메뉴 건너뛰기




Volumn 113, Issue 10, 2009, Pages 2136-2144

Chaperoning erythropoiesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLOBIN; CHAPERONE; GLOBIN; HEAT SHOCK PROTEIN 70; HEMOGLOBIN; MITOCHONDRIAL PROTEIN;

EID: 64049099283     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-09-115238     Document Type: Review
Times cited : (46)

References (146)
  • 1
    • 0021687085 scopus 로고
    • Cell-specific expression of heat shock proteins in chicken reticulocytes and lymphocytes
    • Morimoto R, Fodor E. Cell-specific expression of heat shock proteins in chicken reticulocytes and lymphocytes. J Cell Biol. 1984;99:1316-1323.
    • (1984) J Cell Biol , vol.99 , pp. 1316-1323
    • Morimoto, R.1    Fodor, E.2
  • 2
    • 0023446462 scopus 로고
    • Erythroid lineage-specific expression and inducibility of the major heat shock protein HSP70 during avian embryogenesis
    • Banerji SS, Laing K, Morimoto RI. Erythroid lineage-specific expression and inducibility of the major heat shock protein HSP70 during avian embryogenesis. Genes Dev. 1987;1:946-953.
    • (1987) Genes Dev , vol.1 , pp. 946-953
    • Banerji, S.S.1    Laing, K.2    Morimoto, R.I.3
  • 3
    • 0021685483 scopus 로고
    • Heat shock-induced translational control of HSP70 and globin synthesis in chicken reticulocytes
    • Banerji SS, Theodorakis NG, Morimoto RI. Heat shock-induced translational control of HSP70 and globin synthesis in chicken reticulocytes. Mol Cell Biol. 1984;4:2437-2448.
    • (1984) Mol Cell Biol , vol.4 , pp. 2437-2448
    • Banerji, S.S.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 4
    • 0023038425 scopus 로고
    • Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation
    • Davis JQ, Dansereau D, Johnstone RM, Bennett V. Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation. J Biol Chem. 1986;261: 15368-15371.
    • (1986) J Biol Chem , vol.261 , pp. 15368-15371
    • Davis, J.Q.1    Dansereau, D.2    Johnstone, R.M.3    Bennett, V.4
  • 5
    • 0021247706 scopus 로고
    • Accumulation of a heat shock like protein during differentiation of human eryhroid cell line K562
    • Singh MK, Yu J. Accumulation of a heat shock like protein during differentiation of human eryhroid cell line K562. Nature. 1984;309:631-633.
    • (1984) Nature , vol.309 , pp. 631-633
    • Singh, M.K.1    Yu, J.2
  • 6
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem. 2001;70:603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 7
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 2002;295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 8
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek K, Lewandowska A, Zietkiewicz S. Chaperones in control of protein disaggregation. EMBO J. 2008;27:328-335.
    • (2008) EMBO J , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 9
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil HR. Chaperone machines in action. Curr Opin Struct Biol. 2008;18:35-42.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 11
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanese V, Yam AY, Baughman J, Parnot C, Frydman J. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell. 2006;124:75-88.
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanese, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 12
    • 37349102454 scopus 로고    scopus 로고
    • Hsp104: A weapon to combat diverse neurodegenerative disorders
    • Shorter J. Hsp104: a weapon to combat diverse neurodegenerative disorders. Neurosignals. 2008;16:63-74.
    • (2008) Neurosignals , vol.16 , pp. 63-74
    • Shorter, J.1
  • 13
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, et al. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol. 1999;19:4535-4545.
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3
  • 14
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y, Soda M, Hatakeyama S, et al. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell. 2002;10:55-67.
    • (2002) Mol Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3
  • 15
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • 2:1133-1138
    • Murata S, Minami Y, Minami M, ChibaT, Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2001; 2:1133-1138.
    • EMBO Rep. 2001
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 16
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff B, Chapple JP, van der Spuy J, Hohfeld J, Cheetham ME. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr Biol. 2005;15:1058-1064.
    • (2005) Curr Biol , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 17
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell. 2006;125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 18
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science. 1999;286:1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 19
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • Horwich A. Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. J Clin Invest. 2002;110:1221-1232.
    • (2002) J Clin Invest , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 20
    • 17344361902 scopus 로고    scopus 로고
    • Amissense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P, Caron A, Guicheney P, et al. Amissense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet. 1998;20:92-95.
    • (1998) Nat Genet , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3
  • 21
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • Clark JI, Muchowski PJ. Small heat-shock proteins and their potential role in human disease. Curr Opin Struct Biol. 2000;10:52-59.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 22
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci. 2005;6:11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 23
    • 0013974622 scopus 로고
    • Thalassemia: The consequences of unbalanced hemoglobin synthesis
    • Nathan DG, Gunn RB. Thalassemia: the consequences of unbalanced hemoglobin synthesis. Am J Med. 1966;41:815-830.
    • (1966) Am J Med , vol.41 , pp. 815-830
    • Nathan, D.G.1    Gunn, R.B.2
  • 24
    • 0036180342 scopus 로고    scopus 로고
    • Pathophysiology of thalassemia
    • Schrier SL. Pathophysiology of thalassemia. Curr Opin Hematol. 2002;9:123-126.
    • (2002) Curr Opin Hematol , vol.9 , pp. 123-126
    • Schrier, S.L.1
  • 25
    • 34547872322 scopus 로고    scopus 로고
    • The glucocorticoid responses are shaped by molecular chaperones
    • Grad I, Picard D. The glucocorticoid responses are shaped by molecular chaperones. Mol Cell Endocrinol. 2007;275:2-12.
    • (2007) Mol Cell Endocrinol , vol.275 , pp. 2-12
    • Grad, I.1    Picard, D.2
  • 27
    • 34250329955 scopus 로고    scopus 로고
    • Heat shock paradox and a new role of heat shock proteins and their receptors as anti-inflammation targets
    • Chen Y, Voegeli TS, Liu PP, Noble EG, Currie RW. Heat shock paradox and a new role of heat shock proteins and their receptors as anti-inflammation targets. Inflamm Allergy Drug Targets. 2007;6:91-100.
    • (2007) Inflamm Allergy Drug Targets , vol.6 , pp. 91-100
    • Chen, Y.1    Voegeli, T.S.2    Liu, P.P.3    Noble, E.G.4    Currie, R.W.5
  • 28
    • 16444378781 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: A crucial part of viral survival strategies
    • Mayer MP. Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev Physiol Biochem Pharmacol. 2005;153:1-46.
