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Volumn 1804, Issue 9, 2010, Pages 1869-1881

Proteomic analysis of the transitional endoplasmic reticulum in hepatocellular carcinoma: An organelle perspective on cancer

Author keywords

Cancer biomarker; Hepatocellular carcinoma; Quantitative organelle proteomics; Transitional endoplasmic reticulum

Indexed keywords

AFLATOXIN B1; BASIC TRANSCRIPTION FACTOR 3; CALRETICULIN; CYTOCHROME P450; DYNACTIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE ASSOCIATED PROGESTERONE RECEPTOR COMPONENT 1; MEMBRANE PROTEIN; MYC PROTEIN; NUCLEOLIN; NUCLEOPHOSMIN; PEPTIDE HYDROLASE; PROTEASOME; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PUR BETA; TRIPEPTIDYL PEPTIDASE II; TUMOR MARKER; UBIQUITIN; UNCLASSIFIED DRUG; POISON; PROTEOME;

EID: 77955093828     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.05.008     Document Type: Article
Times cited : (39)

References (121)
  • 1
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann O., Walz B. Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int. Rev. Cytol. 2001, 205:149-214.
    • (2001) Int. Rev. Cytol. , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 2
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata Y., Voeltz G.K., Rapoport T.A. Rough sheets and smooth tubules. Cell 2006, 126:435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 3
    • 39149109255 scopus 로고    scopus 로고
    • Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data
    • Lavoie C., Paiement J. Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data. Histochem. Cell Biol. 2008, 129:117-128.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 117-128
    • Lavoie, C.1    Paiement, J.2
  • 4
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S., Papa F.R., Walter P. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 2006, 22:487-508.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 5
    • 54949135707 scopus 로고    scopus 로고
    • The endoplasmic reticulum in apoptosis and autophagy: role of the BCL-2 protein family
    • Heath-Engel H.M., Chang N.C., Shore G.C. The endoplasmic reticulum in apoptosis and autophagy: role of the BCL-2 protein family. Oncogene 2008, 27:6419-6433.
    • (2008) Oncogene , vol.27 , pp. 6419-6433
    • Heath-Engel, H.M.1    Chang, N.C.2    Shore, G.C.3
  • 6
    • 77953028045 scopus 로고    scopus 로고
    • Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell
    • Stolz A., Wolf D.H. Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell. Biochim. Biophys. Acta 2010, 1803:694-705.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 694-705
    • Stolz, A.1    Wolf, D.H.2
  • 9
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D., Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 2009, 428:438-444.
    • (2009) Nature , vol.428 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 11
    • 0035888074 scopus 로고    scopus 로고
    • Estimating the world cancer burden: Globocan 2000
    • Parkin D.M., Bray F., Ferlay J., Pisani P. Estimating the world cancer burden: Globocan 2000. Int. J. Cancer 2001, 94:153-156.
    • (2001) Int. J. Cancer , vol.94 , pp. 153-156
    • Parkin, D.M.1    Bray, F.2    Ferlay, J.3    Pisani, P.4
  • 12
    • 33747830764 scopus 로고    scopus 로고
    • Hepatocellular carcinoma pathogenesis: from genes to environment
    • Farazi P.A., DePinho R.A. Hepatocellular carcinoma pathogenesis: from genes to environment. Nat. Rev. Cancer 2006, 6:674-687.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 674-687
    • Farazi, P.A.1    DePinho, R.A.2
  • 13
    • 77953237514 scopus 로고    scopus 로고
    • Global burden of aflatoxin-induced hepatocellular carcinoma: a risk assessment, Environ
    • Liu Y., Wu F. Global burden of aflatoxin-induced hepatocellular carcinoma: a risk assessment, Environ. Health Perspect. 2010, 118:818-824.
