메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Comparative Proteomics Reveals Novel Components at the Plasma Membrane of Differentiated HepaRG Cells and Different Distribution in Hepatocyte- and Biliary-Like Cells

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; CATHEPSIN K; CYCLOPHILIN A; LIPOCORTIN 1; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE ISOMERASE A4; PROTEOME; UNCLASSIFIED DRUG;

EID: 84882622610     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0071859     Document Type: Article
Times cited : (12)

References (55)
  • 2
    • 34247517355 scopus 로고    scopus 로고
    • The human hepatoma HepaRG cells: a highly differentiated model for studies of liver metabolism and toxicity of xenobiotics
    • Guillouzo A, Corlu A, Aninat C, Glaise D, Morel F, et al. (2007) The human hepatoma HepaRG cells: a highly differentiated model for studies of liver metabolism and toxicity of xenobiotics. Chem Biol Interact 168: 66-73.
    • (2007) Chem Biol Interact , vol.168 , pp. 66-73
    • Guillouzo, A.1    Corlu, A.2    Aninat, C.3    Glaise, D.4    Morel, F.5
  • 3
    • 34247351508 scopus 로고    scopus 로고
    • Transdifferentiation of hepatocyte-like cells from the human hepatoma HepaRG cell line through bipotent progenitor
    • Cerec V, Glaise D, Garnier D, Morosan S, Turlin B, et al. (2007) Transdifferentiation of hepatocyte-like cells from the human hepatoma HepaRG cell line through bipotent progenitor. Hepatology 45: 957-967.
    • (2007) Hepatology , vol.45 , pp. 957-967
    • Cerec, V.1    Glaise, D.2    Garnier, D.3    Morosan, S.4    Turlin, B.5
  • 4
    • 84866331511 scopus 로고    scopus 로고
    • In vitro evaluation of major in vivo drug metabolic pathways using primary human hepatocytes and HepaRG cells in suspension and a dynamic three-dimensional bioreactor system
    • Darnell M, Ulvestad M, Ellis E, Weidolf L, Andersson TB, (2012) In vitro evaluation of major in vivo drug metabolic pathways using primary human hepatocytes and HepaRG cells in suspension and a dynamic three-dimensional bioreactor system. J Pharmacol Exp Ther 343: 134-144.
    • (2012) J Pharmacol Exp Ther , vol.343 , pp. 134-144
    • Darnell, M.1    Ulvestad, M.2    Ellis, E.3    Weidolf, L.4    Andersson, T.B.5
  • 5
    • 84859163249 scopus 로고    scopus 로고
    • Characterization of primary human hepatocytes, HepG2 cells, and HepaRG cells at the mRNA level and CYP activity in response to inducers and their predictivity for the detection of human hepatotoxins
    • Gerets HH, Tilmant K, Gerin B, Chanteux H, Depelchin BO, et al. (2012) Characterization of primary human hepatocytes, HepG2 cells, and HepaRG cells at the mRNA level and CYP activity in response to inducers and their predictivity for the detection of human hepatotoxins. Cell Biol Toxicol 28: 69-87.
    • (2012) Cell Biol Toxicol , vol.28 , pp. 69-87
    • Gerets, H.H.1    Tilmant, K.2    Gerin, B.3    Chanteux, H.4    Depelchin, B.O.5
  • 6
    • 44149105179 scopus 로고    scopus 로고
    • Long-term functional stability of human HepaRG hepatocytes and use for chronic toxicity and genotoxicity studies
    • Josse R, Aninat C, Glaise D, Dumont J, Fessard V, et al. (2008) Long-term functional stability of human HepaRG hepatocytes and use for chronic toxicity and genotoxicity studies. Drug Metab Dispos 36: 1111-1118.