    • (2005) Rev Physiol Biochem Pharmacol , vol.153 , pp. 1-46
    • Mayer, M.P.1
  • 29
    • 33746330168 scopus 로고    scopus 로고
    • Hsp70 molecular chaperones: Emerging roles in human disease and identification of small molecule modulators
    • Brodsky JL, Chiosis G. Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem. 2006;6:1215-1225.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1215-1225
    • Brodsky, J.L.1    Chiosis, G.2
  • 30
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl LH, Prodromou C, Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 2008;410:439-453.
    • (2008) Biochem J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 31
    • 33645090922 scopus 로고    scopus 로고
    • Proteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum-infected erythrocytes
    • Nyalwidhe J, Lingelbach K. Proteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum-infected erythrocytes. Proteomics. 2006;6: 1563-1573.
    • (2006) Proteomics , vol.6 , pp. 1563-1573
    • Nyalwidhe, J.1    Lingelbach, K.2
  • 32
    • 34548232285 scopus 로고    scopus 로고
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host
    • Botha M, Pesce ER, Blatch GL. The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. Int J Biochem Cell Biol. 2007;39:1781-1803.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1781-1803
    • Botha, M.1    Pesce, E.R.2    Blatch, G.L.3
  • 33
    • 34247513586 scopus 로고    scopus 로고
    • Chaperoning acellular upheaval in malaria: Heat shock proteins in Plasmodium falciparum
    • Acharya P, Kumar R,Tatu U. Chaperoning acellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol Biochem Parasitol. 2007;153:85-94.
    • (2007) Mol Biochem Parasitol , vol.153 , pp. 85-94
    • Acharya, P.1    Kumar, R.2    Tatu, U.3
  • 34
    • 8744228200 scopus 로고    scopus 로고
    • Recurrent fever promotes Plasmodium falciparum development in human erythrocytes
    • Pavithra SR, Banumathy G, Joy O, Singh V, Tatu U. Recurrent fever promotes Plasmodium falciparum development in human erythrocytes. J Biol Chem. 2004;279:46692-46699.
    • (2004) J Biol Chem , vol.279 , pp. 46692-46699
    • Pavithra, S.R.1    Banumathy, G.2    Joy, O.3    Singh, V.4    Tatu, U.5
  • 35
    • 3042541530 scopus 로고    scopus 로고
    • The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin
    • Kumar R, Musiyenko A, Barik S. The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin. Malar J. 2003;2:30.
    • (2003) Malar J , vol.2 , pp. 30
    • Kumar, R.1    Musiyenko, A.2    Barik, S.3
  • 36
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • Banumathy G, Singh V, Pavithra SR, Tatu U. Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem. 2003;278:18336-18345.
    • (2003) J Biol Chem , vol.278 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 37
    • 39049136491 scopus 로고    scopus 로고
    • Diamond Blackfan anemia: A disorder of red blood cell development
    • Ellis SR, Lipton JM. Diamond Blackfan anemia: a disorder of red blood cell development. Curr Top Dev Biol. 2008;82:217-241.
    • (2008) Curr Top Dev Biol , vol.82 , pp. 217-241
    • Ellis, S.R.1    Lipton, J.M.2
  • 38
    • 33845637791 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis
    • Lui JC, Kong SK. Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis. FEBS Lett. 2007;581:109-117.
    • (2007) FEBS Lett , vol.581 , pp. 109-117
    • Lui, J.C.1    Kong, S.K.2
  • 39
    • 2542475112 scopus 로고    scopus 로고
    • Caspase-3 has a nonapoptotic function in erythroid maturation
    • Carlile GW, Smith DH, Wiedmann M. Caspase-3 has a nonapoptotic function in erythroid maturation. Blood. 2004;103:4310-4316.
    • (2004) Blood , vol.103 , pp. 4310-4316
    • Carlile, G.W.1    Smith, D.H.2    Wiedmann, M.3
  • 40
    • 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;193:247-254.
    • (2001) J Exp Med , vol.193 , pp. 247-254
    • Zermati, Y.1    Garrido, C.2    Amsellem, S.3
  • 41
    • 0037131970 scopus 로고    scopus 로고
    • Raf-1 antagonizes erythroid differentiation by restraining caspase activation
    • Kolbus A, Pilat S, Husak Z, et al. Raf-1 antagonizes erythroid differentiation by restraining caspase activation. J Exp Med. 2002;196:1347-1353.
    • (2002) J Exp Med , vol.196 , pp. 1347-1353
    • Kolbus, A.1    Pilat, S.2    Husak, Z.3
  • 42
    • 0032950951 scopus 로고    scopus 로고
    • Apoptotic role of Fas/Fas ligand system in the regulation of erythropoiesis
    • De Maria R, Testa U, Luchetti L, et al. Apoptotic role of Fas/Fas ligand system in the regulation of erythropoiesis. Blood. 1999;93:796-803.
    • (1999) Blood , vol.93 , pp. 796-803
    • De Maria, R.1    Testa, U.2    Luchetti, L.3
  • 43
    • 0033619265 scopus 로고    scopus 로고
    • Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1 [see comments]
    • De Maria R, Zeuner A, Eramo A, et al. Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1 [see comments]. Nature. 1999;401:489-493.
    • (1999) Nature , vol.401 , pp. 489-493
    • De Maria, R.1    Zeuner, A.2    Eramo, A.3
  • 44
    • 0023784657 scopus 로고
    • Maintenance by erythropoietin of viability and maturation of murine erythroid precursor cells
    • Koury MJ, Bondurant MC. Maintenance by erythropoietin of viability and maturation of murine erythroid precursor cells. J Cell Physiol. 1988;137: 65-74.
    • (1988) J Cell Physiol , vol.137 , pp. 65-74
    • Koury, M.J.1    Bondurant, M.C.2
  • 45
    • 33846087085 scopus 로고    scopus 로고
    • Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1
    • Ribeil JA, Zermati Y, Vandekerckhove J, et al. Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature. 2007;445:102-105.
    • (2007) Nature , vol.445 , pp. 102-105
    • Ribeil, J.A.1    Zermati, Y.2    Vandekerckhove, J.3
  • 46
    • 0036479012 scopus 로고    scopus 로고
    • Apoptosis inducing factor (AIF): A novel caspase-indepen-dent death effector released from mitochondria
    • Cande C, Cohen I, Daugas E, et al. Apoptosis inducing factor (AIF): a novel caspase-indepen-dent death effector released from mitochondria. Biochimie. 2002;84:215-222.
