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Volumn 6, Issue 5, 2012, Pages 498-509

Separate mechanisms act concurrently to shed and release the prion protein from the cell

Author keywords

cleavage; Exosomes; Extreme C terminal cleavage; Inhibitor; Prion; Shedding

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; METALLOPROTEINASE INHIBITOR; PRION PROTEIN;

EID: 84869814585     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.22588     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • PMID:2444340
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987; 51:229-40; PMID:2444340; http://dx.doi.org/10.1016/0092-8674(87)90150-4.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 2
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • PMID:1980209
    • Stahl N, Baldwin MA, Burlingame AL, Prusiner SB. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 1990; 29:8879-84; PMID:1980209; http://dx.doi.org/10.1021/ bi00490a001.
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 3
    • 0033301552 scopus 로고    scopus 로고
    • Cell biological studies of the prion protein
    • PMID:11475702
    • Harris DA. Cell biological studies of the prion protein. Curr Issues Mol Biol 1999; 1:65-75; PMID:11475702.
    • (1999) Curr Issues Mol Biol , vol.1 , pp. 65-75
    • Harris, D.A.1
  • 4
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • PMID:8100741
    • Büeler H, Aguzzi A, Sailer A, Greiner RA, Autenried P, Aguet M, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73:1339-47; PMID:8100741; http://dx.doi.org/10.1016/0092-8674(93)90360-3.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Büeler, H.1    Aguzzi, A.2    Sailer, A.3    Greiner, R.A.4    Autenried, P.5    Aguet, M.6
  • 5
    • 28844504671 scopus 로고    scopus 로고
    • Proteolytic cleavage and shedding of the bovine prion protein in two cell culture systems
    • PMID:16140411
    • Zhao H, Klingeborn M, Simonsson M, Linné T. Proteolytic cleavage and shedding of the bovine prion protein in two cell culture systems. Virus Res 2006; 115:43-55; PMID:16140411; http://dx.doi.org/10.1016/j.virusres.2005.07. 004.
    • (2006) Virus Res , vol.115 , pp. 43-55
    • Zhao, H.1    Klingeborn, M.2    Simonsson, M.3    Linné, T.4
  • 6
    • 0029027854 scopus 로고
    • Truncated forms of the human prion protein in normal brain and in prion diseases
    • PMID:7642585
    • Chen SG, Teplow DB, Parchi P, Teller JK, Gambetti P, Autilio-Gambetti L. Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem 1995; 270:19173-80; PMID:7642585; http://dx.doi.org/10. 1074/jbc.270.32.19173.
    • (1995) J Biol Chem , vol.270 , pp. 19173-19180
    • Chen, S.G.1    Teplow, D.B.2    Parchi, P.3    Teller, J.K.4    Gambetti, P.5    Autilio-Gambetti, L.6
  • 7
    • 0032076463 scopus 로고    scopus 로고
    • Prion protein biology
    • PMID:9590169
    • Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Prion protein biology. Cell 1998; 93:337-48; PMID:9590169; http://dx.doi.org/10.1016/S0092-8674(00)81163-0.
    • (1998) Cell , vol.93 , pp. 337-348
    • Prusiner, S.B.1    Scott, M.R.2    DeArmond, S.J.3    Cohen, F.E.4
  • 8
    • 83755162371 scopus 로고    scopus 로고
    • A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation
    • PMID:22025612
    • Westergard L, Turnbaugh JA, Harris DA. A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation. J Biol Chem 2011; 286:44234-42; PMID:22025612; http://dx.doi.org/10.1074/jbc.M111.286195.
    • (2011) J Biol Chem , vol.286 , pp. 44234-44242
    • Westergard, L.1    Turnbaugh, J.A.2    Harris, D.A.3
  • 9
    • 77649091387 scopus 로고    scopus 로고
    • Axonal prion protein is required for peripheral myelin maintenance
    • PMID:20098419
    • Bremer J, Baumann F, Tiberi C, Wessig C, Fischer H, Schwarz P, et al. Axonal prion protein is required for peripheral myelin maintenance. Nat Neurosci 2010; 13:310-8; PMID:20098419; http://dx.doi.org/10.1038/nn.2483.
