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Volumn 1774, Issue 1, 2007, Pages 154-167

Prion infection-impaired functional blocks identified by proteomics enlighten the targets and the curing pathways of an anti-prion drug

Author keywords

Heparan sulfate mimetics; Neuronal cell line; Prion; Proteomics

Indexed keywords

HEAT SHOCK PROTEIN; HEPARAN SULFATE; HEPARAN SULFATE MIMETIC AGENT; PRION PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 33845979139     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.10.016     Document Type: Article
Times cited : (15)

References (78)
  • 3
    • 0033964470 scopus 로고    scopus 로고
    • Effect of amphotericin B on wild-type and mutated prion proteins in cultured cells: putative mechanism of action in transmissible spongiform encephalopathies
    • Mange A., Milhavet O., McMahon H.E., Casanova D., and Lehmann S. Effect of amphotericin B on wild-type and mutated prion proteins in cultured cells: putative mechanism of action in transmissible spongiform encephalopathies. J. Neurochem. 74 (2000) 754-762
    • (2000) J. Neurochem. , vol.74 , pp. 754-762
    • Mange, A.1    Milhavet, O.2    McMahon, H.E.3    Casanova, D.4    Lehmann, S.5
  • 7
    • 0033961817 scopus 로고    scopus 로고
    • Effect of Congo red on wild-type and mutated prion proteins in cultured cells
    • Milhavet O., Mange A., Casanova D., and Lehmann S. Effect of Congo red on wild-type and mutated prion proteins in cultured cells. J. Neurochem. 74 (2000) 222-230
    • (2000) J. Neurochem. , vol.74 , pp. 222-230
    • Milhavet, O.1    Mange, A.2    Casanova, D.3    Lehmann, S.4
  • 10
    • 7444235958 scopus 로고    scopus 로고
    • Cell-surface retention of PrPC by anti-PrP antibody prevents protease-resistant PrP formation
    • Kim C.L., Karino A., Ishiguro N., Shinagawa M., Sato M., and Horiuchi M. Cell-surface retention of PrPC by anti-PrP antibody prevents protease-resistant PrP formation. J. Gen. Virol. 85 (2004) 3473-3482
    • (2004) J. Gen. Virol. , vol.85 , pp. 3473-3482
    • Kim, C.L.1    Karino, A.2    Ishiguro, N.3    Shinagawa, M.4    Sato, M.5    Horiuchi, M.6
  • 11
    • 0029564913 scopus 로고
    • Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells
    • Shyng S.L., Lehmann S., Moulder K.L., and Harris D.A. Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J. Biol. Chem. 270 (1995) 30221-30229
    • (1995) J. Biol. Chem. , vol.270 , pp. 30221-30229
    • Shyng, S.L.1    Lehmann, S.2    Moulder, K.L.3    Harris, D.A.4
  • 12
    • 4344624313 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors or platelet-activating factor antagonists prevent prion replication
    • Bate C., Reid S., and Williams A. Phospholipase A2 inhibitors or platelet-activating factor antagonists prevent prion replication. J. Biol. Chem. 279 (2004) 36405-36411
    • (2004) J. Biol. Chem. , vol.279 , pp. 36405-36411
    • Bate, C.1    Reid, S.2    Williams, A.3
  • 13
    • 2442483932 scopus 로고    scopus 로고
    • Squalestatin cures prion-infected neurons and protects against prion neurotoxicity
    • Bate C., Salmona M., Diomede L., and Williams A. Squalestatin cures prion-infected neurons and protects against prion neurotoxicity. J. Biol. Chem. 279 (2004) 14983-14990
    • (2004) J. Biol. Chem. , vol.279 , pp. 14983-14990
    • Bate, C.1    Salmona, M.2    Diomede, L.3    Williams, A.4
  • 16
    • 12544258339 scopus 로고    scopus 로고
    • Altered interaction and expression of proteins involved in neurosecretion in scrapie-infected GT1-1 cells
    • Sandberg M.K., and Low P. Altered interaction and expression of proteins involved in neurosecretion in scrapie-infected GT1-1 cells. J. Biol. Chem. 280 (2005) 1264-1271
    • (2005) J. Biol. Chem. , vol.280 , pp. 1264-1271
    • Sandberg, M.K.1    Low, P.2
  • 20
    • 33646728858 scopus 로고    scopus 로고
    • Analysis of the cerebellar proteome in a transgenic mouse model of inherited prion disease reveals preclinical alteration of calcineurin activity