    • (2002) Biochimie , vol.84 , pp. 215-222
    • Cande, C.1    Cohen, I.2    Daugas, E.3
  • 48
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor
    • Gurbuxani S, Schmitt E, Cande C, et al. Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor. Oncogene. 2003;22:6669-6678.
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3
  • 49
    • 21344458358 scopus 로고    scopus 로고
    • Hsp70 overexpression sequesters AIF and reduces neonatal hypoxic/ischemic brain injury
    • Matsumori Y, Hong SM, Aoyama K, et al. Hsp70 overexpression sequesters AIF and reduces neonatal hypoxic/ischemic brain injury. J Cereb Blood Flow Metab. 2005;25:899-910.
    • (2005) J Cereb Blood Flow Metab , vol.25 , pp. 899-910
    • Matsumori, Y.1    Hong, S.M.2    Aoyama, K.3
  • 50
    • 17944366977 scopus 로고    scopus 로고
    • Heat shock protein 70 antagonizes apoptosis-inducing factor
    • Ravagnan L, Gurbuxani S, Susin SA, et al. Heat shock protein 70 antagonizes apoptosis-inducing factor. Nat Cell Biol. 2001;3:839-843.
    • (2001) Nat Cell Biol , vol.3 , pp. 839-843
    • Ravagnan, L.1    Gurbuxani, S.2    Susin, S.A.3
  • 51
    • 18244401639 scopus 로고    scopus 로고
    • Loss of Hspa9b in zebrafish recapitulates the ineffective hematopoiesis of the myelodysplastic syndrome
    • Craven SE, French D, Ye W, de Sauvage F, Rosenthal A. Loss of Hspa9b in zebrafish recapitulates the ineffective hematopoiesis of the myelodysplastic syndrome. Blood. 2005;105:3528-3534.
    • (2005) Blood , vol.105 , pp. 3528-3534
    • Craven, S.E.1    French, D.2    Ye, W.3    de Sauvage, F.4    Rosenthal, A.5
  • 52
    • 0033612301 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
    • Voisine C, Craig EA, Zufall N, von Ahsen O, Pfanner N, Voos W. The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70. Cell. 1999;97:565-574.
    • (1999) Cell , vol.97 , pp. 565-574
    • Voisine, C.1    Craig, E.A.2    Zufall, N.3    von Ahsen, O.4    Pfanner, N.5    Voos, W.6
  • 53
    • 0024309756 scopus 로고
    • SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein
    • Craig EA, Kramer J, Shilling J, et al. SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein. Mol Cell Biol. 1989;9:3000-3008.
    • (1989) Mol Cell Biol , vol.9 , pp. 3000-3008
    • Craig, E.A.1    Kramer, J.2    Shilling, J.3
  • 54
    • 0037051942 scopus 로고    scopus 로고
    • Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75
    • Yokoyama K, Fukumoto K, Murakami T, et al. Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75. FEBS Lett. 2002;516:53-57.
    • (2002) FEBS Lett , vol.516 , pp. 53-57
    • Yokoyama, K.1    Fukumoto, K.2    Murakami, T.3
  • 55
    • 0037447901 scopus 로고    scopus 로고
    • Overexpressed mortalin (mot-2)/mthsp70/ GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts
    • Kaul SC, Yaguchi T, Taira K, Reddel RR, Wadhwa R. Overexpressed mortalin (mot-2)/mthsp70/ GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts. Exp Cell Res. 2003;286:96-101.
    • (2003) Exp Cell Res , vol.286 , pp. 96-101
    • Kaul, S.C.1    Yaguchi, T.2    Taira, K.3    Reddel, R.R.4    Wadhwa, R.5
  • 56
    • 34447307977 scopus 로고    scopus 로고
    • Mortalin is a novel mediator of erythropoietin signaling
    • Ohtsuka R, Abe Y, Fujii T, et al. Mortalin is a novel mediator of erythropoietin signaling. Eur J Haematol. 2007;79:114-125.
    • (2007) Eur J Haematol , vol.79 , pp. 114-125
    • Ohtsuka, R.1    Abe, Y.2    Fujii, T.3
  • 57
    • 0028618296 scopus 로고
    • Protein folding and the regulation of signaling pathways
    • Rutherford SL, Zuker CS. Protein folding and the regulation of signaling pathways. Cell. 1994;79: 1129-1132.
    • (1994) Cell , vol.79 , pp. 1129-1132
    • Rutherford, S.L.1    Zuker, C.S.2
  • 58
    • 12344291243 scopus 로고    scopus 로고
    • Pearl LH. Hsp90 and Cdc37: a chaperone cancer conspiracy. Curr Opin Genet Dev. 2005;15:55-61.
    • Pearl LH. Hsp90 and Cdc37: a chaperone cancer conspiracy. Curr Opin Genet Dev. 2005;15:55-61.
  • 59
    • 41949095010 scopus 로고    scopus 로고
    • Higgs DR, Wood WG. Long-range regulation of alpha globin gene expression during erythropoiesis. CurrOpin Hematol. 2008;15:176-183.
    • Higgs DR, Wood WG. Long-range regulation of alpha globin gene expression during erythropoiesis. CurrOpin Hematol. 2008;15:176-183.
  • 60
    • 13844318521 scopus 로고    scopus 로고
    • Control of globin gene expression during development and erythroid differentiation
    • Stamatoyannopoulos G. Control of globin gene expression during development and erythroid differentiation. Exp Hematol. 2005;33:259-271.
    • (2005) Exp Hematol , vol.33 , pp. 259-271
    • Stamatoyannopoulos, G.1
  • 61
    • 52049089667 scopus 로고    scopus 로고
    • Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source
    • Graves PE, Henderson DP, Horstman MJ, Solomon BJ, Olson JS. Enhancing stability and expression of recombinant human hemoglobin in E. coli: progress in the development of a recombinant HBOC source. Biochim Biophys Acta. 2008; 1784:1471-1479.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1471-1479
    • Graves, P.E.1    Henderson, D.P.2    Horstman, M.J.3    Solomon, B.J.4    Olson, J.S.5
  • 62
    • 0015524053 scopus 로고
    • Influence of prosthetic groups on protein folding and subunit assembly, I: Conformational differences between separated human alpha-and beta-globins
    • Yip YK, Waks M, Beychok S. Influence of prosthetic groups on protein folding and subunit assembly, I: conformational differences between separated human alpha-and beta-globins. J Biol Chem. 1972;247:7237-7244.
