Schaad O, Durual S, et al. Growth differentiation factor 15 production is necessary for normal erythroid differentiation and is increased in refractory anaemia with ring-sideroblasts. Br J Haematol. 2009;144(2):251-262.
    • (2009) Br J Haematol , vol.144 , Issue.2 , pp. 251-262
    • Ramirez, J.M.1    Schaad, O.2    Durual, S.3
  • 43
    • 58149399349 scopus 로고    scopus 로고
    • Elevated growth differentiation factor 15 expression in patients with congenital dyserythropoietic anemia type I
    • Tamary H, Shalev H, Perez-Avraham G, et al. Elevated growth differentiation factor 15 expression in patients with congenital dyserythropoietic anemia type I. Blood. 2008;112(13):5241-5244.
    • (2008) Blood , vol.112 , Issue.13 , pp. 5241-5244
    • Tamary, H.1    Shalev, H.2    Perez-Avraham, G.3
  • 44
    • 77951494122 scopus 로고    scopus 로고
    • Growth differentiation factor 15 in erythroid health and disease
    • Tanno T, Noel P, Miller JL. Growth differentiation factor 15 in erythroid health and disease. Curr Opin Hematol. 2010;17(3):184-190.
    • (2010) Curr Opin Hematol , vol.17 , Issue.3 , pp. 184-190
    • Tanno, T.1    Noel, P.2    Miller, J.L.3
  • 45
    • 73349139547 scopus 로고    scopus 로고
    • Cell fate decisions are specified by the dynamic ERK interactome
    • von Kriegsheim A, Baiocchi D, Birtwistle M, et al. Cell fate decisions are specified by the dynamic ERK interactome. Nat Cell Biol. 2009;11(12):1458-1464.
    • (2009) Nat Cell Biol , vol.11 , Issue.12 , pp. 1458-1464
    • Von Kriegsheim, A.1    Baiocchi, D.2    Birtwistle, M.3
  • 47
    • 47049116150 scopus 로고    scopus 로고
    • Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPalpha
    • Pinto JP, Ribeiro S, Pontes H, et al. Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPalpha. Blood. 2008;111(12):5727-5733.
    • (2008) Blood , vol.111 , Issue.12 , pp. 5727-5733
    • Pinto, J.P.1    Ribeiro, S.2    Pontes, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.