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Volumn 15, Issue 1, 2010, Pages 39-53

Monoclonal antibody to novel cell surface epitope on Hsc70 promotes morphogenesis of bile ducts in newborn rat liver

Author keywords

Bile duct; Cell surface; Cholangiocyte; Epitope mapping; Hsc70

Indexed keywords

EPITOPE; HEAT SHOCK PROTEIN 70; MONOCLONAL ANTIBODY; SMALL INTERFERING RNA;

EID: 77449091559     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-009-0120-2     Document Type: Article
Times cited : (10)

References (58)
  • 1
    • 0034613163 scopus 로고    scopus 로고
    • ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes
    • doi:10.1074/jbc. M005226200
    • Arispe N, De Maio A (2000) ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes. J Biol Chem 275:30839-30843. doi:10.1074/jbc. M005226200
    • (2000) J Biol Chem , vol.275 , pp. 30839-30843
    • Arispe, N.1    De Maio, A.2
  • 2
    • 0036819191 scopus 로고    scopus 로고
    • Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70
    • DOI 10.1379/1466-1268(2002)007<0330:LIDTCA>2.0.CO;2
    • Arispe N, Doh M, De Maio A (2002) Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70. Cell Stress Chaperones 7:330-338. doi:10.1379/1466-1268 (2002) 007<0330:LIDTCA>2.0. CO;2 (Pubitemid 36008745)
    • (2002) Cell Stress and Chaperones , vol.7 , Issue.4 , pp. 330-338
    • Arispe, N.1    Doh, M.2    De Maio, A.3
  • 3
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • DOI 10.1096/fj.04-2088com
    • Arispe N, Doh M, Simakova O, Kurganov B, De Maio A (2004) Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 18:1636-1645. doi:10.1096/fj.04-2088com (Pubitemid 39463703)
    • (2004) FASEB Journal , vol.18 , Issue.14 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 4
    • 0027465440 scopus 로고
    • Keratin 14 protein in cultured nonparenchymal rat hepatic epithelial cells: Characterization of keratin 14 and keratin 19 as antigens for the commonly used mouse monoclonal antibody OV-6
    • DOI 10.1002/mc.2940070110
    • Bisgaard HC, Parmelee DC, Dunsford HA, Sechi S, Thorgeirsson SS (1993) Keratin 14 protein in cultured nonparenchymal rat hepatic epithelial cells: characterization of keratin 14 and keratin 19 as antigens for the commonly used mouse monoclonal antibody OV-6. Mol Carcinog 7:60-66. doi:10.1002/mc.2940070110 (Pubitemid 23061289)
    • (1993) Molecular Carcinogenesis , vol.7 , Issue.1 , pp. 60-66
    • Bisgaard, H.C.1    Parmelee, D.C.2    Dunsford, H.A.3    Sechi, S.4    Thorgeirsson, S.S.5
  • 5
    • 0030454056 scopus 로고    scopus 로고
    • Heat-shock protein 72 cell-surface expression on human lung carcinoma cells is associated with an increased sensitivity to lysis mediated by adherent natural killer cells
    • DOI 10.1007/s002620050326
    • Botzler C, Issels R, Multhoff G (1996) Heat-shock protein 72 cellsurface expression on human lung carcinoma cells in associated with an increased sensitivity to lysis mediated by adherent natural killer cells. Cancer Immunol Immunother 43:226-230. doi:10.1007/s002620050326 (Pubitemid 26426255)
    • (1996) Cancer Immunology Immunotherapy , vol.43 , Issue.4 , pp. 226-230
    • Botzler, C.1    Issels, R.2    Multhoff, G.3
  • 6
    • 0031945664 scopus 로고    scopus 로고
    • Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response
    • DOI 10.1379/1466-1268(1998)003<0006:DOELEO>2.3.CO;2
    • Botzler C, Li G, Issels RD, Multhoff G (1998) Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response. Cell Stress Chaperones 3:6-11. doi:10.1379/1466-1268 (1998) 003<0006:DOELEO>2.3. CO;2 (Pubitemid 28159674)
    • (1998) Cell Stress and Chaperones , vol.3 , Issue.1 , pp. 6-11