    • (1972) J Biol Chem , vol.247 , pp. 7237-7244
    • Yip, Y.K.1    Waks, M.2    Beychok, S.3
  • 63
    • 0035996770 scopus 로고    scopus 로고
    • Ordered heme binding ensures the assembly of fully functional hemoglobin: A hypothesis
    • Vasudevan G, McDonald MJ. Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis. Curr Protein Pept Sci. 2002;3:461-466.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 461-466
    • Vasudevan, G.1    McDonald, M.J.2
  • 64
    • 0019763671 scopus 로고
    • Preparation and properties of apohemoglobin and reconstituted hemoglobins
    • Ascoli F, Fanelli MR, Antonini E. Preparation and properties of apohemoglobin and reconstituted hemoglobins. Methods Enzymol. 1981;76:72-87.
    • (1981) Methods Enzymol , vol.76 , pp. 72-87
    • Ascoli, F.1    Fanelli, M.R.2    Antonini, E.3
  • 66
    • 0027942887 scopus 로고
    • Monitoring the effect of subunit assembly on the structural flexibility of human alpha apohemoglobin by steady-state fluorescence
    • O'Malley SM, McDonald MJ. Monitoring the effect of subunit assembly on the structural flexibility of human alpha apohemoglobin by steady-state fluorescence. J Protein Chem. 1994;13:561-567.
    • (1994) J Protein Chem , vol.13 , pp. 561-567
    • O'Malley, S.M.1    McDonald, M.J.2
  • 67
    • 0015818065 scopus 로고
    • Influence of prosthetic groups on protein folding and subunit assembly: Recombination of separated human alpha-and beta-globin chains with heme and alloplex interactions of globin chains with heme containing subunits
    • Waks M, Yip YK, Beychok S. Influence of prosthetic groups on protein folding and subunit assembly: recombination of separated human alpha-and beta-globin chains with heme and alloplex interactions of globin chains with heme containing subunits. J Biol Chem. 1973;248: 6462-6470.
    • (1973) J Biol Chem , vol.248 , pp. 6462-6470
    • Waks, M.1    Yip, Y.K.2    Beychok, S.3
  • 68
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove MS, Olson JS. The stability of holomyoglobin is determined by heme affinity. Biochemistry. 1996;35:11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 71
    • 1242317026 scopus 로고    scopus 로고
    • Heme positively regulates the expression of b-globin at the locus control region via the transcriptional factor Bach1 in erythroid cells
    • Tahara T, Sun J, Nakanishi K, et al. Heme positively regulates the expression of b-globin at the locus control region via the transcriptional factor Bach1 in erythroid cells. J Biol Chem. 2004;279: 5480-5487.
    • (2004) J Biol Chem , vol.279 , pp. 5480-5487
    • Tahara, T.1    Sun, J.2    Nakanishi, K.3
  • 72
    • 4744356825 scopus 로고    scopus 로고
    • Heme dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells
    • Tahara T, Sun J, Igarashi K, Taketani S. Heme dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells. Biochem Biophys Res Commun. 2004;324:77-85.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 77-85
    • Tahara, T.1    Sun, J.2    Igarashi, K.3    Taketani, S.4
  • 73
    • 1242319573 scopus 로고    scopus 로고
    • Heme regulates the dynamic exchange of Bach1 and NF-E2-related factors in the Maf transcription factor network
    • Sun J, Brand M, Zenke Y, Tashiro S, Groudine M, Igarashi K. Heme regulates the dynamic exchange of Bach1 and NF-E2-related factors in the Maf transcription factor network. Proc Natl Acad Sci USA. 2004;101:1461-1466.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1461-1466
    • Sun, J.1    Brand, M.2    Zenke, Y.3    Tashiro, S.4    Groudine, M.5    Igarashi, K.6
  • 74
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: Relevance to anemias
    • Chen JJ. Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias. Blood. 2007;109:2693-2699.
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 75
    • 17944362905 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency
    • Han AP, Yu C, Lu L, et al. Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. EMBO J. 2001;20:6909-6918.
    • (2001) EMBO J , vol.20 , pp. 6909-6918
    • Han, A.P.1    Yu, C.2    Lu, L.3
  • 76
    • 20444464807 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyriaand beta-thalassemia
    • Han AP, Fleming MD, Chen JJ. Heme-regulated eIF2alpha kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyriaand beta-thalassemia. J Clin Invest. 2005; 115:1562-1570.
    • (2005) J Clin Invest , vol.115 , pp. 1562-1570
    • Han, A.P.1    Fleming, M.D.2    Chen, J.J.3
  • 77
    • 51249094266 scopus 로고    scopus 로고
    • Haem-regulated eIF2alpha kinase is necessary for adaptive gene expression in erythroid precursors under the stress of iron deficiency
    • Liu S, Bhattacharya S, Han A, et al. Haem-regulated eIF2alpha kinase is necessary for adaptive gene expression in erythroid precursors under the stress of iron deficiency. Br J Haematol. 2008; 143:129-137.
    • (2008) Br J Haematol , vol.143 , pp. 129-137
    • Liu, S.1    Bhattacharya, S.2    Han, A.3
  • 78
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • Lu L, Han AP, Chen JJ. Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses. Mol Cell Biol. 2001;21:7971-7980.
    • (2001) Mol Cell Biol , vol.21 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 79
    • 0242318392 scopus 로고    scopus 로고
    • High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients
    • Scroggins BT, Prince T, Shao J, et al. High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients. Biochemistry. 2003;42:12550-12561.
    • (2003) Biochemistry , vol.42 , pp. 12550-12561
    • Scroggins, B.T.1    Prince, T.2    Shao, J.3
  • 81
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase
    • Shao J, Grammatikakis N, Scroggins BT, et al. Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase. J Biol Chem. 2001;276:206-214.
    • (2001) J Biol Chem , vol.276 , pp. 206-214
    • Shao, J.1    Grammatikakis, N.2    Scroggins, B.T.3
  • 82
    • 0032766645 scopus 로고    scopus 로고
    • Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2
    • Uma S, Thulasiraman V, Matts RL. Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol. 1999;19:5861-5871.
    • (1999) Mol Cell Biol , vol.19 , pp. 5861-5871
    • Uma, S.1    Thulasiraman, V.2    Matts, R.L.3
  • 83
    • 0032146164 scopus 로고    scopus 로고
    • Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF2alpha kinase in rabbit reticulocyte lysate
    • Thulasiraman V, Xu Z, Uma S, Gu Y, Chen JJ, Matts RL. Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF2alpha kinase in rabbit reticulocyte lysate. Eur J Biochem. 1998;255:552-562.