    • (2008) Drug Metab Dispos , vol.36 , pp. 1111-1118
    • Josse, R.1    Aninat, C.2    Glaise, D.3    Dumont, J.4    Fessard, V.5
  • 7
    • 46249092290 scopus 로고    scopus 로고
    • Translational control plays a prominent role in the hepatocytic differentiation of HepaRG liver progenitor cells
    • Parent R, Beretta L, (2008) Translational control plays a prominent role in the hepatocytic differentiation of HepaRG liver progenitor cells. Genome Biol 9: R19.
    • (2008) Genome Biol , vol.9
    • Parent, R.1    Beretta, L.2
  • 8
    • 79960707493 scopus 로고    scopus 로고
    • Long-term propagation of serum hepatitis C virus (HCV) with production of enveloped HCV particles in human HepaRG hepatocytes
    • Ndongo-Thiam N, Berthillon P, Errazuriz E, Bordes I, De Sequeira S, et al. (2011) Long-term propagation of serum hepatitis C virus (HCV) with production of enveloped HCV particles in human HepaRG hepatocytes. Hepatology 54: 406-417.
    • (2011) Hepatology , vol.54 , pp. 406-417
    • Ndongo-Thiam, N.1    Berthillon, P.2    Errazuriz, E.3    Bordes, I.4    De Sequeira, S.5
  • 9
    • 78049399296 scopus 로고    scopus 로고
    • The use of hepatocytes to investigate HDV infection: the HDV/HepaRG model
    • Sureau C, (2010) The use of hepatocytes to investigate HDV infection: the HDV/HepaRG model. Methods Mol Biol 640: 463-473.
    • (2010) Methods Mol Biol , vol.640 , pp. 463-473
    • Sureau, C.1
  • 11
    • 33846538587 scopus 로고    scopus 로고
    • Viral and cellular determinants involved in hepadnaviral entry
    • Glebe D, Urban S, (2007) Viral and cellular determinants involved in hepadnaviral entry. World J Gastroenterol 13: 22-38.
    • (2007) World J Gastroenterol , vol.13 , pp. 22-38
    • Glebe, D.1    Urban, S.2
  • 12
    • 0029890346 scopus 로고    scopus 로고
    • Hepatitis B virus infection of tupaia hepatocytes in vitro and in vivo
    • Walter E, Keist R, Niederost B, Pult I, Blum HE, (1996) Hepatitis B virus infection of tupaia hepatocytes in vitro and in vivo. Hepatology 24: 1-5.
    • (1996) Hepatology , vol.24 , pp. 1-5
    • Walter, E.1    Keist, R.2    Niederost, B.3    Pult, I.4    Blum, H.E.5
  • 13
    • 84857066990 scopus 로고    scopus 로고
    • Interactions between hepatitis B virus and aflatoxin B(1): effects on p53 induction in HepaRG cells
    • Lereau M, Gouas D, Villar S, Besaratinia A, Hautefeuille A, et al. (2012) Interactions between hepatitis B virus and aflatoxin B(1): effects on p53 induction in HepaRG cells. J Gen Virol 93: 640-650.
    • (2012) J Gen Virol , vol.93 , pp. 640-650
    • Lereau, M.1    Gouas, D.2    Villar, S.3    Besaratinia, A.4    Hautefeuille, A.5
  • 14
    • 72849144468 scopus 로고    scopus 로고
    • Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells
    • Macovei A, Radulescu C, Lazar C, Petrescu S, Durantel D, et al. (2010) Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells. J Virol 84: 243-253.
    • (2010) J Virol , vol.84 , pp. 243-253
    • Macovei, A.1    Radulescu, C.2    Lazar, C.3    Petrescu, S.4    Durantel, D.5
  • 15
    • 84856396808 scopus 로고    scopus 로고
    • Hepatocyte polarization is essential for the productive entry of the hepatitis B virus
    • Schulze A, Mills K, Weiss TS, Urban S, (2012) Hepatocyte polarization is essential for the productive entry of the hepatitis B virus. Hepatology 55: 373-383.
