메뉴 건너뛰기




Volumn 13, Issue 8, 2013, Pages 895-904

Significance of prion and prion-like proteins in cancer development, progression and multi-drug resistance

Author keywords

Epigenetic; PRND; PRNP; Protein misfolding; Tumour marker

Indexed keywords

DOPPEL PROTEIN; FILAMIN A; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE; PRION PROTEIN; PROTEIN P53; SUPEROXIDE DISMUTASE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84888112524     PISSN: 15680096     EISSN: 18735576     Source Type: Journal    
DOI: 10.2174/156800961131300092     Document Type: Review
Times cited : (17)

References (81)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer. Cell 2000, 100 (1), 57-70.
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 0037370476 scopus 로고    scopus 로고
    • The genetics and genomics of cancer
    • Balmain, A.; Gray, J.; Ponder, B., The genetics and genomics of cancer. Nat Genet 2003, 33 (Suppl), 238-244.
    • (2003) Nat Genet , vol.33 , Issue.SUPPL. , pp. 238-244
    • Balmain, A.1    Gray, J.2    Ponder, B.3
  • 4
    • 84888126813 scopus 로고    scopus 로고
    • The structure and function of cells
    • In:, Rhoades, R.; Pflanzer, R.; Ed. Thomson learning inc.: USA
    • Pavalko, F. The structure and function of cells. In: Human Physiology 4th edition. Rhoades, R.; Pflanzer, R.; Ed. Thomson learning inc.: USA, 2003; pp 67-107.
    • (2003) Human Physiology 4th edition , pp. 67-107
    • Pavalko, F.1
  • 5
    • 77953359996 scopus 로고    scopus 로고
    • Anti-PrP antibodies detected at terminal stage of prion-affected mouse
    • Sassa, Y.; Kataoka, N.; Inoshima, Y.; Ishiguro, N. Anti-PrP antibodies detected at terminal stage of prion-affected mouse. Cell Immunol. 2010, 263 (2), 212-218.
    • (2010) Cell Immunol , vol.263 , Issue.2 , pp. 212-218
    • Sassa, Y.1    Kataoka, N.2    Inoshima, Y.3    Ishiguro, N.4
  • 6
    • 77549087970 scopus 로고    scopus 로고
    • Prion protein: From physiology to cancer biology
    • Mehrpour, M.; Codogno, P. Prion protein: From physiology to cancer biology. Cancer Lett. 2010, 290 (1), 1-23.
    • (2010) Cancer Lett , vol.290 , Issue.1 , pp. 1-23
    • Mehrpour, M.1    Codogno, P.2
  • 8
    • 34347398043 scopus 로고    scopus 로고
    • Cellular prion protein promotes proliferation and G1/S transition of human gastric cancer cells SGC7901 and AGS
    • Liang, J.; Pan, Y.; Zhang, D.; Guo, C.; Shi, Y.; Wang, J.; Chen, Y.; Wang, X.; Liu, J.; Guo, X.; Chen, Z.; Qiao, T.; Fan, D. Cellular prion protein promotes proliferation and G1/S transition of human gastric cancer cells SGC7901 and AGS. FASEB J. 2007, 21 (9), 2247-2256.
    • (2007) FASEB J , vol.21 , Issue.9 , pp. 2247-2256
    • Liang, J.1    Pan, Y.2    Zhang, D.3    Guo, C.4    Shi, Y.5    Wang, J.6    Chen, Y.7    Wang, X.8    Liu, J.9    Guo, X.10    Chen, Z.11    Qiao, T.12    Fan, D.13
  • 14
    • 10344251498 scopus 로고    scopus 로고
    • Overexpression and significance of prion protein in gastric cancer and multidrug-resistant gastric carcinoma cell line SGC7901/ADR
    • Du, J.; Pan, Y.; Shi, Y.; Guo, C.; Jin, X.; Sun, L.; Liu, N.; Qiao, T.; Fan, D. Overexpression and significance of prion protein in gastric cancer and multidrug-resistant gastric carcinoma cell line SGC7901/ADR. Int. J. Cancer 2005, 113 (2), 213-220.