    • (2010) Health Perspect. , vol.118 , pp. 818-824
    • Liu, Y.1    Wu, F.2
  • 14
    • 65949095045 scopus 로고    scopus 로고
    • Asia-Pacific Working Party for Prevention of Hepatocellular Carcinoma, prevention of hepatocellular carcinoma in nonviral-related liver diseases
    • Fan J.G., Farrell G.C. Asia-Pacific Working Party for Prevention of Hepatocellular Carcinoma, prevention of hepatocellular carcinoma in nonviral-related liver diseases. J. Gastroenterol. Hepatol. 2009, 24:712-719.
    • (2009) J. Gastroenterol. Hepatol. , vol.24 , pp. 712-719
    • Fan, J.G.1    Farrell, G.C.2
  • 15
    • 77955095296 scopus 로고
    • Ultrastructure of hepatic neoplasia
    • MIT Press, Cambridge, W.H. Butler, P. Newberne (Eds.)
    • Butler W.H., Jones G. Ultrastructure of hepatic neoplasia. Rat Hepatic Neoplasia 1978, 142-179. MIT Press, Cambridge. W.H. Butler, P. Newberne (Eds.).
    • (1978) Rat Hepatic Neoplasia , pp. 142-179
    • Butler, W.H.1    Jones, G.2
  • 17
    • 0014654986 scopus 로고
    • Carcinogenesis in rats by aflatoxins B1, G1, and B2
    • Butler W.H., Greenblatt M., Lijinsky W. Carcinogenesis in rats by aflatoxins B1, G1, and B2. Cancer Res. 1969, 29:2206-2211.
    • (1969) Cancer Res. , vol.29 , pp. 2206-2211
    • Butler, W.H.1    Greenblatt, M.2    Lijinsky, W.3
  • 18
    • 0025768818 scopus 로고
    • GTP-dependent membrane fusion during hepatocarcinogenesis and liver regeneration
    • Paiement J., Dominguez J.M., Guenette A., Roy L. GTP-dependent membrane fusion during hepatocarcinogenesis and liver regeneration. Biochem. Biophys. Res. Commun. 1991, 176:1494-1500.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1494-1500
    • Paiement, J.1    Dominguez, J.M.2    Guenette, A.3    Roy, L.4
  • 19
    • 0028872860 scopus 로고
    • Changes in GTP-dependent fusion and ras-related proteins in membranes from rat hepatocellular carcinomas
    • Lanoix J., Paiement J. Changes in GTP-dependent fusion and ras-related proteins in membranes from rat hepatocellular carcinomas. Cancer Lett. 1995, 98:1-8.
    • (1995) Cancer Lett. , vol.98 , pp. 1-8
    • Lanoix, J.1    Paiement, J.2
  • 20
    • 77955093050 scopus 로고
    • Light microscopy of rat hepatic neoplasia
    • MIT Press, Cambridge, W.H. Butler, P. Newberne (Eds.)
    • Jones G., Butler W.H. Light microscopy of rat hepatic neoplasia. Rat Hepatic Neoplasia 1978, 115-140. MIT Press, Cambridge. W.H. Butler, P. Newberne (Eds.).
    • (1978) Rat Hepatic Neoplasia , pp. 115-140
    • Jones, G.1    Butler, W.H.2
  • 21
    • 84884891118 scopus 로고    scopus 로고
    • Isolation of rough and smooth membrane domains of the endoplasmic reticulum from rat liver
    • Elsevier Science, J.E. Celis (Ed.)
    • Paiement J., Young R., Roy L., Bergeron J.J.M. Isolation of rough and smooth membrane domains of the endoplasmic reticulum from rat liver. Cell Biology: A Laboratory Handbook 2006, Vol. 2:41-44. Elsevier Science. 3rd ed. J.E. Celis (Ed.).
    • (2006) Cell Biology: A Laboratory Handbook , vol.2 , pp. 41-44
    • Paiement, J.1    Young, R.2    Roy, L.3    Bergeron, J.J.M.4
  • 23
    • 0029954633 scopus 로고    scopus 로고
    • Cell-free assembly of rough and smooth endoplasmic reticulum
    • Lavoie C., Lanoix J., Kan F.W., Paiement J. Cell-free assembly of rough and smooth endoplasmic reticulum. J. Cell Sci. 1996, 109:1415-1425.