    • Biasini E., Massignan T., Fioriti L., Rossi V., Dossena S., Salmona M., Forloni G., Bonetto V., and Chiesa R. Analysis of the cerebellar proteome in a transgenic mouse model of inherited prion disease reveals preclinical alteration of calcineurin activity. Proteomics 6 (2006) 2823-2834
    • (2006) Proteomics , vol.6 , pp. 2823-2834
    • Biasini, E.1    Massignan, T.2    Fioriti, L.3    Rossi, V.4    Dossena, S.5    Salmona, M.6    Forloni, G.7    Bonetto, V.8    Chiesa, R.9
  • 21
    • 0032894047 scopus 로고    scopus 로고
    • A substituted dextran enhances muscle fiber survival and regeneration in ischemic and denervated rat EDL muscle
    • Desgranges P., Barbaud C., Caruelle J.P., Barritault D., and Gautron J. A substituted dextran enhances muscle fiber survival and regeneration in ischemic and denervated rat EDL muscle. FASEB J. 13 (1999) 761-766
    • (1999) FASEB J. , vol.13 , pp. 761-766
    • Desgranges, P.1    Barbaud, C.2    Caruelle, J.P.3    Barritault, D.4    Gautron, J.5
  • 22
    • 33845974637 scopus 로고    scopus 로고
    • E. Petit, D. Papy-Garcia and V. Barbier Chassefiere, Procédé de sulfonation de composés comprenant des groupements hydroxyle (OH) libres ou des amines primaires ou secondaires OTR3, Patent no FR2832708 (2002).
  • 23
    • 7944228944 scopus 로고    scopus 로고
    • Towards a reference map of Eimeria tenella sporozoite proteins by two-dimensional electrophoresis and mass spectrometry
    • de Venevelles P., Chich J.F., Faigle W., Loew D., Labbe M., Girard-Misguich F., and Pery P. Towards a reference map of Eimeria tenella sporozoite proteins by two-dimensional electrophoresis and mass spectrometry. Int. J. Parasitol. 34 (2004) 1321-1331
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1321-1331
    • de Venevelles, P.1    Chich, J.F.2    Faigle, W.3    Loew, D.4    Labbe, M.5    Girard-Misguich, F.6    Pery, P.7
  • 24
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beier H., and Gross H.J. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8 (1987) 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 25
    • 33845997975 scopus 로고    scopus 로고
    • SAS Institute Inc. pp. 3884, SAS Institute Inc, Cary, NC, USA 1999.
  • 26
    • 34047109199 scopus 로고    scopus 로고
    • Statistics for proteomics: experimental design and 2-DE differential analysis
    • 10.1016/j.jchromb.2006.09.033
    • Chich J.F., David O., Villers F., Schaeffer B., Lutomski D., and Huet S. Statistics for proteomics: experimental design and 2-DE differential analysis. J. Chromatogr., B. (2006) 10.1016/j.jchromb.2006.09.033
    • (2006) J. Chromatogr., B.
    • Chich, J.F.1    David, O.2    Villers, F.3    Schaeffer, B.4    Lutomski, D.5    Huet, S.6
  • 27
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini Y., and Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc., B 57 (1995) 289-300
    • (1995) J. R. Stat. Soc., B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 32
    • 1542399989 scopus 로고    scopus 로고
    • FatiGO: a web tool for finding significant associations of Gene Ontology terms with groups of genes
    • Al-Shahrour F., Diaz-Uriarte R., and Dopazo J. FatiGO: a web tool for finding significant associations of Gene Ontology terms with groups of genes. Bioinformatics 20 (2004) 578-580
    • (2004) Bioinformatics , vol.20 , pp. 578-580
    • Al-Shahrour, F.1    Diaz-Uriarte, R.2    Dopazo, J.3
  • 35
    • 0023024149 scopus 로고
    • Calmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments
    • Nishida E., Koyasu S., Sakai H., and Yahara I. Calmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments. J. Biol. Chem. 261 (1986) 16033-16036
    • (1986) J. Biol. Chem. , vol.261 , pp. 16033-16036
    • Nishida, E.1    Koyasu, S.2    Sakai, H.3    Yahara, I.4
  • 36
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C., Russelakis-Carneiro M., Maundrell K., Castilla J., and Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 22 (2003) 5435-5445
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 37
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella R.A., Srinivasan M., Haugejorden S.M., and Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J. Biol. Chem. 265 (1990) 1094-1101