    • Botzler, C.1    Li, G.2    Issels, R.D.3    Multhoff, G.4
  • 7
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • DOI 10.1074/jbc.M302326200
    • Broquet AH, Thomas G, Masliah J, Trugnan G, Bachelet M (2003) Expression of the molecular chaperone Hsp70 in detergentresistant microdomains correlates with its membrane delivery and release. J Biol Chem 278:21601-21606. doi:10.1074/jbc. M302326200 (Pubitemid 36792559)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 8
    • 33746704413 scopus 로고    scopus 로고
    • Identification of members of the annexin family in the detergent-insoluble fraction of rat Morris hepatoma plasma membranes
    • DOI 10.1016/j.chroma.2006.02.020, PII S0021967306003670
    • Clifton JG, Brown MK, Huang F et al (2006) Identification of members of the annexin family in the detergent-insoluble fraction of rat Morris hepatoma plasma membranes. J Chromatogr A 1123:205-211. doi:10.1016/j.chroma.2006.02.020 (Pubitemid 44160514)
    • (2006) Journal of Chromatography A , vol.1123 , Issue.2 , pp. 205-211
    • Clifton, J.G.1    Brown, M.K.2    Huang, F.3    Li, X.4    Reutter, W.5    Hofmann, W.6    Hixson, D.C.7    Josic, D.8
  • 9
    • 0030811762 scopus 로고    scopus 로고
    • Evaluation of the differentiation potential of WB-F344 rat liver epithelial stem-like cells in vivo: Differentiation to hepatocytes after transplantation into dipeptidylpeptidase-IV-deficient rat liver
    • Coleman W, McCullough K, Esch G, Faris R, Hixson D, Smith G, Grisham J (1997) Evaluation of the differentiation potential of WB-F344 rat liver epithelial stem-like cells in vivo: differentiation to hepatocytes following transplantation into dipeptidylpeptidase IV-deficient rat liver. Am J Pathol 151:353-359 (Pubitemid 27330056)
    • (1997) American Journal of Pathology , vol.151 , Issue.2 , pp. 353-359
    • Coleman, W.B.1    McCullough, K.D.2    Esch, G.L.3    Paris, R.A.4    Hixson, D.C.5    Smith, G.J.6    Grisham, J.W.7
  • 11
    • 0033828673 scopus 로고    scopus 로고
    • Nuclear translocation and aggregate formation of heat shock cognate protein 70 (Hsc70) in oxidative stress and apoptosis
    • Dastoor Z, Dreyer J (2000) Nuclear translocation and aggregate formation of heat shock cognate protein 70 (Hsc70) in oxidative stress and apoptosis. J Cell Sci 113 (Pt 16):2845-2854
    • (2000) J Cell Sci , vol.113 , Issue.16 PART , pp. 2845-2854
    • Dastoor, Z.1    Dreyer, J.2
  • 12
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • DOI 10.1016/j.febslet.2007.05.039, PII S0014579307005674, Cellular Stress
    • Daugaard M, Rohde M, Jaattela M (2007) The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett 581:3702-3710. doi:10.1016/j.febslet. 2007.05.039 (Pubitemid 47081009)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 14
    • 0032608038 scopus 로고    scopus 로고
    • Heat shock proteins: Facts, thoughts, and dreams
    • doi:10.1097/00024382-199901000-00001
    • De Maio A (1999) Heat shock proteins: facts, thoughts, and dreams. Shock 11:1-12. doi:10.1097/00024382-199901000-00001
    • (1999) Shock , vol.11 , pp. 1-12
    • De Maio, A.1
  • 15
    • 0024363412 scopus 로고
    • Different lineages of chemically induced hepatocellular carcinoma in rats defined by monoclonal antibodies
    • Dunsford HA, Karnasuta C, Hunt JM, Sell S (1989) Different lineages of chemically induced hepatocellular carcinoma in rats defined by monoclonal antibodies. Cancer Res 49:4894-4900 (Pubitemid 19213644)
    • (1989) Cancer Research , vol.49 , Issue.17 , pp. 4894-4900
    • Dunsford, H.A.1    Karnasuta, C.2    Hunt, J.M.3    Sell, S.4
  • 16
    • 34249058118 scopus 로고    scopus 로고
    • Multiple roles of auxilin and Hsc70 in clathrin-mediated endocytosis