    • (2012) Hepatology , vol.55 , pp. 373-383
    • Schulze, A.1    Mills, K.2    Weiss, T.S.3    Urban, S.4
  • 16
    • 84878178356 scopus 로고    scopus 로고
    • Regulation of hepatitis B virus infection by Rab5, rAb7, and the endolysosomal compartment
    • Macovei A, Petrareanu C, Lazar C, Florian P, Branza-Nichita N, (2013) Regulation of hepatitis B virus infection by Rab5, rAb7, and the endolysosomal compartment. J Virol 87: 6415-6427.
    • (2013) J Virol , vol.87 , pp. 6415-6427
    • Macovei, A.1    Petrareanu, C.2    Lazar, C.3    Florian, P.4    Branza-Nichita, N.5
  • 17
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M, (2003) Mass spectrometry-based proteomics. Nature 422: 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 18
    • 84873991171 scopus 로고    scopus 로고
    • Investigation of stable and transient protein-protein interactions: Past, present, and future
    • Ngounou Wetie AG, Sokolowska I, Woods AG, Roy U, Loo JA, et al. (2013) Investigation of stable and transient protein-protein interactions: Past, present, and future. Proteomics 13: 538-557.
    • (2013) Proteomics , vol.13 , pp. 538-557
    • Ngounou Wetie, A.G.1    Sokolowska, I.2    Woods, A.G.3    Roy, U.4    Loo, J.A.5
  • 21
    • 60849133938 scopus 로고    scopus 로고
    • Proteomic analysis of HepaRG cells: a novel cell line that supports hepatitis B virus infection
    • Narayan R, Gangadharan B, Hantz O, Antrobus R, Garcia A, et al. (2009) Proteomic analysis of HepaRG cells: a novel cell line that supports hepatitis B virus infection. J Proteome Res 8: 118-122.
    • (2009) J Proteome Res , vol.8 , pp. 118-122
    • Narayan, R.1    Gangadharan, B.2    Hantz, O.3    Antrobus, R.4    Garcia, A.5
  • 22
    • 84864440753 scopus 로고    scopus 로고
    • Proteomic analysis of plasma membranes isolated from undifferentiated and differentiated HepaRG cells
    • Sokolowska I, Dorobantu C, Woods AG, Macovei A, Branza-Nichita N, et al. (2012) Proteomic analysis of plasma membranes isolated from undifferentiated and differentiated HepaRG cells. Proteome Sci 10: 47.
    • (2012) Proteome Sci , vol.10 , pp. 47
    • Sokolowska, I.1    Dorobantu, C.2    Woods, A.G.3    Macovei, A.4    Branza-Nichita, N.5
  • 23
    • 78049401342 scopus 로고    scopus 로고
    • The HepaRG cell line: biological properties and relevance as a tool for cell biology, drug metabolism, and virology studies
    • Marion MJ, Hantz O, Durantel D, (2010) The HepaRG cell line: biological properties and relevance as a tool for cell biology, drug metabolism, and virology studies. Methods Mol Biol 640: 261-272.
    • (2010) Methods Mol Biol , vol.640 , pp. 261-272
    • Marion, M.J.1    Hantz, O.2    Durantel, D.3
  • 24
    • 84857995363 scopus 로고    scopus 로고
    • Identification of consistent alkylation of cysteine-less peptides in a proteomics experiment
    • Woods AG, Sokolowska I, Darie CC, (2012) Identification of consistent alkylation of cysteine-less peptides in a proteomics experiment. Biochem Biophys Res Commun 419: 305-308.
    • (2012) Biochem Biophys Res Commun , vol.419 , pp. 305-308
    • Woods, A.G.1    Sokolowska, I.2    Darie, C.C.3
  • 25
    • 81855192712 scopus 로고    scopus 로고
    • Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry
    • Darie CC, Deinhardt K, Zhang G, Cardasis HS, Chao MV, et al. (2011) Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry. Proteomics 11: 4514-4528.