    • (1998) Eur J Biochem , vol.255 , pp. 552-562
    • Thulasiraman, V.1    Xu, Z.2    Uma, S.3    Gu, Y.4    Chen, J.J.5    Matts, R.L.6
  • 84
    • 0031009879 scopus 로고    scopus 로고
    • The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress
    • Xu Z, Pal JK, Thulasiraman V, Hahn HP, Chen JJ, Matts RL. The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress. Eur J Biochem. 1997; 246:461-470.
    • (1997) Eur J Biochem , vol.246 , pp. 461-470
    • Xu, Z.1    Pal, J.K.2    Thulasiraman, V.3    Hahn, H.P.4    Chen, J.J.5    Matts, R.L.6
  • 85
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation
    • Uma S, Hartson SD, Chen JJ, Matts RL. Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation. J Biol Chem. 1997;272:11648-11656.
    • (1997) J Biol Chem , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.D.2    Chen, J.J.3    Matts, R.L.4
  • 86
    • 0002794530 scopus 로고
    • Hemoglobin synthesis and the thalassemias
    • Handin RI, Lux SE, Stossel TP, eds, Philadelphia, PA: J. B. Lippincott Company;
    • Forget BG, Pearson HA. Hemoglobin synthesis and the thalassemias. In: Handin RI, Lux SE, Stossel TP, eds. BLOOD Principles & Practice of Hematology. Philadelphia, PA: J. B. Lippincott Company; 1995:1525-1990.
    • (1995) BLOOD Principles & Practice of Hematology , pp. 1525-1990
    • Forget, B.G.1    Pearson, H.A.2
  • 87
    • 0016660866 scopus 로고
    • Formation of superoxide in the autoxidation of the isolated alpha and beta chains of human hemoglobin and its involvement in hemichrome precipitation
    • Brunori M, Falcino G, Fioreti E. Formation of superoxide in the autoxidation of the isolated alpha and beta chains of human hemoglobin and its involvement in hemichrome precipitation. Eur Biochem. 1975;53:99-104.
    • (1975) Eur Biochem , vol.53 , pp. 99-104
    • Brunori, M.1    Falcino, G.2    Fioreti, E.3
  • 89
    • 0014214766 scopus 로고
    • Evidence for soluble alpha-chains as intermediates in hemoglobin synthesis in the rabbit reticulocyte
    • Shaeffer JR. Evidence for soluble alpha-chains as intermediates in hemoglobin synthesis in the rabbit reticulocyte. Biochem Biophys Res Comm. 1967;28:647-652.
    • (1967) Biochem Biophys Res Comm , vol.28 , pp. 647-652
    • Shaeffer, J.R.1
  • 91
    • 12344326653 scopus 로고    scopus 로고
    • Clinical aspects of beta thalassemia
    • Steinberg MH, Forget BG, Higgs DR, Nagel RL, eds, Cambridge, United Kingdom: Cambridge University Press;
    • Olivieri NF, Weatherall DJ. Clinical aspects of beta thalassemia. In: Steinberg MH, Forget BG, Higgs DR, Nagel RL, eds. Disorders of Hemoglobin. Cambridge, United Kingdom: Cambridge University Press; 2001:277-341.
    • (2001) Disorders of Hemoglobin , pp. 277-341
    • Olivieri, N.F.1    Weatherall, D.J.2
  • 92
    • 0021064993 scopus 로고
    • Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent
    • Shaeffer JR. Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent. J Biol Chem. 1983;258:13172-13177.
    • (1983) J Biol Chem , vol.258 , pp. 13172-13177
    • Shaeffer, J.R.1
  • 93
    • 0031849189 scopus 로고    scopus 로고
    • Enhancement by ubiquitin aldehyde of proteolysis of hemoglobin alpha subunits in beta-thalassemic hemolysates
    • Shaeffer JR, Cohen RE. Enhancement by ubiquitin aldehyde of proteolysis of hemoglobin alpha subunits in beta-thalassemic hemolysates. Ann N Y Acad Sci. 1998;850:394-397.
    • (1998) Ann N Y Acad Sci , vol.850 , pp. 394-397
    • Shaeffer, J.R.1    Cohen, R.E.2
  • 94
    • 0028988055 scopus 로고
    • Degradation of monoubiquitinated alpha-globin by 26S proteasomes
    • Shaeffer JR, Kania MA. Degradation of monoubiquitinated alpha-globin by 26S proteasomes. Biochemistry. 1995;34:4015-4021.
    • (1995) Biochemistry , vol.34 , pp. 4015-4021
    • Shaeffer, J.R.1    Kania, M.A.2
  • 95
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature. 2008;454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 96
    • 33644968962 scopus 로고    scopus 로고
    • High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone
    • Vasseur-Godbillon C, Hamdane D, Marden MC, Baudin-Creuza V. High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone. Protein Eng Des Sel. 2006;19:91-97.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 91-97
    • Vasseur-Godbillon, C.1    Hamdane, D.2    Marden, M.C.3    Baudin-Creuza, V.4
  • 97
    • 0037071860 scopus 로고    scopus 로고
    • An abundant erythroid protein that stabilizes free alpha hemoglobin
    • Kihm AJ, Kong Y, Hong W, et al. An abundant erythroid protein that stabilizes free alpha hemoglobin. Nature. 2002;417:758-763.
    • (2002) Nature , vol.417 , pp. 758-763
    • Kihm, A.J.1    Kong, Y.2    Hong, W.3
  • 98
    • 85047690518 scopus 로고    scopus 로고
    • Loss of alphahemoglobin-stabilizing protein impairs erythropoiesis and exacerbates beta-thalassemia
    • Kong Y, Zhou S, Kihm AJ, et al. Loss of alphahemoglobin-stabilizing protein impairs erythropoiesis and exacerbates beta-thalassemia. J Clin Invest. 2004;114:1457-1466.
    • (2004) J Clin Invest , vol.114 , pp. 1457-1466
    • Kong, Y.1    Zhou, S.2    Kihm, A.J.3
  • 99
    • 39149123488 scopus 로고    scopus 로고
    • Reduction of AHSP synthesis in hemininduced K562 cells and EPO-induced CD34(+) cells leads to alpha-globin precipitation, impairment of normal hemoglobin production, and increased cell death
    • Pinho FO, de Albuquerque DM, Olalla Saad ST, Costa FF. Reduction of AHSP synthesis in hemininduced K562 cells and EPO-induced CD34(+) cells leads to alpha-globin precipitation, impairment of normal hemoglobin production, and increased cell death. Exp Hematol. 2008;36:265-272.