    • (2005) Int. J. Cancer , vol.113 , Issue.2 , pp. 213-220
    • Du, J.1    Pan, Y.2    Shi, Y.3    Guo, C.4    Jin, X.5    Sun, L.6    Liu, N.7    Qiao, T.8    Fan, D.9
  • 16
    • 33846472404 scopus 로고    scopus 로고
    • Reversal of multidrug resistance of gastric cancer cells by downregulation of Akt1 with Akt1 siRNA
    • Han, Z.; Hong, L.; Wu, K.; Han, S.; Shen, H.; Liu, C.; Han, Y.; Liu, Z.; Fan, D. Reversal of multidrug resistance of gastric cancer cells by downregulation of Akt1 with Akt1 siRNA. J. Exp. Clin. Cancer Res. 2006, 25 (4), 601-606.
    • (2006) J. Exp. Clin. Cancer Res , vol.25 , Issue.4 , pp. 601-606
    • Han, Z.1    Hong, L.2    Wu, K.3    Han, S.4    Shen, H.5    Liu, C.6    Han, Y.7    Liu, Z.8    Fan, D.9
  • 17
    • 33746127253 scopus 로고
    • Über eine eigenartige herdförmige erkrankung des zentralnervensystems (Vorläufige mitteilung)
    • Creutzfeldt, H. Über eine eigenartige herdförmige erkrankung des zentralnervensystems (Vorläufige mitteilung). Z. f. d. g. Neuru. Psych. 1920, 57 (1), 1-18.
    • (1920) Z. f. d. g. Neuru. Psych , vol.57 , Issue.1 , pp. 1-18
    • Creutzfeldt, H.1
  • 18
    • 0032544725 scopus 로고    scopus 로고
    • Transmissible Spongiform Encephalopathies
    • Liemann, S.; Glockshuber, R. Transmissible Spongiform Encephalopathies. Biochem. Biophys. Res. Comm. 1998, 250 (2), 187-193.
    • (1998) Biochem. Biophys. Res. Comm , vol.250 , Issue.2 , pp. 187-193
    • Liemann, S.1    Glockshuber, R.2
  • 19
    • 0037184778 scopus 로고    scopus 로고
    • Fundamentals of prion biology and diseases
    • DeArmond, S. J.; Bouzamondo, E. Fundamentals of prion biology and diseases. Toxicology 2002, 181-182, 9-16.
    • (2002) Toxicology , vol.181-182 , pp. 9-16
    • DeArmond, S.J.1    Bouzamondo, E.2
  • 20
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216 (4542), 136-144.
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 25
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M.; Serpell, L. C.; Bartlam, M.; Fraser, P. E.; Pepys, M. B.; Blake, C. C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 1997, 273 (3), 729-739.
    • (1997) J. Mol. Biol , vol.273 , Issue.3 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.E.4    Pepys, M.B.5    Blake, C.C.6
  • 26
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin, P.; Melki, R.; Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 2010, 11 (4), 301-307.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , Issue.4 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 27
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi, A.; Rajendran, L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009, 64 (6), 783-790.
    • (2009) Neuron , vol.64 , Issue.6 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 29
    • 0036842066 scopus 로고    scopus 로고
    • PrPC is sorted to the basolateral membrane of epithelial cells independently of its association with rafts
    • Sarnataro, D.; Paladino, S.; Campana, V.; Grassi, J.; Nitsch, L.; Zurzolo, C. PrPC is sorted to the basolateral membrane of epithelial cells independently of its association with rafts. Traffic 2002, 3 (11), 810-821.