    • (1996) J. Cell Sci. , vol.109 , pp. 1415-1425
    • Lavoie, C.1    Lanoix, J.2    Kan, F.W.3    Paiement, J.4
  • 29
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., Yates J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76:4193-4201.
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 31
    • 0014050602 scopus 로고
    • Electron microscopic examination of subcellular fractions. I. The preparation of representative samples from suspensions of particles
    • Baudhuin P., Evrard P., Berthet J. Electron microscopic examination of subcellular fractions. I. The preparation of representative samples from suspensions of particles. J. Cell Biol. 1967, 32:181-191.
    • (1967) J. Cell Biol. , vol.32 , pp. 181-191
    • Baudhuin, P.1    Evrard, P.2    Berthet, J.3
  • 32
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles
    • Morisseau C., Hammock B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 2005, 45:311-333.
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 33
    • 0026050723 scopus 로고
    • Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1
    • Hayes J.D., Judah D.J., McLellan L.I., Neal G.E. Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1. Pharmacol. Ther. 1991, 50:443-472.
    • (1991) Pharmacol. Ther. , vol.50 , pp. 443-472
    • Hayes, J.D.1    Judah, D.J.2    McLellan, L.I.3    Neal, G.E.4
  • 34
    • 0034651240 scopus 로고    scopus 로고
    • Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver
    • Kelly V.P., Ellis E.M., Manson M.M., Chanas S.A., Moffat G.J., McLeod R., Judah D.J., Neal G.E., Hayes J.D. Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver. Cancer Res. 2000, 60:957-969.
    • (2000) Cancer Res. , vol.60 , pp. 957-969
    • Kelly, V.P.1    Ellis, E.M.2    Manson, M.M.3    Chanas, S.A.4    Moffat, G.J.5    McLeod, R.6    Judah, D.J.7    Neal, G.E.8    Hayes, J.D.9
  • 37
    • 33749263503 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray
    • Hu R., Xu C., Shen G., Jain M.R., Khor T.O., Gopalkrishnan A., Lin W., Reddy B., Chan J.Y., Kong A.N. Identification of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray. Life Sci. 2006, 79:1944-1955.
    • (2006) Life Sci. , vol.79 , pp. 1944-1955
    • Hu, R.1    Xu, C.2    Shen, G.3    Jain, M.R.4    Khor, T.O.5    Gopalkrishnan, A.6    Lin, W.7    Reddy, B.8    Chan, J.Y.9    Kong, A.N.10
  • 40
    • 33646806787 scopus 로고    scopus 로고
    • Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action
    • Peluso J.J., Pappalardo A., Losel R., Wehling M. Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action. Endocrinology 2006, 147:3133-3140.
    • (2006) Endocrinology , vol.147 , pp. 3133-3140
    • Peluso, J.J.1    Pappalardo, A.2    Losel, R.3    Wehling, M.4
  • 43
    • 43249120558 scopus 로고    scopus 로고
    • Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component-1
    • Peluso J.J., Liu X., Saunders M.M., Claffey K.P., Phoenix K. Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component-1. J. Clin. Endocrinol. Metab. 2008, 93:1592-1599.
    • (2008) J. Clin. Endocrinol. Metab. , vol.93 , pp. 1592-1599
    • Peluso, J.J.1    Liu, X.2    Saunders, M.M.3    Claffey, K.P.4    Phoenix, K.5
  • 44
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII
    • Kloetzel P.M. Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII. Nat. Immunol. 2004, 5:661-669.
    • (2004) Nat. Immunol. , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 45
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment
    • Raposo G., van Santen H.M., Leijendekker R., Geuze H.J., Ploegh H.L. Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 1995, 131:1403-1419.
    • (1995) J. Cell Biol. , vol.131 , pp. 1403-1419
    • Raposo, G.1    van Santen, H.M.2    Leijendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 46
    • 4644247806 scopus 로고    scopus 로고
    • Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice
    • Zuber C., Fan J.Y., Guhl B., Roth J. Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice. FASEB J. 2004, 18:917-919.