    • DOI 10.1111/j.1600-0854.2007.00568.x
    • Eisenberg E, Greene LE (2007) Multiple roles of auxilin and hsc70 in clathrin-mediated endocytosis. Traffic 8:640-646. doi:10.1111/j.1600-0854.2007. 00568.x (Pubitemid 46785147)
    • (2007) Traffic , vol.8 , Issue.6 , pp. 640-646
    • Eisenberg, E.1    Greene, L.E.2
  • 17
    • 0032837196 scopus 로고    scopus 로고
    • Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality
    • Elefant F, Palter KB (1999) Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality. Mol Biol Cell 10:2101-2117 (Pubitemid 29343122)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.7 , pp. 2101-2117
    • Elefant, F.1    Palter, K.B.2
  • 18
    • 0037155284 scopus 로고    scopus 로고
    • Hsc/Hsp70 interacting protein (Hip) associates with CXCR2 and regulates the receptor signaling and trafficking
    • DOI 10.1074/jbc.M110588200
    • Fan GH, Yang W, Sai J, Richmond A (2002) Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking. J Biol Chem 277:6590-6597. doi:10.1074/jbc. M110588200 (Pubitemid 34968459)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6590-6597
    • Fan, G.-H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 19
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • doi:10.1002/ijc.2910510418
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C (1992) Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 51:613-619. doi:10.1002/ijc.2910510418
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 20
    • 0034879081 scopus 로고    scopus 로고
    • Contribution of heat shock proteins to cell protection from complement-mediated lysis
    • Fishelson Z, Hochman I, Greene LE, Eisenberg E (2001) Contribution of heat shock proteins to cell protection from complement-mediated lysis. Int Immunol 13:983-991. doi:10.1093/intimm/13.8.983 (Pubitemid 32750501)
    • (2001) International Immunology , vol.13 , Issue.8 , pp. 983-991
    • Fishelson, Z.1    Hochman, I.2    Greene, L.E.3    Eisenberg, E.4
  • 21
    • 44849133308 scopus 로고    scopus 로고
    • Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3
    • Gehrmann M, Liebisch G, Schmitz G et al (2008) Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3. PLoS ONE 3:e1925
    • (2008) PLoS ONE , vol.3
    • Gehrmann, M.1    Liebisch, G.2    Schmitz, G.3
  • 22
    • 0034492976 scopus 로고    scopus 로고
    • Temporal analysis of hepatocyte differentiation by small hepatocyte-like progenitor cells during liver regeneration in retrorsine-exposed rats
    • Gordon GJ, Coleman WB, Grisham JW (2000) Temporal analysis of hepatocyte differentiation by small hepatocyte-like progenitor cells during liver regeneration in retrorsine-exposed rats. Am J Pathol 157:771-786 (Pubitemid 32109370)
    • (2000) American Journal of Pathology , vol.157 , Issue.3 , pp. 771-786
    • Gordon, G.J.1    Coleman, W.B.2    Grisham, J.W.3
  • 23
    • 34248195469 scopus 로고    scopus 로고
    • Lipid rafts and membrane traffic
    • DOI 10.1016/j.febslet.2007.03.019, PII S0014579307002736, Membrane Trafficking
    • Hanzal-Bayer MF, Hancock JF (2007) Lipid rafts and membrane traffic. FEBS Lett 581:2098-2104. doi:10.1016/j.febs let.2007.03.019 (Pubitemid 46709907)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2098-2104
    • Hanzal-Bayer, M.F.1    Hancock, J.F.2
  • 24
    • 0031665599 scopus 로고    scopus 로고
    • Localization of pNT22 70 kDa heat shock cognate-like protein in the plasma membrane
    • Hirai I, Sato N, Qi W, Ohtani S, Torigoe T, Kikuchi K (1998) Localization of pNT22 70 kDa heat shock cognate-like protein in the plasma membrane. Cell Struct Funct 23:153-158 (Pubitemid 28401137)