    • (1990) J. Biol. Chem. , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 38
    • 10944246574 scopus 로고    scopus 로고
    • Pinning down phosphorylated tau and tauopathies
    • Lim J., and Lu K.P. Pinning down phosphorylated tau and tauopathies. Biochim. Biophys. Acta 1739 (2005) 311-322
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 311-322
    • Lim, J.1    Lu, K.P.2
  • 39
    • 18344377030 scopus 로고    scopus 로고
    • The p53 pathway: positive and negative feedback loops
    • Harris S.L., and Levine A.J. The p53 pathway: positive and negative feedback loops. Oncogene 24 (2005) 2899-2908
    • (2005) Oncogene , vol.24 , pp. 2899-2908
    • Harris, S.L.1    Levine, A.J.2
  • 40
    • 4143066846 scopus 로고    scopus 로고
    • Metalloendopeptidase EC 3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells
    • Jeske N.A., Glucksman M.J., and Roberts J.L. Metalloendopeptidase EC 3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells. J. Neurochem. 90 (2004) 819-828
    • (2004) J. Neurochem. , vol.90 , pp. 819-828
    • Jeske, N.A.1    Glucksman, M.J.2    Roberts, J.L.3
  • 42
    • 0033043062 scopus 로고    scopus 로고
    • Cathepsin D in cancer metastasis: a protease and a ligand
    • Rochefort H., and Liaudet-Coopman E. Cathepsin D in cancer metastasis: a protease and a ligand. APMIS 107 (1999) 86-95
    • (1999) APMIS , vol.107 , pp. 86-95
    • Rochefort, H.1    Liaudet-Coopman, E.2
  • 43
    • 1542357656 scopus 로고    scopus 로고
    • Meta-analysis of the association of the cathepsin D Ala224Val gene polymorphism with the risk of Alzheimer's disease: a HuGE gene-disease association review
    • Ntais C., Polycarpou A., and Ioannidis J.P. Meta-analysis of the association of the cathepsin D Ala224Val gene polymorphism with the risk of Alzheimer's disease: a HuGE gene-disease association review. Am. J. Epidemiol. 159 (2004) 527-536
    • (2004) Am. J. Epidemiol. , vol.159 , pp. 527-536
    • Ntais, C.1    Polycarpou, A.2    Ioannidis, J.P.3
  • 45
    • 0029840653 scopus 로고    scopus 로고
    • The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies
    • Hsich G., Kenney K., Gibbs C.J., Lee K.H., and Harrington M.G. The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N. Engl. J. Med. 335 (1996) 924-930
    • (1996) N. Engl. J. Med. , vol.335 , pp. 924-930
    • Hsich, G.1    Kenney, K.2    Gibbs, C.J.3    Lee, K.H.4    Harrington, M.G.5
  • 46
    • 0347480218 scopus 로고    scopus 로고
    • The translationally controlled tumour protein (TCTP)
    • Bommer U.A., and Thiele B.J. The translationally controlled tumour protein (TCTP). Int. J. Biochem. Cell Biol. 36 (2004) 379-385
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 379-385
    • Bommer, U.A.1    Thiele, B.J.2
  • 48
    • 5344238879 scopus 로고    scopus 로고
    • E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1) gene promoter
    • Seelan R.S., Parthasarathy L.K., and Parthasarathy R.N. E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1) gene promoter. Arch. Biochem. Biophys. 431 (2004) 95-106
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 95-106
    • Seelan, R.S.1    Parthasarathy, L.K.2    Parthasarathy, R.N.3
  • 49
    • 0032855980 scopus 로고    scopus 로고
    • Controlling cytoskeleton structure by phosphoinositide-protein interactions: phosphoinositide binding protein domains and effects of lipid packing
    • Janmey P.A., Xian W., and Flanagan L.A. Controlling cytoskeleton structure by phosphoinositide-protein interactions: phosphoinositide binding protein domains and effects of lipid packing. Chem. Phys. Lipids 101 (1999) 93-107
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 93-107
    • Janmey, P.A.1    Xian, W.2    Flanagan, L.A.3
  • 50
    • 0028856782 scopus 로고
    • Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast
    • Qian Y.W., and Lee E.Y. Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast. J. Biol. Chem. 270 (1995) 25507-25513
    • (1995) J. Biol. Chem. , vol.270 , pp. 25507-25513
    • Qian, Y.W.1    Lee, E.Y.2
  • 51
    • 27544505297 scopus 로고    scopus 로고
    • Tumour suppressor retinoblastoma protein Rb: a transcriptional regulator