    • (2010) Nat Neurosci , vol.13 , pp. 310-318
    • Bremer, J.1    Baumann, F.2    Tiberi, C.3    Wessig, C.4    Fischer, H.5    Schwarz, P.6
  • 10
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • PMID:19850936
    • Guillot-Sestier MV, Sunyach C, Druon C, Scarzello S, Checler F. The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J Biol Chem 2009; 284:35973-86; PMID:19850936; http://dx.doi.org/10.1074/jbc.M109.051086.
    • (2009) J Biol Chem , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 11
    • 84871089578 scopus 로고    scopus 로고
    • The alpha-secretasederived fragment of cellular prion, N1, protects against monomeric and oligomeric Abeta-associated cell death
    • PMID:22184125
    • Guillot-Sestier MV, Sunyach C, Ferreira ST, Marzolo MP, Bauer C, Thevenet A, et al. The alpha-secretasederived fragment of cellular prion, N1, protects against monomeric and oligomeric Abeta-associated cell death. J Biol Chem 2011; PMID:22184125.
    • (2011) J Biol Chem
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Ferreira, S.T.3    Marzolo, M.P.4    Bauer, C.5    Thevenet, A.6
  • 12
    • 69249128689 scopus 로고    scopus 로고
    • Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein
    • PMID:19564338
    • Taylor DR, Parkin ET, Cocklin SL, Ault JR, Ashcroft AE, Turner AJ, et al. Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein. J Biol Chem 2009; 284:22590-600; PMID:19564338; http://dx.doi.org/10.1074/jbc.M109.032599.
    • (2009) J Biol Chem , vol.284 , pp. 22590-22600
    • Taylor, D.R.1    Parkin, E.T.2    Cocklin, S.L.3    Ault, J.R.4    Ashcroft, A.E.5    Turner, A.J.6
  • 13
    • 53349177064 scopus 로고    scopus 로고
    • Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles
    • PMID:18422484
    • Alais S, Simoes S, Baas D, Lehmann S, Raposo G, Darlix JL, et al. Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles. Biol Cell 2008; 100:603-15; PMID:18422484; http://dx.doi.org/10.1042/ BC20080025.
    • (2008) Biol Cell , vol.100 , pp. 603-615
    • Alais, S.1    Simoes, S.2    Baas, D.3    Lehmann, S.4    Raposo, G.5    Darlix, J.L.6
  • 14
  • 15
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • PMID:17334982
    • Vella LJ, Sharples RA, Lawson VA, Masters CL, Cappai R, Hill AF. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J Pathol 2007; 211:582-90; PMID:17334982; http://dx.doi.org/10.1002/ path.2145.
    • (2007) J Pathol , vol.211 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 16
    • 84860864336 scopus 로고    scopus 로고
    • Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle
    • PMID:22447932
    • Liang J, Wang W, Sorensen D, Medina S, Ilchenko S, Kiselar J, et al. Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle. J Biol Chem 2012; 287:16510-20; PMID:22447932; http://dx.doi.org/10.1074/jbc.M112.360891.
    • (2012) J Biol Chem , vol.287 , pp. 16510-16520
    • Liang, J.1    Wang, W.2    Sorensen, D.3    Medina, S.4    Ilchenko, S.5    Kiselar, J.6
  • 17
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • PMID:16236709
    • Cissé MA, Sunyach C, Lefranc-Jullien S, Postina R, Vincent B, Checler F. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J Biol Chem 2005; 280:40624-31; PMID:16236709; http://dx.doi.org/10.1074/jbc.M506069200.
    • (2005) J Biol Chem , vol.280 , pp. 40624-40631
    • Cissé, M.A.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 18
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • PMID:11477090
    • Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 2001; 276:37743-6; PMID:11477090.
    • (2001) J Biol Chem , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6
  • 19
    • 79957510525 scopus 로고    scopus 로고
    • Lack of a-disintegrin-and-metallo-proteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo
    • PMID:21619641
    • Altmeppen HC, Prox J, Puig B, Kluth MA, Bernreuther C, Thurm D, et al. Lack of a-disintegrin-and-metallo-proteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo. Mol Neurodegener 2011; 6:36; PMID:21619641; http://dx.doi.org/10.1186/1750-1326-6- 36.