    • (2004) FASEB J. , vol.18 , pp. 917-919
    • Zuber, C.1    Fan, J.Y.2    Guhl, B.3    Roth, J.4
  • 48
    • 58249095936 scopus 로고    scopus 로고
    • PCPH/ENTPD5 expression confers to prostate cancer cells resistance against cisplatin-induced apoptosis through protein kinase Calpha-mediated Bcl-2 stabilization
    • Villar J., Quadri H.S., Song I., Tomita Y., Tirado O.M., Notario V. PCPH/ENTPD5 expression confers to prostate cancer cells resistance against cisplatin-induced apoptosis through protein kinase Calpha-mediated Bcl-2 stabilization. Cancer Res. 2009, 69:102-110.
    • (2009) Cancer Res. , vol.69 , pp. 102-110
    • Villar, J.1    Quadri, H.S.2    Song, I.3    Tomita, Y.4    Tirado, O.M.5    Notario, V.6
  • 50
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: linking Ca2+ signalling to membrane dynamics
    • Gerke V., Creutz C.E., Moss S.E. Annexins: linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell Biol. 2005, 6:449-461.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 51
    • 0036351802 scopus 로고    scopus 로고
    • Annexin 2 "secretion" accompanying exocytosis of chromaffin cells: possible mechanisms of annexin release
    • Faure A.V., Migne C., Devilliers G., Ayala-Sanmartin J. Annexin 2 "secretion" accompanying exocytosis of chromaffin cells: possible mechanisms of annexin release. Exp. Cell Res. 2002, 276:79-89.
    • (2002) Exp. Cell Res. , vol.276 , pp. 79-89
    • Faure, A.V.1    Migne, C.2    Devilliers, G.3    Ayala-Sanmartin, J.4
  • 52
    • 70349778596 scopus 로고    scopus 로고
    • Membrane biogenesis: networking at the ER with atlastin
    • Farhan H., Hauri H.P. Membrane biogenesis: networking at the ER with atlastin. Curr. Biol. 2009, 13:R906-R908.
    • (2009) Curr. Biol. , vol.13
    • Farhan, H.1    Hauri, H.P.2
  • 56
    • 12344277564 scopus 로고    scopus 로고
    • Coupling of ER exit to microtubules through direct interaction of COPII with dynactin
    • Watson P., Forster R., Palmer K.J., Pepperkok R., Stephens D.J. Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat. Cell Biol. 2005, 7:48-55.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 48-55
    • Watson, P.1    Forster, R.2    Palmer, K.J.3    Pepperkok, R.4    Stephens, D.J.5
  • 57
    • 33750534358 scopus 로고    scopus 로고
    • The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A
    • Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M. The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A. Mol. Biol. Cell 2006, 17:4876-4887.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4876-4887
    • Yamasaki, A.1    Tani, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 59
    • 0038387865 scopus 로고    scopus 로고
    • Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23
    • Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat. Cell Biol. 2003, 5:661-667.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 661-667
    • Cohen, M.1    Stutz, F.2    Belgareh, N.3    Haguenauer-Tsapis, R.4    Dargemont, C.5
  • 60
    • 0035963292 scopus 로고    scopus 로고
    • Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease
    • Soncini C., Berdo I., Draetta G. Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease. Oncogene 2001, 20:3869-3879.
    • (2001) Oncogene , vol.20 , pp. 3869-3879
    • Soncini, C.1    Berdo, I.2    Draetta, G.3
  • 61
    • 0021690458 scopus 로고
    • Binding of ATP citrate lyase to the microsomal fraction of rat liver
    • Linn T.C., Srere P.A. Binding of ATP citrate lyase to the microsomal fraction of rat liver. J. Biol. Chem. 1984, 259:13379-13384.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13379-13384
    • Linn, T.C.1    Srere, P.A.2
  • 64
    • 0035161710 scopus 로고    scopus 로고
    • Localization of glucose-6-phosphate dehydrogenase activity on ribosomes of granular endoplasmic reticulum, in peroxisomes and peripheral cytoplasm of rat liver parenchymal cells
    • Frederiks W.M., Vreeling-Sindelarova H. Localization of glucose-6-phosphate dehydrogenase activity on ribosomes of granular endoplasmic reticulum, in peroxisomes and peripheral cytoplasm of rat liver parenchymal cells. Histochem. J. 2001, 33:345-353.