    • Zhu L. Tumour suppressor retinoblastoma protein Rb: a transcriptional regulator. Eur. J. Cancer 41 (2005) 2415-2427
    • (2005) Eur. J. Cancer , vol.41 , pp. 2415-2427
    • Zhu, L.1
  • 54
    • 0842265979 scopus 로고    scopus 로고
    • Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma
    • Mulla A., Christian H.C., Solito E., Mendoza N., Morris J.F., and Buckingham J.C. Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma. Clin. Endocrinol. (Oxf.) 60 (2004) 107-119
    • (2004) Clin. Endocrinol. (Oxf.) , vol.60 , pp. 107-119
    • Mulla, A.1    Christian, H.C.2    Solito, E.3    Mendoza, N.4    Morris, J.F.5    Buckingham, J.C.6
  • 55
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • White A.R., Guirguis R., Brazier M.W., Jobling M.F., Hill A.F., Beyreuther K., Barrow C.J., Masters C.L., Collins S.J., and Cappai R. Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol. Dis. 8 (2001) 299-316
    • (2001) Neurobiol. Dis. , vol.8 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3    Jobling, M.F.4    Hill, A.F.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Collins, S.J.9    Cappai, R.10
  • 57
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • Bosque P.J., and Prusiner S.B. Cultured cell sublines highly susceptible to prion infection. J. Virol. 74 (2000) 4377-4386
    • (2000) J. Virol. , vol.74 , pp. 4377-4386
    • Bosque, P.J.1    Prusiner, S.B.2
  • 58
    • 27744577768 scopus 로고    scopus 로고
    • The actin cytoskeleton in ageing and apoptosis
    • Gourlay C.W., and Ayscough K.R. The actin cytoskeleton in ageing and apoptosis. FEMS Yeast Res. 5 (2005) 1193-1198
    • (2005) FEMS Yeast Res. , vol.5 , pp. 1193-1198
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 59
    • 0347064330 scopus 로고    scopus 로고
    • Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin
    • Morot-Gaudry-Talarmain Y., Rezaei H., Guermonprez L., Treguer E., and Grosclaude J. Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin. J. Neurochem. 87 (2003) 1456-1470
    • (2003) J. Neurochem. , vol.87 , pp. 1456-1470
    • Morot-Gaudry-Talarmain, Y.1    Rezaei, H.2    Guermonprez, L.3    Treguer, E.4    Grosclaude, J.5
  • 60
    • 3042595161 scopus 로고    scopus 로고
    • Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin
    • Mange A., Crozet C., Lehmann S., and Beranger F. Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin. J. Cell. Sci. 117 (2004) 2411-2416
    • (2004) J. Cell. Sci. , vol.117 , pp. 2411-2416
    • Mange, A.1    Crozet, C.2    Lehmann, S.3    Beranger, F.4
  • 61
    • 21744435912 scopus 로고    scopus 로고
    • Reactive oxygen species-dependent TNF-alpha converting enzyme activation through stimulation of 5-HT2B and alpha1D autoreceptors in neuronal cells
    • Pietri M., Schneider B., Mouillet-Richard S., Ermonval M., Mutel V., Launay J.M., and Kellermann O. Reactive oxygen species-dependent TNF-alpha converting enzyme activation through stimulation of 5-HT2B and alpha1D autoreceptors in neuronal cells. FASEB J. 19 (2005) 1078-1087
    • (2005) FASEB J. , vol.19 , pp. 1078-1087
    • Pietri, M.1    Schneider, B.2    Mouillet-Richard, S.3    Ermonval, M.4    Mutel, V.5    Launay, J.M.6    Kellermann, O.7
  • 64
    • 0032382433 scopus 로고    scopus 로고
    • Cellular catabolism of heparan sulfate proteoglycans
    • Yanagishita M. Cellular catabolism of heparan sulfate proteoglycans. Trends Glycosci. Glycotechnol. 10 (1998) 57-63
    • (1998) Trends Glycosci. Glycotechnol. , vol.10 , pp. 57-63
    • Yanagishita, M.1
  • 65
    • 0032382035 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in neural development
    • Yamaguchi Y. Heparan sulfate proteoglycans in neural development. Trends Glycosci. Glycotechnol. 10 (1998) 161-173
    • (1998) Trends Glycosci. Glycotechnol. , vol.10 , pp. 161-173
    • Yamaguchi, Y.1
  • 67
    • 0347134486 scopus 로고    scopus 로고
    • Proteomic analysis of the tumorigenic human prostate cell line M12 after microcell-mediated transfer of chromosome 19 demonstrates reduction of vimentin