    • (2002) Traffic , vol.3 , Issue.11 , pp. 810-821
    • Sarnataro, D.1    Paladino, S.2    Campana, V.3    Grassi, J.4    Nitsch, L.5    Zurzolo, C.6
  • 30
    • 34548221936 scopus 로고    scopus 로고
    • Structural and hydration properties of the partially unfolded states of the prion protein
    • De Simone, A.; Zagari, A.; Derreumaux, P. Structural and hydration properties of the partially unfolded states of the prion protein. Biophys. J. 2007, 93 (4), 1284-1292.
    • (2007) Biophys. J , vol.93 , Issue.4 , pp. 1284-1292
    • De Simone, A.1    Zagari, A.2    Derreumaux, P.3
  • 31
    • 0036925662 scopus 로고    scopus 로고
    • Genomic characterization of the human prion protein (PrP) gene locus
    • Makrinou, E.; Collinge, J.; Antoniou, M. Genomic characterization of the human prion protein (PrP) gene locus. Mamm. Genome 2002, 13 (12), 696-703.
    • (2002) Mamm. Genome , vol.13 , Issue.12 , pp. 696-703
    • Makrinou, E.1    Collinge, J.2    Antoniou, M.3
  • 33
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • Stewart, R. S.; Harris, D. A. Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J. Biol. Chem. 2003, 278 (46), 45960-45968.
    • (2003) J. Biol. Chem , vol.278 , Issue.46 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 34
    • 0037031950 scopus 로고    scopus 로고
    • Intramolecular versus intermolecular disulfide bonds in prion proteins
    • Welker, E.; Raymond, L. D.; Scheraga, H. A.; Caughey, B. Intramolecular versus intermolecular disulfide bonds in prion proteins. J. Biol. Chem. 2002, 277 (36), 33477-33481.
    • (2002) J. Biol. Chem , vol.277 , Issue.36 , pp. 33477-33481
    • Welker, E.1    Raymond, L.D.2    Scheraga, H.A.3    Caughey, B.4
  • 35
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • Hooper, N. Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem. Soc. F. Trans. 2005, 33, 335-338.
    • (2005) Biochem. Soc. F. Trans , vol.33 , pp. 335-338
    • Hooper, N.1
  • 36
    • 1642410070 scopus 로고    scopus 로고
    • Alpha-and beta-cleavages of the amino-terminus of the cellular prion protein
    • Mange, A.; Beranger, F.; Peoc'h, K.; Onodera, T.; Frobert, Y.; Lehmann, S. Alpha-and beta-cleavages of the amino-terminus of the cellular prion protein. Biol Cell 2004, 96 (2), 125-132.
    • (2004) Biol Cell , vol.96 , Issue.2 , pp. 125-132
    • Mange, A.1    Beranger, F.2    Peoc'h, K.3    Onodera, T.4    Frobert, Y.5    Lehmann, S.6
  • 37
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • Vincent, B.; Paitel, E.; Frobert, Y.; Lehmann, S.; Grassi, J.; Checler, F. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J. Biol. Chem. 2000, 275 (45), 35612-35616.
    • (2000) J. Biol. Chem , vol.275 , Issue.45 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3    Lehmann, S.4    Grassi, J.5    Checler, F.6
  • 38
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • Jimenez-Huete, A.; Lievens, P. M.; Vidal, R.; Piccardo, P.; Ghetti, B.; Tagliavini, F.; Frangione, B.; Prelli, F. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am. J. Pathol. 1998, 153 (5), 1561-1572.
    • (1998) Am. J. Pathol , vol.153 , Issue.5 , pp. 1561-1572
    • Jimenez-Huete, A.1    Lievens, P.M.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6    Frangione, B.7    Prelli, F.8
  • 39
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan, K. M.; Stahl, N.; Prusiner, S. B. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1992, 1 (10), 1343-1352.
    • (1992) Protein Sci , vol.1 , Issue.10 , pp. 1343-1352
    • Pan, K.M.1    Stahl, N.2    Prusiner, S.B.3
  • 41
    • 27744547982 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress
    • Watt, N. T.; Taylor, D. R.; Gillott, A.; Thomas, D. A.; Perera, W. S.; Hooper, N. M. Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress. J. Biol. Chem. 2005, 280 (43), 35914-35921.