    • (2001) Histochem. J. , vol.33 , pp. 345-353
    • Frederiks, W.M.1    Vreeling-Sindelarova, H.2
  • 65
    • 0031847686 scopus 로고    scopus 로고
    • Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum
    • Benlimame N., Le P.U., Nabi I.R. Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol. Biol. Cell 1998, 9:1773-1786.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1773-1786
    • Benlimame, N.1    Le, P.U.2    Nabi, I.R.3
  • 66
    • 0037224507 scopus 로고    scopus 로고
    • Overexpression of the autocrine motility factor/phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts
    • Tsutsumi S., Hogan V., Nabi I.R., Raz A. Overexpression of the autocrine motility factor/phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts. Cancer Res. 2003, 63:242-249.
    • (2003) Cancer Res. , vol.63 , pp. 242-249
    • Tsutsumi, S.1    Hogan, V.2    Nabi, I.R.3    Raz, A.4
  • 67
    • 37549032762 scopus 로고    scopus 로고
    • Down-regulation of phosphoglucose isomerase/autocrine motility factor expression sensitizes human fibrosarcoma cells to oxidative stress leading to cellular senescence
    • Funasaka T., Hu H., Hogan V., Raz A. Down-regulation of phosphoglucose isomerase/autocrine motility factor expression sensitizes human fibrosarcoma cells to oxidative stress leading to cellular senescence. J. Biol. Chem. 2007, 282:36362-36369.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36362-36369
    • Funasaka, T.1    Hu, H.2    Hogan, V.3    Raz, A.4
  • 68
    • 70350164417 scopus 로고    scopus 로고
    • How and why does the endoplasmic reticulum move?
    • Bola B., Allan V. How and why does the endoplasmic reticulum move?. Biochem. Soc. Trans. 2009, 37:961-965.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 961-965
    • Bola, B.1    Allan, V.2
  • 71
    • 0032476663 scopus 로고    scopus 로고
    • A novel direct interaction of endoplasmic reticulum with microtubules
    • Klopfenstein D.R., Kappeler F., Hauri H.P. A novel direct interaction of endoplasmic reticulum with microtubules. EMBO J. 1998, 17:6168-6177.
    • (1998) EMBO J. , vol.17 , pp. 6168-6177
    • Klopfenstein, D.R.1    Kappeler, F.2    Hauri, H.P.3
  • 73
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G., Kim V., Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 2002, 3:195-205.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.2    Kataoka, N.3
  • 74
    • 35648963627 scopus 로고    scopus 로고
    • Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues
    • Sun W., Xing B., Sun Y., Du X., Lu M., Hao C., Lu Z., Mi W., Wu S., Wei H., Gao X., Zhu Y., Jiang Y., Qian X., He F. Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues. Mol. Cell. Proteomics 2007, 6:1798-1808.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1798-1808
    • Sun, W.1    Xing, B.2    Sun, Y.3    Du, X.4    Lu, M.5    Hao, C.6    Lu, Z.7    Mi, W.8    Wu, S.9    Wei, H.10    Gao, X.11    Zhu, Y.12    Jiang, Y.13    Qian, X.14    He, F.15
  • 75
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes
    • Visa N., Alzhanova-Ericsson A.T., Sun X., Kiseleva E., Bjorkroth B., Wurtz T., Daneholt B. A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell 1996, 84:253-264.
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1    Alzhanova-Ericsson, A.T.2    Sun, X.3    Kiseleva, E.4    Bjorkroth, B.5    Wurtz, T.6    Daneholt, B.7
  • 77
    • 27744569843 scopus 로고    scopus 로고
    • MTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz M.K., Ballif B.A., Gygi S.P., Blenis J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 2005, 123:569-580.