    • (2011) Mol Neurodegener , vol.6 , pp. 36
    • Altmeppen, H.C.1    Prox, J.2    Puig, B.3    Kluth, M.A.4    Bernreuther, C.5    Thurm, D.6
  • 20
    • 70349783752 scopus 로고    scopus 로고
    • Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo
    • PMID:19632330
    • Endres K, Mitteregger G, Kojro E, Kretzschmar H, Fahrenholz F. Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo. Neurobiol Dis 2009; 36:233-41; PMID:19632330; http://dx.doi. org/10.1016/j.nbd.2009.07.015.
    • (2009) Neurobiol Dis , vol.36 , pp. 233-241
    • Endres, K.1    Mitteregger, G.2    Kojro, E.3    Kretzschmar, H.4    Fahrenholz, F.5
  • 21
    • 0027405573 scopus 로고
    • Processing of a cellular prion protein: Identification of N- and C-terminal cleavage sites
    • PMID:8093841
    • Harris DA, Huber MT, van Dijken P, Shyng SL, Chait BT, Wang R. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry 1993; 32:1009-16; PMID:8093841; http://dx.doi.org/10.1021/ bi00055a003.
    • (1993) Biochemistry , vol.32 , pp. 1009-1016
    • Harris, D.A.1    Huber, M.T.2    Van Dijken, P.3    Shyng, S.L.4    Chait, B.T.5    Wang, R.6
  • 22
    • 77949405435 scopus 로고    scopus 로고
    • Unexpected tolerance of alpha-cleavage of the prion protein to sequence variations
    • PMID:20161712
    • Oliveira-Martins JB, Yusa S, Calella AM, Bridel C, Baumann F, Dametto P, et al. Unexpected tolerance of alpha-cleavage of the prion protein to sequence variations. PLoS One 2010; 5:e9107; PMID:20161712; http://dx.doi.org/10.1371/ journal.pone.0009107.
    • (2010) PLoS One , vol.5
    • Oliveira-Martins, J.B.1    Yusa, S.2    Calella, A.M.3    Bridel, C.4    Baumann, F.5    Dametto, P.6
  • 23
    • 0036257318 scopus 로고    scopus 로고
    • Mutant prion protein acquires resistance to protease in mouse neuroblastoma cells
    • PMID:11961279
    • Wegner C, Römer A, Schmalzbauer R, Lorenz H, Windl O, Kretzschmar HA. Mutant prion protein acquires resistance to protease in mouse neuroblastoma cells. J Gen Virol 2002; 83:1237-45; PMID:11961279.
    • (2002) J Gen Virol , vol.83 , pp. 1237-1245
    • Wegner, C.1    Römer, A.2    Schmalzbauer, R.3    Lorenz, H.4    Windl, O.5    Kretzschmar, H.A.6
  • 24
    • 33745565356 scopus 로고    scopus 로고
    • Retrovirus infection strongly enhances scrapie infectivity release in cell culture
    • PMID:16724107
    • Leblanc P, Alais S, Porto-Carreiro I, Lehmann S, Grassi J, Raposo G, et al. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J 2006; 25:2674-85; PMID:16724107; http://dx.doi.org/10.1038/sj. emboj.7601162.
    • (2006) EMBO J , vol.25 , pp. 2674-2685
    • Leblanc, P.1    Alais, S.2    Porto-Carreiro, I.3    Lehmann, S.4    Grassi, J.5    Raposo, G.6
  • 25
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Chapter 3:Unit 3 22
    • Thery C, Amigorena S, Raposo G, Clayton A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr Protoc Cell Biol 2006; Chapter 3:Unit 3 22.
    • (2006) Curr Protoc Cell Biol
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 26
    • 27744581333 scopus 로고    scopus 로고
    • The N-terminal cleavage of cellular prion protein in the human brain
    • PMID:16263114
    • Laffont-Proust I, Faucheux BA, Hässig R, Sazdovitch V, Simon S, Grassi J, et al. The N-terminal cleavage of cellular prion protein in the human brain. FEBS Lett 2005; 579:6333-7; PMID:16263114; http://dx.doi.org/10.1016/j. febslet.2005.10.013.