    • (2008) Exp Hematol , vol.36 , pp. 265-272
    • Pinho, F.O.1    de Albuquerque, D.M.2    Olalla Saad, S.T.3    Costa, F.F.4
  • 100
    • 0037175053 scopus 로고    scopus 로고
    • Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein
    • Gell D, Kong Y, Eaton SA, Weiss MJ, Mackay JP. Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein. J Biol Chem. 2002;277:40602-40609.
    • (2002) J Biol Chem , vol.277 , pp. 40602-40609
    • Gell, D.1    Kong, Y.2    Eaton, S.A.3    Weiss, M.J.4    Mackay, J.P.5
  • 101
    • 4544359805 scopus 로고    scopus 로고
    • NMR structure of the alpha-hemoglobin stabilizing protein: Insights into conformational heterogeneity and binding
    • Santiveri CM, Perez-Canadillas JM, Vadivelu MK, et al. NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding. J Biol Chem. 2004;279: 34963-34970.
    • (2004) J Biol Chem , vol.279 , pp. 34963-34970
    • Santiveri, C.M.1    Perez-Canadillas, J.M.2    Vadivelu, M.K.3
  • 102
    • 20444445134 scopus 로고    scopus 로고
    • Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem
    • Feng L, Zhou S, Gu L, et al. Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem. Nature. 2005;435: 697-701.
    • (2005) Nature , vol.435 , pp. 697-701
    • Feng, L.1    Zhou, S.2    Gu, L.3
  • 103
    • 8844285199 scopus 로고    scopus 로고
    • Molecular mechanism of AHSP-mediated stabilization of alphahemoglobin
    • Feng L, Gell DA, Zhou S, et al. Molecular mechanism of AHSP-mediated stabilization of alphahemoglobin. Cell. 2004;119:629-640.
    • (2004) Cell , vol.119 , pp. 629-640
    • Feng, L.1    Gell, D.A.2    Zhou, S.3
  • 104
  • 105
    • 33845924644 scopus 로고    scopus 로고
    • Biochemical fates of alpha hemoglobin bound to alpha hemoglobin stabilizing protein (AHSP)
    • Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ. Biochemical fates of alpha hemoglobin bound to alpha hemoglobin stabilizing protein (AHSP).J Biol Chem. 2006;281:32611-32618.
    • (2006) J Biol Chem , vol.281 , pp. 32611-32618
    • Zhou, S.1    Olson, J.S.2    Fabian, M.3    Weiss, M.J.4    Gow, A.J.5
  • 106
    • 34447121854 scopus 로고    scopus 로고
    • An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesis
    • Yu X, Kong Y, Dore LC, et al. An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesis. J Clin Invest. 2007;117:1856-1865.
    • (2007) J Clin Invest , vol.117 , pp. 1856-1865
    • Yu, X.1    Kong, Y.2    Dore, L.C.3
  • 107
    • 55249087434 scopus 로고    scopus 로고
    • An iron responsive element-like stem-loop regulates alpha hemoglobin stabilizing protein mRNA
    • Dos Santos CO, Dore LC, Valentine E, et al. An iron responsive element-like stem-loop regulates alpha hemoglobin stabilizing protein mRNA. J Biol Chem. 2008;283:26956-26964.
    • (2008) J Biol Chem , vol.283 , pp. 26956-26964
    • Dos Santos, C.O.1    Dore, L.C.2    Valentine, E.3
  • 108
    • 29744437673 scopus 로고    scopus 로고
    • Role of alpha hemoglobin-stabilizing protein in normal erythropoiesis and (3-thalassemia
    • Weiss MJ, Zhou S, Feng L, et al. Role of alpha hemoglobin-stabilizing protein in normal erythropoiesis and (3-thalassemia. Ann N YAcad Sci. 2005;1054:103-117.
    • (2005) Ann N YAcad Sci , vol.1054 , pp. 103-117
    • Weiss, M.J.1    Zhou, S.2    Feng, L.3
  • 109
    • 0029164636 scopus 로고
    • Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo
    • Archer JE, Vega LR, Solomon F. Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo. Cell. 1995;82:425-434.
    • (1995) Cell , vol.82 , pp. 425-434
    • Archer, J.E.1    Vega, L.R.2    Solomon, F.3
  • 110
    • 0035715785 scopus 로고    scopus 로고
    • Type II chaperonins, prefoldin, and the tubulin-specific chaperones
    • Cowan NJ, Lewis SA. Type II chaperonins, prefoldin, and the tubulin-specific chaperones. Adv Protein Chem. 2001;59:73-104.
    • (2001) Adv Protein Chem , vol.59 , pp. 73-104
    • Cowan, N.J.1    Lewis, S.A.2
  • 111
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai N, Hosokawa M, Itohara S, et al. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol. 2000;150:1499-1506.
    • (2000) J Cell Biol , vol.150 , pp. 1499-1506
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3
  • 112
    • 0034657132 scopus 로고    scopus 로고
    • Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen
    • Tasab M, Batten MR, Bulleid NJ. Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen. EMBO J. 2000; 19:2204-2211.
    • (2000) EMBO J , vol.19 , pp. 2204-2211
    • Tasab, M.1    Batten, M.R.2    Bulleid, N.J.3
  • 113
    • 34248206669 scopus 로고    scopus 로고
    • The first case of Hb Groene Hart [alpha119(H2)Pro→Ser, CCT→TCT (alpha1)] homozygosity confirms that a thalassemia phenotype is associated with this abnormal hemoglobin variant
    • Giordano PC, Zweegman S, Akkermans N, et al. The first case of Hb Groene Hart [alpha119(H2)Pro→Ser, CCT→TCT (alpha1)] homozygosity confirms that a thalassemia phenotype is associated with this abnormal hemoglobin variant. Hemoglobin. 2007;31:179-182.
    • (2007) Hemoglobin , vol.31 , pp. 179-182
    • Giordano, P.C.1    Zweegman, S.2    Akkermans, N.3
  • 114
    • 38549144245 scopus 로고    scopus 로고
    • Hb Foggia or alpha 117 (GH5)Phe → Ser: A new alpha 2 globin allele affecting the alpha Hb-AHSP interaction
    • Lacerra G, Scarano C, Musollino G, Flagiello A, Pucci P, Carestia C. Hb Foggia or alpha 117 (GH5)Phe → Ser: a new alpha 2 globin allele affecting the alpha Hb-AHSP interaction. Haematologica. 2008;93:141-142.