    • (2005) J. Biol. Chem , vol.280 , Issue.43 , pp. 35914-35921
    • Watt, N.T.1    Taylor, D.R.2    Gillott, A.3    Thomas, D.A.4    Perera, W.S.5    Hooper, N.M.6
  • 43
    • 84863713439 scopus 로고    scopus 로고
    • Unraveling the neuroprotective mechanisms of PrP (C) in excitotoxicity
    • Llorens, F.; Del Rio, J. A. Unraveling the neuroprotective mechanisms of PrP (C) in excitotoxicity. Prion 2012, 6 (3), 245-251.
    • (2012) Prion , vol.6 , Issue.3 , pp. 245-251
    • Llorens, F.1    Del Rio, J.A.2
  • 44
    • 34249936265 scopus 로고    scopus 로고
    • The cellular prion protein (PrP(C): Its physiological function and role in disease
    • Westergard, L.; Christensen, H. M.; Harris, D. A. The cellular prion protein (PrP(C): its physiological function and role in disease. Biochimica. Biophysica. Acta. 2007, 1772 (6), 629-644.
    • (2007) Biochimica. Biophysica. Acta , vol.1772 , Issue.6 , pp. 629-644
    • Westergard, L.1    Christensen, H.M.2    Harris, D.A.3
  • 48
    • 0034899833 scopus 로고    scopus 로고
    • Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum
    • Laine, J.; Marc, M. E.; Sy, M. S.; Axelrad, H. Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum. Eur. J. Neurosci. 2001, 14 (1), 47-56.
    • (2001) Eur. J. Neurosci , vol.14 , Issue.1 , pp. 47-56
    • Laine, J.1    Marc, M.E.2    Sy, M.S.3    Axelrad, H.4
  • 49
    • 3242717853 scopus 로고    scopus 로고
    • Differential expression of the prion-like protein doppel gene (PRND) in astrocytomas: A new molecular marker potentially involved in tumor progression
    • Comincini, S.; Facoetti, A.; Del Vecchio, I.; Peoc'h, K.; Laplanche, J. L.; Magrassi, L.; Ceroni, M.; Ferretti, L.; Nano, R. Differential expression of the prion-like protein doppel gene (PRND) in astrocytomas: a new molecular marker potentially involved in tumor progression. Anticancer Res. 2004, 24 (3a), 1507-1517.
    • (2004) Anticancer Res , vol.24 , Issue.3 A , pp. 1507-1517
    • Comincini, S.1    Facoetti, A.2    Del Vecchio, I.3    Peoc'h, K.4    Laplanche, J.L.5    Magrassi, L.6    Ceroni, M.7    Ferretti, L.8    Nano, R.9
  • 50
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil, D. P.; Park, J.; Hemmings, B. A. PKB binding proteins. Getting in on the Akt. Cell 2002, 111 (3), 293-303.
    • (2002) Cell , vol.111 , Issue.3 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 51
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco, I.; Sawyers, C. L. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat. Rev. Cancer 2002, 2 (7), 489-501.
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.7 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 52
    • 84863174749 scopus 로고    scopus 로고
    • Octarepeat peptides of prion are essential for multidrug resistance in gastric cancer cells
    • Wang, J. H.; Du, J. P.; Li, S. J.; Zhai, L. P.; Yang, X. Y.; Wang, Z. H.; Wu, Z. T.; Han, Y. Octarepeat peptides of prion are essential for multidrug resistance in gastric cancer cells. J. Dig. Dis. 2012, 13 (3), 143-152.