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 78
    • 33947145667 scopus 로고    scopus 로고
    • Endoplasmic reticulum and Golgi localization sequences for mammalian target of rapamycin
    • Liu X., Zheng X.F. Endoplasmic reticulum and Golgi localization sequences for mammalian target of rapamycin. Mol. Biol. Cell 2007, 18:1073-1082.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1073-1082
    • Liu, X.1    Zheng, X.F.2
  • 79
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin D.A., Sabatini D.M. Defining the role of mTOR in cancer. Cancer Cell 2007, 12:9-22.
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 83
    • 33746353084 scopus 로고    scopus 로고
    • The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation
    • Messias A.C., Harnisch C., Ostareck-Lederer A., Sattler M., Ostareck D.H. The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation. J. Mol. Biol. 2006, 361:470-481.
    • (2006) J. Mol. Biol. , vol.361 , pp. 470-481
    • Messias, A.C.1    Harnisch, C.2    Ostareck-Lederer, A.3    Sattler, M.4    Ostareck, D.H.5
  • 84
    • 66349107721 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase is regulated through c-Src-mediated tyrosine phosphorylation in endothelial cells
    • Pan S., World C.J., Kovacs C.J., Berk B.C. Glucose 6-phosphate dehydrogenase is regulated through c-Src-mediated tyrosine phosphorylation in endothelial cells. Arterioscler. Thromb. Vasc. Biol. 2009, 29:895-901.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 895-901
    • Pan, S.1    World, C.J.2    Kovacs, C.J.3    Berk, B.C.4
  • 85
    • 37448999546 scopus 로고    scopus 로고
    • Ribosomal stress induces processing of Mybbp1a and its translocation from the nucleolus to the nucleoplasm
    • Yamauchi T., Keough R.A., Gonda T.J., Ishii S. Ribosomal stress induces processing of Mybbp1a and its translocation from the nucleolus to the nucleoplasm. Genes Cells 2008, 13:27-39.
    • (2008) Genes Cells , vol.13 , pp. 27-39
    • Yamauchi, T.1    Keough, R.A.2    Gonda, T.J.3    Ishii, S.4
  • 87
    • 0037197962 scopus 로고    scopus 로고
    • Characterization of the c-MYC-regulated transcriptome by SAGE: identification and analysis of c-MYC target genes
    • Menssen A., Hermeking H. Characterization of the c-MYC-regulated transcriptome by SAGE: identification and analysis of c-MYC target genes. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:6274-6279.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6274-6279
    • Menssen, A.1    Hermeking, H.2
  • 88
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-kappaB transcription factors. Oncogene 1999, 18:6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 90
    • 33746713687 scopus 로고    scopus 로고
    • CYP4B1: an enigmatic P450 at the interface between xenobiotic and endobiotic metabolism
    • Baer B.R., Rettie A.E. CYP4B1: an enigmatic P450 at the interface between xenobiotic and endobiotic metabolism. Drug Metab. Rev. 2006, 38:451-476.
    • (2006) Drug Metab. Rev. , vol.38 , pp. 451-476
    • Baer, B.R.1    Rettie, A.E.2
  • 92
    • 2942560784 scopus 로고    scopus 로고
    • Effect of hypoxia on cytochrome P450 activity and expression
    • Fradette C., Du Souich P. Effect of hypoxia on cytochrome P450 activity and expression. Curr. Drug Metab. 2004, 5:257-271.
    • (2004) Curr. Drug Metab. , vol.5 , pp. 257-271
    • Fradette, C.1    Du Souich, P.2
  • 93
    • 63049110388 scopus 로고    scopus 로고
    • Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type specific functions
    • Pan C., Kumar C., Bohl S., Klingmueller U., Mann M. Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type specific functions. Mol. Cell. Proteomics 2008, 8:443-450.