    • (2011) Proteomics , vol.11 , pp. 4514-4528
    • Darie, C.C.1    Deinhardt, K.2    Zhang, G.3    Cardasis, H.S.4    Chao, M.V.5
  • 26
  • 27
    • 0032830130 scopus 로고    scopus 로고
    • The transferrin receptor: role in health and disease
    • Ponka P, Lok CN, (1999) The transferrin receptor: role in health and disease. Int J Biochem Cell Biol 31: 1111-1137.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1111-1137
    • Ponka, P.1    Lok, C.N.2
  • 28
    • 34748873467 scopus 로고    scopus 로고
    • Identification of transcriptional targets of the dual-function transcription factor/phosphatase eyes absent
    • Jemc J, Rebay I, (2007) Identification of transcriptional targets of the dual-function transcription factor/phosphatase eyes absent. Dev Biol 310: 416-429.
    • (2007) Dev Biol , vol.310 , pp. 416-429
    • Jemc, J.1    Rebay, I.2
  • 29
    • 0027509048 scopus 로고
    • Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons
    • Yonemura S, Nagafuchi A, Sato N, Tsukita S, (1993) Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons. J Cell Biol 120: 437-449.
    • (1993) J Cell Biol , vol.120 , pp. 437-449
    • Yonemura, S.1    Nagafuchi, A.2    Sato, N.3    Tsukita, S.4
  • 30
    • 34447580876 scopus 로고    scopus 로고
    • Subcellular proteomics of cell differentiation: quantitative analysis of the plasma membrane proteome of Caco-2 cells
    • Pshezhetsky AV, Fedjaev M, Ashmarina L, Mazur A, Budman L, et al. (2007) Subcellular proteomics of cell differentiation: quantitative analysis of the plasma membrane proteome of Caco-2 cells. Proteomics 7: 2201-2215.
    • (2007) Proteomics , vol.7 , pp. 2201-2215
    • Pshezhetsky, A.V.1    Fedjaev, M.2    Ashmarina, L.3    Mazur, A.4    Budman, L.5
  • 31
    • 79953287011 scopus 로고    scopus 로고
    • HIV envelope: challenges and opportunities for development of entry inhibitors
    • Caffrey M, (2011) HIV envelope: challenges and opportunities for development of entry inhibitors. Trends Microbiol 19: 191-197.
    • (2011) Trends Microbiol , vol.19 , pp. 191-197
    • Caffrey, M.1
  • 32
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: a structural view of the herpesvirus entry machinery
    • Connolly SA, Jackson JO, Jardetzky TS, Longnecker R, (2011) Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol 9: 369-381.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 33
    • 79551639004 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Cosset FL, Lavillette D, (2011) Cell entry of enveloped viruses. Adv Genet 73: 121-183.
    • (2011) Adv Genet , vol.73 , pp. 121-183
    • Cosset, F.L.1    Lavillette, D.2
  • 34
    • 0034791499 scopus 로고    scopus 로고
    • Annexin expressions are temporally and spatially regulated during rat hepatocyte differentiation
    • Della Gaspera B, Braut-Boucher F, Bomsel M, Chatelet F, Guguen-Guillouzo C, et al. (2001) Annexin expressions are temporally and spatially regulated during rat hepatocyte differentiation. Dev Dyn 222: 206-217.
    • (2001) Dev Dyn , vol.222 , pp. 206-217
    • Della Gaspera, B.1    Braut-Boucher, F.2    Bomsel, M.3    Chatelet, F.4    Guguen-Guillouzo, C.5
  • 35
    • 77956799975 scopus 로고    scopus 로고
    • Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell type-dependent role in regulating infectivity
    • Rai T, Mosoian A, Resh MD, (2010) Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell type-dependent role in regulating infectivity. J Virol 84: 9783-9792.
    • (2010) J Virol , vol.84 , pp. 9783-9792
    • Rai, T.1    Mosoian, A.2    Resh, M.D.3
  • 36
    • 80655125503 scopus 로고    scopus 로고
    • Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity
    • Yang SL, Chou YT, Wu CN, Ho MS, (2011) Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity. J Virol 85: 11809-11820.