    • (2012) J. Dig. Dis , vol.13 , Issue.3 , pp. 143-152
    • Wang, J.H.1    Du, J.P.2    Li, S.J.3    Zhai, L.P.4    Yang, X.Y.5    Wang, Z.H.6    Wu, Z.T.7    Han, Y.8
  • 53
    • 0037191512 scopus 로고    scopus 로고
    • Differentially expressed gene profiles between multidrug resistant gastric adenocarcinoma cells and their parental cells
    • Zhao, Y.; You, H.; Liu, F.; An, H.; Shi, Y.; Yu, Q.; Fan, D. Differentially expressed gene profiles between multidrug resistant gastric adenocarcinoma cells and their parental cells. Cancer Lett. 2002, 185 (2), 211-218.
    • (2002) Cancer Lett , vol.185 , Issue.2 , pp. 211-218
    • Zhao, Y.1    You, H.2    Liu, F.3    An, H.4    Shi, Y.5    Yu, Q.6    Fan, D.7
  • 54
    • 0024779132 scopus 로고
    • P-glycoprotein: Multidrugresistance and a superfamily of membrane-associated transport proteins
    • Juranka, P. F.; Zastawny, R. L.; Ling, V. P-glycoprotein: multidrugresistance and a superfamily of membrane-associated transport proteins. FASEBJ 1989, 3 (14), 2583-2592.
    • (1989) FASEBJ , vol.3 , Issue.14 , pp. 2583-2592
    • Juranka, P.F.1    Zastawny, R.L.2    Ling, V.3
  • 55
    • 80054860599 scopus 로고    scopus 로고
    • Dynamic changes and surveillance function of prion protein expression in gastric cancer drug resistance
    • Wang, J. H.; Du, J. P.; Zhang, Y. H.; Zhao, X. J.; Fan, R. Y.; Wang, Z. H.; Wu, Z. T.; Han, Y. Dynamic changes and surveillance function of prion protein expression in gastric cancer drug resistance. World J. Gastroenterol. 2011, 17 (35), 3986-3993.
    • (2011) World J. Gastroenterol , vol.17 , Issue.35 , pp. 3986-3993
    • Wang, J.H.1    Du, J.P.2    Zhang, Y.H.3    Zhao, X.J.4    Fan, R.Y.5    Wang, Z.H.6    Wu, Z.T.7    Han, Y.8
  • 57
    • 0037093087 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in pancreatic cancer cells using cDNA microarray
    • Han, H.; Bearss, D. J.; Browne, L. W.; Calaluce, R.; Nagle, R. B.; Von Hoff, D. D. Identification of differentially expressed genes in pancreatic cancer cells using cDNA microarray. Cancer Res. 2002, 62 (10), 2890-2896.
    • (2002) Cancer Res , vol.62 , Issue.10 , pp. 2890-2896
    • Han, H.1    Bearss, D.J.2    Browne, L.W.3    Calaluce, R.4    Nagle, R.B.5    Von Hoff, D.D.6
  • 58
    • 77957552124 scopus 로고    scopus 로고
    • Binding of pro-prion to filamin A: By design or an unfortunate blunder
    • Li, C.; Xin, W.; Sy, M. S. Binding of pro-prion to filamin A: by design or an unfortunate blunder. Oncogene 2010, 29 (39), 5329-5345.
    • (2010) Oncogene , vol.29 , Issue.39 , pp. 5329-5345
    • Li, C.1    Xin, W.2    Sy, M.S.3
  • 59
    • 36349016768 scopus 로고    scopus 로고
    • Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death
    • Meslin, F.; Hamai, A.; Gao, P.; Jalil, A.; Cahuzac, N.; Chouaib, S.; Mehrpour, M. Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death. Cancer Res. 2007, 67 (22), 10910-10919.
    • (2007) Cancer Res , vol.67 , Issue.22 , pp. 10910-10919
    • Meslin, F.1    Hamai, A.2    Gao, P.3    Jalil, A.4    Cahuzac, N.5    Chouaib, S.6    Mehrpour, M.7
  • 60
    • 59349095913 scopus 로고    scopus 로고
    • The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel
    • Li, Q. Q.; Cao, X. X.; Xu, J. D.; Chen, Q.; Wang, W. J.; Tang, F.; Chen, Z. Q.; Liu, X. P.; Xu, Z. D. The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel. Cell. Mol. Life Sci CMLS 2009, 66 (3), 504-515.