    • Liu X., Wu Y., Zehner Z.E., Jackson-Cook C., and Ware J.L. Proteomic analysis of the tumorigenic human prostate cell line M12 after microcell-mediated transfer of chromosome 19 demonstrates reduction of vimentin. Electrophoresis 24 (2003) 3445-3453
    • (2003) Electrophoresis , vol.24 , pp. 3445-3453
    • Liu, X.1    Wu, Y.2    Zehner, Z.E.3    Jackson-Cook, C.4    Ware, J.L.5
  • 68
    • 0035318367 scopus 로고    scopus 로고
    • Genetic alterations and expression of the protein phosphatase 1 genes in human cancers
    • Takakura S., Kohno T., Manda R., Okamoto A., Tanaka T., and Yokota J. Genetic alterations and expression of the protein phosphatase 1 genes in human cancers. Int. J. Oncol. 18 (2001) 817-824
    • (2001) Int. J. Oncol. , vol.18 , pp. 817-824
    • Takakura, S.1    Kohno, T.2    Manda, R.3    Okamoto, A.4    Tanaka, T.5    Yokota, J.6
  • 71
    • 20444394457 scopus 로고    scopus 로고
    • A functional heparan sulfate mimetic implicates both heparanase and heparan sulfate in tumor angiogenesis and invasion in a mouse model of multistage cancer
    • Joyce J.A., Freeman C., Meyer-Morse N., Parish C.R., and Hanahan D. A functional heparan sulfate mimetic implicates both heparanase and heparan sulfate in tumor angiogenesis and invasion in a mouse model of multistage cancer. Oncogene 24 (2005) 4037-4051
    • (2005) Oncogene , vol.24 , pp. 4037-4051
    • Joyce, J.A.1    Freeman, C.2    Meyer-Morse, N.3    Parish, C.R.4    Hanahan, D.5
  • 72
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen S., Mange A., Dong L., Lehmann S., and Schachner M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol. Cell. Neurosci. 22 (2003) 227-233
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 227-233
    • Chen, S.1    Mange, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 73
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A., Sytnyk V., Leshchyns'ka I., and Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 169 (2005) 341-354
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 74
    • 33644766915 scopus 로고    scopus 로고
    • Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis
    • Steele A.D., Emsley J.G., Ozdinler P.H., Lindquist S., and Macklis J.D. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 3416-3421
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3416-3421
    • Steele, A.D.1    Emsley, J.G.2    Ozdinler, P.H.3    Lindquist, S.4    Macklis, J.D.5
  • 75
    • 12544259444 scopus 로고    scopus 로고
    • Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio)
    • Cotto E., Andre M., Forgue J., Fleury H.J., and Babin P.J. Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio). FEBS J. 272 (2005) 500-513
    • (2005) FEBS J. , vol.272 , pp. 500-513
    • Cotto, E.1    Andre, M.2    Forgue, J.3    Fleury, H.J.4    Babin, P.J.5
  • 76
    • 23044447121 scopus 로고    scopus 로고
    • Proteomics profiling of nuclear proteins for kidney fibroblasts suggests hypoxia, meiosis, and cancer may meet in the nucleus
    • Shakib K., Norman J.T., Fine L.G., Brown L.R., and Godovac-Zimmermann J. Proteomics profiling of nuclear proteins for kidney fibroblasts suggests hypoxia, meiosis, and cancer may meet in the nucleus. Proteomics 5 (2005) 2819-2838
    • (2005) Proteomics , vol.5 , pp. 2819-2838
    • Shakib, K.1    Norman, J.T.2    Fine, L.G.3    Brown, L.R.4    Godovac-Zimmermann, J.5
  • 77
    • 33845434935 scopus 로고    scopus 로고
    • Proteomics analysis in Alzheimer's disease: new insights into mechanisms of neurodegeneration
    • Butterfield D.A., and Boyd-Kimball D. Proteomics analysis in Alzheimer's disease: new insights into mechanisms of neurodegeneration. Int. Rev. Neurobiol. 61 (2004) 159-188
    • (2004) Int. Rev. Neurobiol. , vol.61 , pp. 159-188
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 78
    • 2142760058 scopus 로고    scopus 로고
    • Proteomics in postgenomic neuroscience: the end of the beginning
    • Choudhary J., and Grant S.G. Proteomics in postgenomic neuroscience: the end of the beginning. Nat. Neurosci. 7 (2004) 440-445
    • (2004) Nat. Neurosci. , vol.7 , pp. 440-445
    • Choudhary, J.1    Grant, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.