    • (1998) Cell Structure and Function , vol.23 , Issue.3 , pp. 153-158
    • Hirai, I.1    Sato, N.2    Qi, W.3    Ohtani, S.4    Torigoe, T.5    Kikuchi, K.6
  • 25
    • 0342630017 scopus 로고    scopus 로고
    • Development and phenotypic heterogeneity of intrahepatic biliary epithelial cells
    • Sirica AE, Longnecker DS eds, Marcel Dekker, New York
    • Hixson DC, Fowler LC (1997) Development and phenotypic heterogeneity of intrahepatic biliary epithelial cells. In: Sirica AE, Longnecker DS (eds) Biliary and pancreatic ductal epithelium. Marcel Dekker, New York, pp 1-40
    • (1997) Biliary and Pancreatic Ductal Epithelium , pp. 1-40
    • Hixson, D.C.1    Fowler, L.C.2
  • 26
    • 0034077478 scopus 로고    scopus 로고
    • Differentiation status of rat ductal cells and ethionine-induced hepatic carcinomas defined with surface-reactive monoclonal antibodies
    • DOI 10.1006/exmp.2000.2302
    • Hixson DC, Brown J, McBride AC, Affigne S (2000) Differentiation status of rat ductal cells and ethionine-induced hepatic carcinomas defined with surface-reactive monoclonal antibodies. Exp Mol Pathol 68:152-169. doi:10.1006/exmp. 2000.2302 (Pubitemid 30337516)
    • (2000) Experimental and Molecular Pathology , vol.68 , Issue.3 , pp. 152-169
    • Hixson, D.C.1    Brown, J.2    McBride, A.C.3    Affigne, S.4
  • 27
    • 51449098448 scopus 로고    scopus 로고
    • Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum
    • doi:10.1111/j.1348-0421.2008.00017.x
    • Kamiguchi K, Torigoe T, Fujiwara O et al (2008) Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum. Microbiol Immunol 52:94-106. doi:10.1111/j.1348-0421.2008.00017.x
    • (2008) Microbiol Immunol , vol.52 , pp. 94-106
    • Kamiguchi, K.1    Torigoe, T.2    Fujiwara, O.3
  • 28
    • 0034710901 scopus 로고    scopus 로고
    • Clonogenic hepatoblasts, common precursors for hepatocytic and biliary lineages, are lacking classical major histocompatibility complex class I antigen
    • doi:10.1073/pnas.97.22.12132
    • Kubota H, Reid LM (2000) Clonogenic hepatoblasts, common precursors for hepatocytic and biliary lineages, are lacking classical major histocompatibility complex class I antigen. Proc Natl Acad Sci U S A 97:12132-12137. doi:10.1073/pnas.97.22.12132
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12132-12137
    • Kubota, H.1    Reid, L.M.2
  • 29
    • 33745946236 scopus 로고    scopus 로고
    • Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes
    • DOI 10.1002/elps.200600059
    • Lawson EL, Clifton JG, Huang F, Li X, Hixson DC, Josic D (2006) Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes. Electrophoresis 27:2747-2758. doi:10.1002/elps.200600059 (Pubitemid 44057524)
    • (2006) Electrophoresis , vol.27 , Issue.13 , pp. 2747-2758
    • Lawson, E.L.1    Clifton, J.G.2    Huang, F.3    Li, X.4    Hixson, D.C.5    Josic, D.6
  • 30
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • doi:10.1007/s00018-004-4464-6
    • Mayer MP, Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62:670-684. doi:10.1007/s00018-004-4464-6
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 31
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • doi:10.1002/ijc.2910610222
    • Multhoff G, Botzler C, Wiesnet M, Muller E, Meier T, Wilmanns W, Issels RD (1995) A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int J Cancer 61:272-279. doi:10.1002/ijc.2910610222
    • (1995) Int J Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Muller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 32
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: A recognition structure for natural killer cells