    • (2009) Cell. Mol. Life Sci CMLS , vol.66 , Issue.3 , pp. 504-515
    • Li, Q.Q.1    Cao, X.X.2    Xu, J.D.3    Chen, Q.4    Wang, W.J.5    Tang, F.6    Chen, Z.Q.7    Liu, X.P.8    Xu, Z.D.9
  • 61
    • 21744447704 scopus 로고    scopus 로고
    • Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells
    • Roucou, X.; Giannopoulos, P. N.; Zhang, Y.; Jodoin, J.; Goodyer, C. G.; LeBlanc, A. Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells. Cell Death Differ. 2005, 12 (7), 783-795.
    • (2005) Cell Death Differ , vol.12 , Issue.7 , pp. 783-795
    • Roucou, X.1    Giannopoulos, P.N.2    Zhang, Y.3    Jodoin, J.4    Goodyer, C.G.5    LeBlanc, A.6
  • 62
    • 42549132465 scopus 로고    scopus 로고
    • POLR2F, ATP6V0A1 and PRNP expression in colorectal cancer: New molecules with prognostic significance?
    • Antonacopoulou, A. G.; Grivas, P. D.; Skarlas, L.; Kalofonos, M.; Scopa, C. D.; Kalofonos, H. P. POLR2F, ATP6V0A1 and PRNP expression in colorectal cancer: new molecules with prognostic significance? Anticancer Res. 2008, 28 (2B), 1221-1227.
    • (2008) Anticancer Res , vol.28 , Issue.2 B , pp. 1221-1227
    • Antonacopoulou, A.G.1    Grivas, P.D.2    Skarlas, L.3    Kalofonos, M.4    Scopa, C.D.5    Kalofonos, H.P.6
  • 64
    • 66749188623 scopus 로고    scopus 로고
    • Antibodies to prion protein inhibit human colon cancer cell growth
    • McEwan, J. F.; Windsor, M. L.; Cullis-Hill, S. D. Antibodies to prion protein inhibit human colon cancer cell growth. Tumour Biol. 2009, 30 (3), 141-147.
    • (2009) Tumour Biol , vol.30 , Issue.3 , pp. 141-147
    • McEwan, J.F.1    Windsor, M.L.2    Cullis-Hill, S.D.3
  • 65
    • 79955465845 scopus 로고    scopus 로고
    • Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells
    • Yap, Y. H.; Say, Y. H. Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells. Cancer Lett. 2011, 306 (1), 111-119.
    • (2011) Cancer Lett , vol.306 , Issue.1 , pp. 111-119
    • Yap, Y.H.1    Say, Y.H.2
  • 66
    • 0033429672 scopus 로고    scopus 로고
    • Redoxregulation of intrinsic prion expression in multicellular prostate tumor spheroids
    • Sauer, H.; Dagdanova, A.; Hescheler, J.; Wartenberg, M. Redoxregulation of intrinsic prion expression in multicellular prostate tumor spheroids. Free Radic. Biol. Med. 1999, 27 (11-12), 1276-1283.
    • (1999) Free Radic. Biol. Med , vol.27 , Issue.11-12 , pp. 1276-1283
    • Sauer, H.1    Dagdanova, A.2    Hescheler, J.3    Wartenberg, M.4
  • 67
    • 0034282872 scopus 로고    scopus 로고
    • Doppel is an N-glycosylated, glycosylphosphatidylinositolanchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss
    • Silverman, G. L.; Qin, K.; Moore, R. C.; Yang, Y.; Mastrangelo, P.; Tremblay, P.; Prusiner, S. B.; Cohen, F. E.; Westaway, D. Doppel is an N-glycosylated, glycosylphosphatidylinositolanchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss. J. Biol. Chem. 2000, 275 (35), 26834-26841.