    • (2005) FEBS Lett , vol.579 , pp. 6333-6337
    • Laffont-Proust, I.1    Faucheux, B.A.2    Hässig, R.3    Sazdovitch, V.4    Simon, S.5    Grassi, J.6
  • 27
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • PMID:8101844
    • Shyng SL, Huber MT, Harris DA. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J Biol Chem 1993; 268:15922-8; PMID:8101844.
    • (1993) J Biol Chem , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 28
    • 80053330454 scopus 로고    scopus 로고
    • The N-terminal, polybasic region is critical for prion protein neuroprotective activity
    • PMID:21980526
    • Turnbaugh JA, Westergard L, Unterberger U, Biasini E, Harris DA. The N-terminal, polybasic region is critical for prion protein neuroprotective activity. PLoS One 2011; 6:e25675; PMID:21980526; http://dx.doi.org/10.1371/ journal.pone.0025675.
    • (2011) PLoS One , vol.6
    • Turnbaugh, J.A.1    Westergard, L.2    Unterberger, U.3    Biasini, E.4    Harris, D.A.5
  • 29
    • 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
    • PMID:9811348
    • Jiménez-Huete A, Lievens PM, Vidal R, Piccardo P, Ghetti B, Tagliavini F, et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 1998; 153:1561-72; PMID:9811348; http://dx.doi.org/10.1016/ S0002-9440(10)65744-6.
    • (1998) Am J Pathol , vol.153 , pp. 1561-1572
    • Jiménez-Huete, A.1    Lievens, P.M.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6
  • 30
    • 2542434845 scopus 로고    scopus 로고
    • Calpain-dependent endoproteolytic cleavage of PrPSc modulates scrapie prion propagation
    • PMID:15026410
    • Yadavalli R, Guttmann RP, Seward T, Centers AP, Williamson RA, Telling GC. Calpain-dependent endoproteolytic cleavage of PrPSc modulates scrapie prion propagation. J Biol Chem 2004; 279:21948- 56; PMID:15026410; http://dx.doi.org/10.1074/jbc.M400793200.
    • (2004) J Biol Chem , vol.279 , pp. 21948-21956
    • Yadavalli, R.1    Guttmann, R.P.2    Seward, T.3    Centers, A.P.4    Williamson, R.A.5    Telling, G.C.6
  • 31
    • 0035970784 scopus 로고    scopus 로고
    • Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies
    • PMID:11277980
    • Liu T, Zwingman T, Li R, Pan T, Wong BS, Petersen RB, et al. Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies. Brain Res 2001; 896:118-29; PMID:11277980; http://dx.doi.org/10.1016/S0006-8993(01)02050-9.
    • (2001) Brain Res , vol.896 , pp. 118-129
    • Liu, T.1    Zwingman, T.2    Li, R.3    Pan, T.4    Wong, B.S.5    Petersen, R.B.6
  • 32
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • PMID:7698979
    • Taraboulos A, Scott M, Semenov A, Avrahami D, Laszlo L, Prusiner SB. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J Cell Biol 1995; 129:121-32; PMID:7698979; http://dx.doi.org/10.1083/jcb.129.1.121.
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 33
    • 25844491032 scopus 로고    scopus 로고
    • Proteolytic processing of the ovine prion protein in cell cultures
    • PMID:16182247
    • Tveit H, Lund C, Olsen CM, Ersdal C, Prydz K, Harbitz I, et al. Proteolytic processing of the ovine prion protein in cell cultures. Biochem Biophys Res Commun 2005; 337:232-40; PMID:16182247; http://dx.doi.org/10.1016/j. bbrc.2005.09.031.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 232-240
    • Tveit, H.1    Lund, C.2    Olsen, C.M.3    Ersdal, C.4    Prydz, K.5    Harbitz, I.6
  • 34
    • 59349099006 scopus 로고    scopus 로고
    • Alpha-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts
    • PMID:19056496
    • Walmsley AR, Watt NT, Taylor DR, Perera WS, Hooper NM. alpha-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts. Mol Cell Neurosci 2009; 40:242-8; PMID:19056496; http://dx.doi.org/10.1016/j.mcn.2008.10.012.