    • Multhoff G, Botzler C, Jennen L, Schmidt J, Ellwart J, Issels R (1997) Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J Immunol 158:4341-4350 (Pubitemid 127483936)
    • (1997) Journal of Immunology , vol.158 , Issue.9 , pp. 4341-4350
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3    Schmidt, J.4    Ellwart, J.5    Issels, R.6
  • 34
    • 0035205080 scopus 로고    scopus 로고
    • A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity
    • DOI 10.1379/1466-1268(2001)006<0337:AMHPSN>2.0.CO;2
    • Multhoff G, Pfister K, Gehrmann M, Hantschel M, Gross C, Hafner M, Hiddemann W (2001) A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity. Cell Stress Chaperones 6:337-344. doi:10.1379/1466-1268 (2001) 006<0337:AMHPSN>2.0. CO;2 (Pubitemid 33123486)
    • (2001) Cell Stress and Chaperones , vol.6 , Issue.4 , pp. 337-344
    • Multhoff, G.1    Pfister, K.2    Gehrmann, M.3    Hantschel, M.4    Gross, C.5    Hafner, M.6    Hiddemann, W.7
  • 35
    • 0038617815 scopus 로고    scopus 로고
    • Auxilin-dynamin interactions link the uncoating ATPase chaperone machinery with vesicle formation
    • DOI 10.1016/S1534-5807(03)00157-6, PII S1534580703001576
    • Newmyer SL, Christensen A, Sever S (2003) Auxilin-dynamin interactions link the uncoating ATPase chaperone machinery with vesicle formation. Dev Cell 4:929-940. doi:10.1016/S1534-5807 (03) 00157-6 (Pubitemid 36676043)
    • (2003) Developmental Cell , vol.4 , Issue.6 , pp. 929-940
    • Newmyer, S.L.1    Christensen, A.2    Sever, S.3
  • 36
    • 0029979179 scopus 로고    scopus 로고
    • Blast-like cell compartment in carcinogen-induced proliferating bile ductules
    • Novikoff PM, Yam A, Oikawa I (1996) Blast-like cell compartment in carcinogen-induced proliferating bile ductules. Am J Pathol 148:1473-1492 (Pubitemid 26135890)
    • (1996) American Journal of Pathology , vol.148 , Issue.5 , pp. 1473-1492
    • Novikoff, P.M.1    Yam, A.2    Oikawa, I.3
  • 37
    • 41949099869 scopus 로고    scopus 로고
    • Dissecting lipid raft facilitated cell signaling pathways in cancer
    • Patra SK (2008) Dissecting lipid raft facilitated cell signaling pathways in cancer. Biochim Biophys Acta 1785:182-206
    • (2008) Biochim Biophys Acta , vol.1785 , pp. 182-206
    • Patra, S.K.1
  • 38
    • 0034698087 scopus 로고    scopus 로고
    • The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor
    • DOI 10.1074/jbc.M002035200
    • Rajapandi T, Greene LE, Eisenberg E (2000) The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor. J Biol Chem 275:22597-22604. doi:10.1074/jbc. M002035200 (Pubitemid 30621853)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.29 , pp. 22597-22604
    • Rajapandi, T.1    Greene, L.E.2    Eisenberg, E.3
  • 39
    • 0033944602 scopus 로고    scopus 로고
    • The heat shock cognate protein hsc73 assembles with adenosine receptors to form functional modules in the cell membrane
    • DOI 10.1128/MCB.20.14.5164-5174.2000
    • Sarrio S, Casado V, Escriche M et al (2000) The heat shock cognate protein hsc73 assembles with A (1) adenosine receptors to form functional modules in the cell membrane. Mol Cell Biol 20:5164-5174. doi:10.1128/MCB.20.14. 5164-5174.2000 (Pubitemid 30431569)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.14 , pp. 5164-5174
    • Sarrio, S.1    Casado, V.2    Escriche, M.3    Ciruela, F.4    Mallol, J.5    Canela, E.I.6    Lluis, C.7    Franco, R.8
  • 40
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman DM, Schmid SL, Braell WA, Rothman JE (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 99:723-733. doi:10.1083/jcb.99.2.723 (Pubitemid 14065201)
    • (1984) Journal of Cell Biology , vol.99 , Issue.2 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 41