    • (2008) Mol. Cell. Proteomics , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3    Klingmueller, U.4    Mann, M.5
  • 94
    • 67749114265 scopus 로고    scopus 로고
    • CYP2D6 and tamoxifen: DNA matters in breast cancer
    • Hoskins J.M., Carey L.A., McLeod H.L. CYP2D6 and tamoxifen: DNA matters in breast cancer. Nat. Rev. Cancer 2009, 9:576-586.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 576-586
    • Hoskins, J.M.1    Carey, L.A.2    McLeod, H.L.3
  • 95
    • 34249930470 scopus 로고    scopus 로고
    • Targeting cytochrome P450 enzymes: a new approach in anti-cancer drug development
    • Bruno R.D., Njar V.C. Targeting cytochrome P450 enzymes: a new approach in anti-cancer drug development. Bioorg. Med. Chem. 2007, 15:5047-5060.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 5047-5060
    • Bruno, R.D.1    Njar, V.C.2
  • 96
    • 16544394847 scopus 로고    scopus 로고
    • Overexpression of regucalcin suppresses cell death in cloned rat hepatoma H4-II-E cells induced by tumor necrosis factor-alpha or thapsigargin
    • Izumi T., Yamaguchi M. Overexpression of regucalcin suppresses cell death in cloned rat hepatoma H4-II-E cells induced by tumor necrosis factor-alpha or thapsigargin. J. Cell. Biochem. 2004, 92:296-306.
    • (2004) J. Cell. Biochem. , vol.92 , pp. 296-306
    • Izumi, T.1    Yamaguchi, M.2
  • 98
    • 33745728461 scopus 로고    scopus 로고
    • Fatty acid synthase and cancer: new application of an old pathway
    • Kuhajda F.P. Fatty acid synthase and cancer: new application of an old pathway. Cancer Res. 2006, 66:5977-5980.
    • (2006) Cancer Res. , vol.66 , pp. 5977-5980
    • Kuhajda, F.P.1
  • 104
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner M., Pluquet O., Bouchecareilh M., Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res. 2007, 67:10631-10634.
    • (2007) Cancer Res. , vol.67 , pp. 10631-10634
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 109
    • 34247146913 scopus 로고    scopus 로고
    • The final touches make perfect the Peptide-MHC Class I repertoire
    • Hammer G.E., Kanaseki T., Shastri N. The final touches make perfect the Peptide-MHC Class I repertoire. Immunity 2007, 26:397-406.
    • (2007) Immunity , vol.26 , pp. 397-406
    • Hammer, G.E.1    Kanaseki, T.2    Shastri, N.3
  • 110
  • 111
    • 11144286431 scopus 로고    scopus 로고
    • Coordinated downregulation of the antigen presentation machinery and HLA class I/beta2-microglobulin complex is responsible for HLA-ABC loss in bladder cancer
    • Romero J.M., Jimenez P., Cabrera T., Cozar J.M., Pedrinaci S., Tallada M., Garrido F., Ruiz-Cabello F. Coordinated downregulation of the antigen presentation machinery and HLA class I/beta2-microglobulin complex is responsible for HLA-ABC loss in bladder cancer. Int. J. Cancer 2005, 113:605-610.
    • (2005) Int. J. Cancer , vol.113 , pp. 605-610
    • Romero, J.M.1    Jimenez, P.2    Cabrera, T.3    Cozar, J.M.4    Pedrinaci, S.5    Tallada, M.6    Garrido, F.7    Ruiz-Cabello, F.8
  • 119
    • 0023003549 scopus 로고
    • Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA
    • Kedersha N.L., Rome L.H. Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA. J. Cell Biol. 1986, 103:699-709.
    • (1986) J. Cell Biol. , vol.103 , pp. 699-709
    • Kedersha, N.L.1    Rome, L.H.2
  • 121
    • 44449147036 scopus 로고    scopus 로고
    • Tumor cell metabolism: cancer's Achilles' heel
    • Kroemer G., Pouyssegur J. Tumor cell metabolism: cancer's Achilles' heel. Cancer Cell 2008, 13:472-482.
    • (2008) Cancer Cell , vol.13 , pp. 472-482
    • Kroemer, G.1    Pouyssegur, J.2


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