    • (2011) J Virol , vol.85 , pp. 11809-11820
    • Yang, S.L.1    Chou, Y.T.2    Wu, C.N.3    Ho, M.S.4
  • 37
    • 84863158307 scopus 로고    scopus 로고
    • Human annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection
    • Ma H, Kien F, Maniere M, Zhang Y, Lagarde N, et al. (2012) Human annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection. J Virol 86: 1789-1801.
    • (2012) J Virol , vol.86 , pp. 1789-1801
    • Ma, H.1    Kien, F.2    Maniere, M.3    Zhang, Y.4    Lagarde, N.5
  • 38
    • 0033058107 scopus 로고    scopus 로고
    • Transfection of a rat hepatoma cell line with a construct expressing human liver annexin V confers susceptibility to hepatitis B virus infection
    • Gong ZJ, De Meyer S, van Pelt J, Hertogs K, Depla E, et al. (1999) Transfection of a rat hepatoma cell line with a construct expressing human liver annexin V confers susceptibility to hepatitis B virus infection. Hepatology 29: 576-584.
    • (1999) Hepatology , vol.29 , pp. 576-584
    • Gong, Z.J.1    De Meyer, S.2    van Pelt, J.3    Hertogs, K.4    Depla, E.5
  • 39
    • 58149193234 scopus 로고    scopus 로고
    • STRING 8-a global view on proteins and their functional interactions in 630 organisms
    • Jensen LJ, Kuhn M, Stark M, Chaffron S, Creevey C, et al. (2009) STRING 8-a global view on proteins and their functional interactions in 630 organisms. Nucleic Acids Res 37: D412-416.
    • (2009) Nucleic Acids Res , vol.37
    • Jensen, L.J.1    Kuhn, M.2    Stark, M.3    Chaffron, S.4    Creevey, C.5
  • 40
    • 78651324347 scopus 로고    scopus 로고
    • The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored
    • Szklarczyk D, Franceschini A, Kuhn M, Simonovic M, Roth A, et al. (2011) The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored. Nucleic Acids Res 39: D561-568.
    • (2011) Nucleic Acids Res , vol.39
    • Szklarczyk, D.1    Franceschini, A.2    Kuhn, M.3    Simonovic, M.4    Roth, A.5
  • 41
    • 84872858776 scopus 로고    scopus 로고
    • Insights into the roles of cyclophilin A during influenza virus infection
    • Liu X, Zhao Z, Liu W, (2013) Insights into the roles of cyclophilin A during influenza virus infection. Viruses 5: 182-191.
    • (2013) Viruses , vol.5 , pp. 182-191
    • Liu, X.1    Zhao, Z.2    Liu, W.3
  • 42
    • 77949417535 scopus 로고    scopus 로고
    • Hepatitis B virus (HBV) surface antigen interacts with and promotes cyclophilin a secretion: possible link to pathogenesis of HBV infection
    • Tian X, Zhao C, Zhu H, She W, Zhang J, et al. (2010) Hepatitis B virus (HBV) surface antigen interacts with and promotes cyclophilin a secretion: possible link to pathogenesis of HBV infection. J Virol 84: 3373-3381.
    • (2010) J Virol , vol.84 , pp. 3373-3381
    • Tian, X.1    Zhao, C.2    Zhu, H.3    She, W.4    Zhang, J.5
  • 43
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: unpredicted non-ER locations and functions
    • Turano C, Coppari S, Altieri F, Ferraro A, (2002) Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 193: 154-163.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 44
    • 84859085046 scopus 로고    scopus 로고
    • Endothelial cell surface expression of protein disulfide isomerase activates beta1 and beta3 integrins and facilitates dengue virus infection
    • Wan SW, Lin CF, Lu YT, Lei HY, Anderson R, et al. (2012) Endothelial cell surface expression of protein disulfide isomerase activates beta1 and beta3 integrins and facilitates dengue virus infection. J Cell Biochem 113: 1681-1691.