    • 0031891207 scopus 로고    scopus 로고
    • Comparison of liver progenitor cells in human atypical ductular reactions with those seen in experimental models of liver injury
    • DOI 10.1002/hep.510270202
    • Sell S (1998) Comparison of liver progenitor cells in human atypical ductular reactions with those seen in experimental models of liver injury. Hepatology 27:317-331. doi:10.1002/hep. 510270202 (Pubitemid 28081042)
    • (1998) Hepatology , vol.27 , Issue.2 , pp. 317-331
    • Sell, S.1
  • 42
    • 33644512665 scopus 로고    scopus 로고
    • Response to injury
    • Landes Company, Austin
    • Sell S, Ilic Z (eds) (1997) Response to injury. Liver stem cells. Landes Company, Austin, 223-286
    • (1997) Liver Stem Cells , pp. 223-286
    • Sell, S.1    Ilic, Z.2
  • 43
    • 0028294877 scopus 로고
    • Maturation arrest of stem cell differentiation is a common pathway for the cellular origin of teratocarcinomas and epithelial cancers
    • Sell S, Pierce GB (1994) Maturation arrest of stem cell differentiation is a common pathway for the cellular origin of teratocarcinomas and epithelial cancers. Lab Invest 70:6-22 (Pubitemid 24080100)
    • (1994) Laboratory Investigation , vol.70 , Issue.1 , pp. 6-22
    • Sell, S.1    Pierce, G.B.2
  • 45
    • 40449087411 scopus 로고    scopus 로고
    • Requirement of Nmyristoyltransferase 1 in the development of monocytic lineage
    • Shrivastav A, Varma S, Lawman Z et al (2008) Requirement of Nmyristoyltransferase 1 in the development of monocytic lineage. J Immunol 180:1019-1028
    • (2008) J Immunol , vol.180 , pp. 1019-1028
    • Shrivastav, A.1    Varma, S.2    Lawman, Z.3
  • 46
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • DOI 10.1038/42408
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569-572. doi:10.1038/42408 (Pubitemid 27248754)
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 47
    • 33751551702 scopus 로고    scopus 로고
    • Cholangiocyte marker-positive and -negative fetal liver cells differ significantly in their ability to regenerate the livers of adult rats exposed to retrorsine
    • DOI 10.1242/dev.02589
    • Simper-Ronan R, Brilliant K, Flanagan D, Carreiro M, Callanan H, Sabo E, Hixson DC (2006) Cholangiocyte marker-positive and - negative fetal liver cells differ significantly in their ability to regenerate the livers of adult rats exposed to retrorsine. Development 133:4269-4279. doi:10.1242/dev. 02589 (Pubitemid 44830670)
    • (2006) Development , vol.133 , Issue.21 , pp. 4269-4279
    • Simper-Ronan, R.1    Brillian, K.2    Flanagan, D.3    Carreiro, M.4    Callanan, H.5    Sabo, E.6    Hixson, D.C.7
  • 48
    • 0023316845 scopus 로고
    • Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells
    • Sorger PK, Pelham HR (1987) Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. Embo J 6:993-998
    • (1987) Embo J , vol.6 , pp. 993-998
    • Sorger, P.K.1    Pelham, H.R.2
  • 49
    • 0037033798 scopus 로고    scopus 로고
    • Clonal identification and characterization of self-renewing pluripotent stem cells in the developing liver
    • DOI 10.1083/jcb.200108066
    • Suzuki A, Zheng YY, Kaneko S, Onodera M, Fukao K, Nakauchi H, Taniguchi H (2002) Clonal identification and characterization of self-renewing pluripotent stem cells in the developing liver. J Cell Biol 156:173-184. doi:10.1083/jcb.200108066 (Pubitemid 34846945)
    • (2002) Journal of Cell Biology , vol.156 , Issue.1 , pp. 173-184
    • Suzuki, A.1    Zheng, Y.-W.2    Kaneko, S.3    Onodera, M.4    Fukao, K.5    Nakauchi, H.6    Taniguchi, H.7
  • 50
    • 0029951710 scopus 로고    scopus 로고
    • Growth and differentiation in culture of clonogenic hepatocytes that express both phenotypes of hepatocytes and biliary epithelial cells