    • (2009) Mol Cell Neurosci , vol.40 , pp. 242-248
    • Walmsley, A.R.1    Watt, N.T.2    Taylor, D.R.3    Perera, W.S.4    Hooper, N.M.5
  • 35
    • 0027291065 scopus 로고
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor
    • PMID:7691278
    • Borchelt DR, Rogers M, Stahl N, Telling G, Prusiner SB. Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Glycobiology 1993; 3:319-29; PMID:7691278; http://dx.doi.org/10.1093/glycob/3.4.319.
    • (1993) Glycobiology , vol.3 , pp. 319-329
    • Borchelt, D.R.1    Rogers, M.2    Stahl, N.3    Telling, G.4    Prusiner, S.B.5
  • 36
    • 1642524321 scopus 로고    scopus 로고
    • Dual mechanisms for shedding of the cellular prion protein
    • PMID:14711812
    • Parkin ET, Watt NT, Turner AJ, Hooper NM. Dual mechanisms for shedding of the cellular prion protein. J Biol Chem 2004; 279:11170-8; PMID:14711812; http://dx.doi.org/10.1074/jbc.M312105200.
    • (2004) J Biol Chem , vol.279 , pp. 11170-11178
    • Parkin, E.T.1    Watt, N.T.2    Turner, A.J.3    Hooper, N.M.4
  • 37
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • PMID:12446128
    • Checler F, Vincent B. Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends Neurosci 2002; 25:616-20; PMID:12446128; http://dx.doi.org/10.1016/S0166-2236(02)02263-4.
    • (2002) Trends Neurosci , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 38
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • PMID:10952979
    • 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; 275:35612-6; PMID:10952979; http://dx.doi.org/10.1074/jbc.M004628200.
    • (2000) J Biol Chem , vol.275 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3    Lehmann, S.4    Grassi, J.5    Checler, F.6
  • 39
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: Composition, biogenesis and function
    • PMID:12154376
    • Théry C, Zitvogel L, Amigorena S. Exosomes: composition, biogenesis and function. Nat Rev Immunol 2002; 2:569-79; PMID:12154376.
    • (2002) Nat Rev Immunol , vol.2 , pp. 569-579
    • Théry, C.1    Zitvogel, L.2    Amigorena, S.3
  • 40
  • 41
    • 0030613755 scopus 로고    scopus 로고
    • Prion (PrPSc)-specific epitope defined by a monoclonal antibody
    • PMID:9363892
    • Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 1997; 390:74-7; PMID:9363892; http://dx.doi.org/10.1038/36337.
    • (1997) Nature , vol.390 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3    Moser, M.4    Schaller, O.5    Fischer, R.6
  • 42
    • 33747386522 scopus 로고    scopus 로고
    • Rapid and discriminatory diagnosis of scrapie and BSE in retro-pharyngeal lymph nodes of sheep
    • PMID:16764717
    • Langeveld JP, Jacobs JG, Erkens JH, Bossers A, van Zijderveld FG, van Keulen LJ. Rapid and discriminatory diagnosis of scrapie and BSE in retro-pharyngeal lymph nodes of sheep. BMC Vet Res 2006; 2:19; PMID:16764717; http://dx.doi.org/10.1186/1746-6148-2-19.
    • (2006) BMC Vet Res , vol.2 , pp. 19
    • Langeveld, J.P.1    Jacobs, J.G.2    Erkens, J.H.3    Bossers, A.4    Van Zijderveld, F.G.5    Van Keulen, L.J.6
  • 43
    • 0033102301 scopus 로고    scopus 로고
    • A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines
    • PMID:10049818
    • Vorberg I, Buschmann A, Harmeyer S, Saalmüller A, Pfaff E, Groschup MH. A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines. Virology 1999; 255:26-31; PMID:10049818; http://dx.doi.org/10.1006/viro.1998.9561.
    • (1999) Virology , vol.255 , pp. 26-31
    • Vorberg, I.1    Buschmann, A.2    Harmeyer, S.3    Saalmüller, A.4    Pfaff, E.5    Groschup, M.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.