    • (2012) J Cell Biochem , vol.113 , pp. 1681-1691
    • Wan, S.W.1    Lin, C.F.2    Lu, Y.T.3    Lei, H.Y.4    Anderson, R.5
  • 45
    • 0029950355 scopus 로고    scopus 로고
    • Expression, subcellular distribution and plasma membrane binding of cathepsin B and gelatinases in bone metastatic tissue
    • Arkona C, Wiederanders B, (1996) Expression, subcellular distribution and plasma membrane binding of cathepsin B and gelatinases in bone metastatic tissue. Biol Chem 377: 695-702.
    • (1996) Biol Chem , vol.377 , pp. 695-702
    • Arkona, C.1    Wiederanders, B.2
  • 46
    • 0017255236 scopus 로고
    • Interaction of human cathepsin D with the inhibitor pepstatin
    • Knight CG, Barrett AJ, (1976) Interaction of human cathepsin D with the inhibitor pepstatin. Biochem J 155: 117-125.
    • (1976) Biochem J , vol.155 , pp. 117-125
    • Knight, C.G.1    Barrett, A.J.2
  • 47
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: insights into their divergence and evolution
    • Chen B, Piel WH, Gui L, Bruford E, Monteiro A, (2005) The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86: 627-637.
    • (2005) Genomics , vol.86 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Monteiro, A.5
  • 48
    • 0035901097 scopus 로고    scopus 로고
    • HBV-specific peptide associated with heat-shock protein gp96
    • Meng SD, Gao T, Gao GF, Tien P, (2001) HBV-specific peptide associated with heat-shock protein gp96. Lancet 357: 528-529.
    • (2001) Lancet , vol.357 , pp. 528-529
    • Meng, S.D.1    Gao, T.2    Gao, G.F.3    Tien, P.4
  • 49
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM, (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 50
    • 0035844136 scopus 로고    scopus 로고
    • Stable association of hsp90 and p23, but Not hsp70, with active human telomerase
    • Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE, (2001) Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem 276: 15571-15574.
    • (2001) J Biol Chem , vol.276 , pp. 15571-15574
    • Forsythe, H.L.1    Jarvis, J.L.2    Turner, J.W.3    Elmore, L.W.4    Holt, S.E.5
  • 52
    • 0030936089 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2
    • Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, et al. (1997) Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis 18: 588-598.
    • (1997) Electrophoresis , vol.18 , pp. 588-598
    • Rasmussen, R.K.1    Ji, H.2    Eddes, J.S.3    Moritz, R.L.4    Reid, G.E.5
  • 53
    • 84863447582 scopus 로고    scopus 로고
    • Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cells
    • Sokolowska I, Woods AG, Gawinowicz MA, Roy U, Darie CC, (2012) Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cells. FEBS J 279: 2579-2594.
    • (2012) FEBS J , vol.279 , pp. 2579-2594
    • Sokolowska, I.1    Woods, A.G.2    Gawinowicz, M.A.3    Roy, U.4    Darie, C.C.5
  • 54
    • 84855854555 scopus 로고    scopus 로고
    • Identification of potential tumor differentiation factor (TDF) receptor from steroid-responsive and steroid-resistant breast cancer cells
    • Sokolowska I, Woods AG, Gawinowicz MA, Roy U, Darie CC, (2012) Identification of potential tumor differentiation factor (TDF) receptor from steroid-responsive and steroid-resistant breast cancer cells. J Biol Chem 287: 1719-1733.
    • (2012) J Biol Chem , vol.287 , pp. 1719-1733
    • Sokolowska, I.1    Woods, A.G.2    Gawinowicz, M.A.3    Roy, U.4    Darie, C.C.5
  • 55
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y, Oda Y, Tabata T, Sato T, Nagasu T, et al. (2005) Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4: 1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.