    • Tateno C, Yoshizato K (1996) Growth and differentiation in culture of clonogenic hepatocytes that express both phenotypes of hepatocytes and biliary epithelial cells. Am J Pathol 149:1593-1605 (Pubitemid 26363966)
    • (1996) American Journal of Pathology , vol.149 , Issue.5 , pp. 1593-1605
    • Tateno, C.1    Yoshizato, K.2
  • 51
    • 0030112681 scopus 로고    scopus 로고
    • A hitchhiker's guide to the human Hsp70 family
    • Tavaria M, Gabriele T, Kola I, Anderson RL (1996) A hitchhiker's guide to the human Hsp70 family. Cell Stress Chaperones 1:23-28. doi:10.1379/1466-1268 (1996) 001<0023:AHSGTT>2.3. CO;2 (Pubitemid 126672886)
    • (1996) Cell Stress and Chaperones , vol.1 , Issue.1 , pp. 23-28
    • Tavaria, M.1    Gabriele, T.2    Kola, I.3    Anderson, R.L.4
  • 52
    • 0035315845 scopus 로고    scopus 로고
    • A CD14-independent LPS receptor cluster
    • DOI 10.1038/86342
    • Triantafilou K, Triantafilou M, Dedrick RL (2001) A CD14-independent LPS receptor cluster. Nat Immunol 2:338-345. doi:10.1038/86342 (Pubitemid 33706345)
    • (2001) Nature Immunology , vol.2 , Issue.4 , pp. 338-345
    • Triantafilou, K.1    Triantafilou, M.2    Dedrick, R.L.3
  • 54
    • 1542275420 scopus 로고    scopus 로고
    • Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70
    • DOI 10.1074/jbc.M308848200
    • Tsukahara F, Maru Y (2004) Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70. J Biol Chem 279:8867-8872. doi:10.1074/jbc. M308848200 (Pubitemid 38295946)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8867-8872
    • Tsukahara, F.1    Maru, Y.2
  • 55
    • 0345211494 scopus 로고    scopus 로고
    • Dynamic restricted expression of the chaperone Hsc70 in early chick development
    • DOI 10.1016/S0925-4773(99)00015-5, PII S0925477399000155
    • Vega-Nunez E, Pena-Melian A, de la Rosa EJ, de Pablo F (1999) Dynamic restricted expression of the chaperone Hsc70 in early chick development. Mech Dev 82:199-203. doi:10.1016/S0925-4773 (99) 00015-5 (Pubitemid 29243068)
    • (1999) Mechanisms of Development , vol.82 , Issue.1-2 , pp. 199-203
    • Vega-Nunez, E.1    Pena-Melian, A.2    De La Rosa, E.J.3    De Pablo, F.4
  • 56
    • 0027218229 scopus 로고
    • Characterization of a mature bile duct antigen expressed on a subpopulation of biliary ductular cells but absent from oval cells
    • DOI 10.1016/0270-9139(93)90019-J
    • Yang L, Faris RA, Hixson DC (1993a) Characterization of a mature bile duct antigen expressed on a subpopulation of biliary ductular cells but absent from oval cells. Hepatology 18:357-366 (Pubitemid 23225107)
    • (1993) Hepatology , vol.18 , Issue.2 , pp. 357-366
    • Yang, L.1    Faris, R.A.2    Hixson, D.C.3
  • 57
    • 0027408238 scopus 로고
    • Long-term culture and characteristics of normal rat liver bile duct epithelial cells
    • Yang L, Faris RA, Hixson DC (1993b) Long-term culture and characteristics of normal rat liver bile duct epithelial cells. Gastroenterology 104:840-852 (Pubitemid 23059584)
    • (1993) Gastroenterology , vol.104 , Issue.3 , pp. 840-852
    • Yang, L.1    Faris, R.A.2    Hixson, D.C.3
  • 58
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • DOI 10.1016/j.immuni.2005.03.009, PII S1074761305001044
    • Zhou D, Li P, Lin Y et al (2005) Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 22:571-581. doi:10.1016/j.immuni. 2005.03.009 (Pubitemid 40719193)
    • (2005) Immunity , vol.22 , Issue.5 , pp. 571-581
    • Zhou, D.1    Li, P.2    Lin, Y.3    Lott, J.M.4    Hislop, A.D.5    Canaday, D.H.6    Brutkiewicz, R.R.7    Blum, J.S.8


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