    • (2008) Haematologica , vol.93 , pp. 141-142
    • Lacerra, G.1    Scarano, C.2    Musollino, G.3    Flagiello, A.4    Pucci, P.5    Carestia, C.6
  • 115
    • 33750908580 scopus 로고    scopus 로고
    • Impaired binding of AHSP to alpha chain variants: Hb Groene Hart illustrates a mechanism leading to unstable hemoglobins with alpha thalassemic like syndrome
    • Vasseur-Godbillon C, Marden MC, Giordano P, Wajcman H, Baudin-Creuza V. Impaired binding of AHSP to alpha chain variants: Hb Groene Hart illustrates a mechanism leading to unstable hemoglobins with alpha thalassemic like syndrome. Blood Cells Mol Dis. 2006;37:173-179.
    • (2006) Blood Cells Mol Dis , vol.37 , pp. 173-179
    • Vasseur-Godbillon, C.1    Marden, M.C.2    Giordano, P.3    Wajcman, H.4    Baudin-Creuza, V.5
  • 116
    • 38349170152 scopus 로고    scopus 로고
    • Population analysis of the alpha hemoglobin stabilizing protein (AHSP) gene identifies sequence variants that alter expression and function
    • dos Santos CO, Zhou S, Secolin R, et al. Population analysis of the alpha hemoglobin stabilizing protein (AHSP) gene identifies sequence variants that alter expression and function. Am J Hematol. 2008;83:103-108.
    • (2008) Am J Hematol , vol.83 , pp. 103-108
    • dos Santos, C.O.1    Zhou, S.2    Secolin, R.3
  • 117
    • 1942425504 scopus 로고    scopus 로고
    • Evaluation of alpha hemoglobin stabilizing protein (AHSP) as a genetic modifier in patients with beta thalassemia
    • Viprakasit V, Tanphaichitr VS, Chinchang W, Sangkla P, Weiss MJ, Higgs DR. Evaluation of alpha hemoglobin stabilizing protein (AHSP) as a genetic modifier in patients with beta thalassemia. Blood. 2004;103:3296-3299.
    • (2004) Blood , vol.103 , pp. 3296-3299
    • Viprakasit, V.1    Tanphaichitr, V.S.2    Chinchang, W.3    Sangkla, P.4    Weiss, M.J.5    Higgs, D.R.6
  • 118
    • 0344735769 scopus 로고    scopus 로고
    • Transcript level of erythroid differentiation-related factor, a candidate surrogate marker for transmissible spongiform encephalopathy diseases in blood, shows a broad range of variation in healthy individuals
    • Glock B, Winter M, Rennhofer SO, et al. Transcript level of erythroid differentiation-related factor, a candidate surrogate marker for transmissible spongiform encephalopathy diseases in blood, shows a broad range of variation in healthy individuals. Transfusion. 2003;43:1706-1710.
    • (2003) Transfusion , vol.43 , pp. 1706-1710
    • Glock, B.1    Winter, M.2    Rennhofer, S.O.3
  • 119
    • 33646689318 scopus 로고    scopus 로고
    • Alpha-haemoglobin stabilising protein is a quantitative trait gene that modifies the phenotype of beta-thalassaemia
    • Lai MI, Jiang J, Silver N, et al. Alpha-haemoglobin stabilising protein is a quantitative trait gene that modifies the phenotype of beta-thalassaemia. Br J Haematol. 2006;133:675-682.
    • (2006) Br J Haematol , vol.133 , pp. 675-682
    • Lai, M.I.1    Jiang, J.2    Silver, N.3
  • 120
    • 35548933854 scopus 로고    scopus 로고
    • Identification of two new synthetic histone deacetylase inhibitors that modulate globin gene expression in erythroid cells from healthy donors and patients with thalassemia
    • Mai A, Jelicic K, Rotili D, et al. Identification of two new synthetic histone deacetylase inhibitors that modulate globin gene expression in erythroid cells from healthy donors and patients with thalassemia. Mol Pharmacol. 2007;72:1111-1123.
    • (2007) Mol Pharmacol , vol.72 , pp. 1111-1123
    • Mai, A.1    Jelicic, K.2    Rotili, D.3
  • 121
    • 28244472034 scopus 로고    scopus 로고
    • GATA-1 and Oct-1 are required for expression of the human alpha-hemoglobin-stabilizing protein gene
    • Gallagher PG, Liem RI, Wong E, Weiss MJ, Bodine DM. GATA-1 and Oct-1 are required for expression of the human alpha-hemoglobin-stabilizing protein gene. J Biol Chem. 2005;280: 39016-39023.
    • (2005) J Biol Chem , vol.280 , pp. 39016-39023
    • Gallagher, P.G.1    Liem, R.I.2    Wong, E.3    Weiss, M.J.4    Bodine, D.M.5
  • 122
    • 33646678018 scopus 로고    scopus 로고
    • Alpha hemoglobin stabilizing protein (AHSP) is a susceptibility gene to drug/infection-induced hemolytic anemia [abstract]
    • Kanno H, Kamatani N, HamadaT, et al. Alpha hemoglobin stabilizing protein (AHSP) is a susceptibility gene to drug/infection-induced hemolytic anemia [abstract]. Blood. 2005;106:479a.
    • (2005) Blood , vol.106
    • Kanno, H.1    Kamatani, N.2    HamadaT3
  • 123
    • 67349206474 scopus 로고    scopus 로고
    • Alpha-hemoglobin-stabilizing protein (AHSP) in hemolysis, elevated liver enzyme, and low platelet (HELLP) syndrome, intrauterine growth restriction (IUGR) and fetal death
    • Emanuelli M, Sartini D, Rossi V, et al. Alpha-hemoglobin-stabilizing protein (AHSP) in hemolysis, elevated liver enzyme, and low platelet (HELLP) syndrome, intrauterine growth restriction (IUGR) and fetal death. Cell Stress Chaperones. 2008; 13:67-71.
    • (2008) Cell Stress Chaperones , vol.13 , pp. 67-71
    • Emanuelli, M.1    Sartini, D.2    Rossi, V.3
  • 124
    • 1942432701 scopus 로고    scopus 로고
    • AHSP expression in beta-thalassemia carriers with thalassemia intermedia phenotype [abstract]
    • Galanello R, Perseu L, Giagu N, Sole G. AHSP expression in beta-thalassemia carriers with thalassemia intermedia phenotype [abstract]. Blood. 2003;102:1881.
    • (2003) Blood , vol.102 , pp. 1881
    • Galanello, R.1    Perseu, L.2    Giagu, N.3    Sole, G.4
  • 125
    • 29144434072 scopus 로고    scopus 로고
    • Expression of alpha hemoglobin stabilizing protein gene (AHSP) during erythropoiesis and beta thalassemia [abstract]
    • dos Santos CO, Duarte AS, Saad ST, Costa FF. Expression of alpha hemoglobin stabilizing protein gene (AHSP) during erythropoiesis and beta thalassemia [abstract]. Blood. 2003;102:3837a.