    • (2000) J. Biol. Chem , vol.275 , Issue.35 , pp. 26834-26841
    • Silverman, G.L.1    Qin, K.2    Moore, R.C.3    Yang, Y.4    Mastrangelo, P.5    Tremblay, P.6    Prusiner, S.B.7    Cohen, F.E.8    Westaway, D.9
  • 69
    • 0037432187 scopus 로고    scopus 로고
    • Prion-like protein Doppel expression is not modified in scrapieinfected cells and in the brains of patients with Creutzfeldt-Jakob disease
    • Peoc'h, K.; Volland, H.; De Gassart, A.; Beaudry, P.; Sazdovitch, V.; Sorgato, M. C.; Creminon, C.; Laplanche, J. L.; Lehmann, S. Prion-like protein Doppel expression is not modified in scrapieinfected cells and in the brains of patients with Creutzfeldt-Jakob disease. FEBS Lett. 2003, 536 (1-3), 61-65.
    • (2003) FEBS Lett , vol.536 , Issue.1-3 , pp. 61-65
    • Peoc'h, K.1    Volland, H.2    De Gassart, A.3    Beaudry, P.4    Sazdovitch, V.5    Sorgato, M.C.6    Creminon, C.7    Laplanche, J.L.8    Lehmann, S.9
  • 70
    • 0035812297 scopus 로고    scopus 로고
    • The prion gene complex encoding PrP(C) and Doppel: Insights from mutational analysis
    • Mastrangelo, P.; Westaway, D. The prion gene complex encoding PrP(C) and Doppel: insights from mutational analysis. Gene 2001, 275 (1), 1-18.
    • (2001) Gene , vol.275 , Issue.1 , pp. 1-18
    • Mastrangelo, P.1    Westaway, D.2
  • 71
    • 0037424610 scopus 로고    scopus 로고
    • NMR structure of the human doppel protein
    • Luhrs, T.; Riek, R.; Guntert, P.; Wuthrich, K. NMR structure of the human doppel protein. J. Mol. Biol. 2003, 326 (5), 1549-1557.
    • (2003) J. Mol. Biol , vol.326 , Issue.5 , pp. 1549-1557
    • Luhrs, T.1    Riek, R.2    Guntert, P.3    Wuthrich, K.4
  • 73
    • 0036498430 scopus 로고    scopus 로고
    • Small is not beautiful: Antagonizing functions for the prion protein PrP(C) and its homologue Dpl
    • Behrens, A.; Aguzzi, A. Small is not beautiful: antagonizing functions for the prion protein PrP(C) and its homologue Dpl. Trends Neurosci. 2002, 25 (3), 150-154.
    • (2002) Trends Neurosci , vol.25 , Issue.3 , pp. 150-154
    • Behrens, A.1    Aguzzi, A.2
  • 77
    • 0032694084 scopus 로고    scopus 로고
    • DNA methylation is the primary silencing mechanism for a set of germ line-and tumor-specific genes with a CpG-rich promoter
    • De, S., Lurquin, C., Lethe, B., Martelange, V., Boon, T. DNA methylation is the primary silencing mechanism for a set of germ line-and tumor-specific genes with a CpG-rich promoter. Mol. Cell Biol. 1999, 19, 7327-7335.
    • (1999) Mol. Cell Biol , vol.19 , pp. 7327-7335
    • De, S.1    Lurquin, C.2    Lethe, B.3    Martelange, V.4    Boon, T.5
  • 78
    • 77954215302 scopus 로고    scopus 로고
    • Current strategies to target p53 in cancer
    • Chen, F.; Wang, W.; El-Deiry, W. S. Current strategies to target p53 in cancer. Biochem. Pharmacol. 2010, 80 (5), 724-730.
    • (2010) Biochem. Pharmacol , vol.80 , Issue.5 , pp. 724-730
    • Chen, F.1    Wang, W.2    El-Deiry, W.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.