    • (2003) Blood , vol.102
    • dos Santos, C.O.1    Duarte, A.S.2    Saad, S.T.3    Costa, F.F.4
  • 126
    • 24644467815 scopus 로고    scopus 로고
    • AHSP and beta-thalassemia: A possible genetic modifier
    • dos Santos CO, Costa FF. AHSP and beta-thalassemia: a possible genetic modifier. Hematology. 2005;10:157-161.
    • (2005) Hematology , vol.10 , pp. 157-161
    • dos Santos, C.O.1    Costa, F.F.2
  • 127
    • 0029065710 scopus 로고
    • Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation
    • Wefes I, Mastrandrea LD, Haldeman M, et al. Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation. Proc Natl Acad Sci U S A. 1995;92:4982-4986.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4982-4986
    • Wefes, I.1    Mastrandrea, L.D.2    Haldeman, M.3
  • 128
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice JF. Chaperone-mediated autophagy. Autophagy. 2007;3:295-299.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 129
    • 41449115693 scopus 로고    scopus 로고
    • NIX induces mitochondrial autophagy in reticulocytes
    • Zhang J, Ney PA. NIX induces mitochondrial autophagy in reticulocytes. Autophagy. 2008;4:354-356.
    • (2008) Autophagy , vol.4 , pp. 354-356
    • Zhang, J.1    Ney, P.A.2
  • 130
    • 37649017266 scopus 로고    scopus 로고
    • NIX is required for programmed mitochondrial clearance during reticulocyte maturation
    • Schweers RL, Zhang J, Randall MS, et al. NIX is required for programmed mitochondrial clearance during reticulocyte maturation. Proc Natl Acad Sci U S A. 2007;104:19500-19505.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19500-19505
    • Schweers, R.L.1    Zhang, J.2    Randall, M.S.3
  • 131
    • 47049100413 scopus 로고    scopus 로고
    • Essential role for Nix in autophagic maturation of erythroid cells
    • Sandoval H, Thiagarajan P, Dasgupta SK, et al. Essential role for Nix in autophagic maturation of erythroid cells. Nature. 2008;454:232-235.
    • (2008) Nature , vol.454 , pp. 232-235
    • Sandoval, H.1    Thiagarajan, P.2    Dasgupta, S.K.3
  • 132
    • 0141989227 scopus 로고    scopus 로고
    • Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2
    • Yamanaka K, Ishikawa H, Megumi Y, et al. Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2. Nat Cell Biol. 2003;5:336-340.
    • (2003) Nat Cell Biol , vol.5 , pp. 336-340
    • Yamanaka, K.1    Ishikawa, H.2    Megumi, Y.3
  • 133
    • 22544452148 scopus 로고    scopus 로고
    • Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2
    • Ishikawa H, Kato M, Hori H, et al. Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Mol Cell. 2005; 19:171-181.
    • (2005) Mol Cell , vol.19 , pp. 171-181
    • Ishikawa, H.1    Kato, M.2    Hori, H.3
  • 134
    • 38349019916 scopus 로고    scopus 로고
    • HOIL-1 is not required for iron-mediated IRP2 degradation in HEK293 cells
    • Zumbrennen KB, Hanson ES, Leibold EA. HOIL-1 is not required for iron-mediated IRP2 degradation in HEK293 cells. Biochim Biophys Acta. 2008;1783:246-252.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 246-252
    • Zumbrennen, K.B.1    Hanson, E.S.2    Leibold, E.A.3
  • 135
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 2008;22:1427-1438.
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 136
  • 137
    • 51349093260 scopus 로고    scopus 로고
    • Pharmacological induction of the heat shock response improves myelination in a neuropathic model
    • Rangaraju S, Madorsky I, Pileggi JG, Kamal A, Notterpek L. Pharmacological induction of the heat shock response improves myelination in a neuropathic model. Neurobiol Dis. 2008;32:105-115.
    • (2008) Neurobiol Dis , vol.32 , pp. 105-115
    • Rangaraju, S.1    Madorsky, I.2    Pileggi, J.G.3    Kamal, A.4    Notterpek, L.5
  • 138
    • 33749176269 scopus 로고    scopus 로고
    • Cytosolic chaperonin prevents polyglutamine toxicitywith altering the aggregation state
    • KitamuraA, Kubota H, Pack CG, et al. Cytosolic chaperonin prevents polyglutamine toxicitywith altering the aggregation state. Nat Cell Biol. 2006;8:1163-1170.
    • (2006) Nat Cell Biol , vol.8 , pp. 1163-1170
    • Kitamura, A.1    Kubota, H.2    Pack, C.G.3
  • 139
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, Kalmar B, Dick JR, Riddoch-Contreras J, Burnstock G, Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med. 2004;10:402-405.
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 140
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 (HSF1)-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N, Nagai Y, Popiel HA, Okamoto Y, Yamaguchi M, Toda T. Heat shock transcription factor 1 (HSF1)-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem. 2008;283:26188-26197.
    • (2008) J Biol Chem , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 141
    • 33847369469 scopus 로고    scopus 로고
    • The high affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey CA, Kamal A, Lundgren K, et al. The high affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest. 2007;117:648-658.
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3
  • 142
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings CJ, Sun Y, Opal P, et al. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum Mol Genet. 2001;10:1511-1518.
    • (2001) Hum Mol Genet , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3
  • 143
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, Mancini MA, AntalffyB, DeFranco DB, Orr HT, Zoghbi HY. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet. 1998;19:148-154.
    • (1998) Nat Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 144
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. Chaperone suppression of alpha synuclein toxicity in a Drosophila model for Parkinson's disease. Science. 2002;295:865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 145
    • 34248327285 scopus 로고    scopus 로고
    • CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model
    • Adachi H, Waza M, Tokui K, et al. CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model. J Neurosci. 2007;27:5115-5126.
    • (2007) J Neurosci , vol.27 , pp. 5115-5126
    • Adachi, H.1    Waza, M.2    Tokui, K.3
  • 146
    • 51349150684 scopus 로고    scopus 로고
    • Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
    • Lo Bianco C, Shorter J, Regulier E, et al. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. J Clin Invest. 2008; 118:3087-3097.
    • (2008) J Clin Invest , vol.118 , pp. 3087-3097
    • Lo Bianco, C.1    Shorter, J.2    Regulier, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.