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Volumn 13, Issue 6, 2003, Pages 399-408

Towards cellular receptors for prions

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR PRION PROTEIN; INFECTIOUS PRION PROTEIN; ISOPROTEIN; LAMININ RECEPTOR; LIGAND; NERVE CELL ADHESION MOLECULE; PRION PROTEIN; PROTEIN X; UNCLASSIFIED DRUG;

EID: 0242443377     PISSN: 10529276     EISSN: None     Source Type: Journal    
DOI: 10.1002/rmv.408     Document Type: Review
Times cited : (44)

References (91)
  • 1
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel PH, Yik JH. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim Biophys Acta 2002; 1572: 341-363.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.2
  • 2
    • 0035292695 scopus 로고    scopus 로고
    • Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family
    • Hussain MM. Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family. Front Biosci 2001; 6: D417-D428.
    • (2001) Front Biosci , vol.6
    • Hussain, M.M.1
  • 3
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P, Beaumont C, Richardson DR. Function and regulation of transferrin and ferritin. Semin Hematol 1998; 35: 35-54.
    • (1998) Semin Hematol , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 4
    • 0037380993 scopus 로고    scopus 로고
    • Regulation of glial cell number and differentiation by ecdysone and Fos signaling
    • Giesen K, Lammel U, Langehans D, Krukkert K, Bunse I, Klambt C. Regulation of glial cell number and differentiation by ecdysone and Fos signaling. Mech Dev 2003; 120: 401-413.
    • (2003) Mech Dev , vol.120 , pp. 401-413
    • Giesen, K.1    Lammel, U.2    Langehans, D.3    Krukkert, K.4    Bunse, I.5    Klambt, C.6
  • 5
    • 0036344505 scopus 로고    scopus 로고
    • Neurotrophin signaling through the p75 neurotrophin receptor
    • Roux PP, Barker PA. Neurotrophin signaling through the p75 neurotrophin receptor. Prog Neurobiol 2002; 67: 203-233.
    • (2002) Prog Neurobiol , vol.67 , pp. 203-233
    • Roux, P.P.1    Barker, P.A.2
  • 7
    • 0036229694 scopus 로고    scopus 로고
    • Networks and cross-talk: Integrin signalling spreads
    • Schwartz MA, Ginsberg MH. Networks and cross-talk: integrin signalling spreads. Nat Cell Biol 2002; 4: E65-E68.
    • (2002) Nat Cell Biol , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 8
    • 0035223849 scopus 로고    scopus 로고
    • Early events of rotavirus infection: The search for the receptor(s)
    • Arias CF, Guerrero CA, Mendez E, et al. Early events of rotavirus infection: the search for the receptor(s). Novartis Found Symp 2001; 238: 47-60.
    • (2001) Novartis Found Symp , vol.238 , pp. 47-60
    • Arias, C.F.1    Guerrero, C.A.2    Mendez, E.3
  • 9
    • 0035377521 scopus 로고    scopus 로고
    • Infection by Trypanosoma cruzi. Identification of a parasite ligand and its host cell receptor
    • Magdesian MH, Giordano R, Ulrich H, et al. Infection by Trypanosoma cruzi. Identification of a parasite ligand and its host cell receptor. J Biol Chem 2001; 276: 19382-19389.
    • (2001) J Biol Chem , vol.276 , pp. 19382-19389
    • Magdesian, M.H.1    Giordano, R.2    Ulrich, H.3
  • 10
    • 0021961303 scopus 로고
    • Presence of laminin receptors in Staphylococcus aureus
    • Lopes JD, dos RM, Brentani RR. Presence of laminin receptors in Staphylococcus aureus. Science 1985; 229: 275-277.
    • (1985) Science , vol.229 , pp. 275-277
    • Lopes, J.D.1    Dos, R.M.2    Brentani, R.R.3
  • 11
    • 0037031877 scopus 로고    scopus 로고
    • Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type I glycoprotein D
    • Liu J, Shriver Z, Pope RM, et al. Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type I glycoprotein D. J Biol Chem 2002; 277: 33456-33467.
    • (2002) J Biol Chem , vol.277 , pp. 33456-33467
    • Liu, J.1    Shriver, Z.2    Pope, R.M.3
  • 12
    • 0036187509 scopus 로고    scopus 로고
    • Natural selection on the erythrocyte surface
    • Baum J, Ward RH, Conway DJ. Natural selection on the erythrocyte surface. Mol Biol Evol 2002; 19: 223-229.
    • (2002) Mol Biol Evol , vol.19 , pp. 223-229
    • Baum, J.1    Ward, R.H.2    Conway, D.J.3
  • 13
    • 0037417217 scopus 로고    scopus 로고
    • Trypanosoma cruzi antigen that interacts with the beta1-adrenergic receptor and modifies myocardial contractile activity
    • Joensen L, Borda E, Kohout T, Perry S, Garcia G, Sterin-Borda L. Trypanosoma cruzi antigen that interacts with the beta1-adrenergic receptor and modifies myocardial contractile activity. Mol Biochem Parasitol 2003; 127: 169-177.
    • (2003) Mol Biochem Parasitol , vol.127 , pp. 169-177
    • Joensen, L.1    Borda, E.2    Kohout, T.3    Perry, S.4    Garcia, G.5    Sterin-Borda, L.6
  • 14
    • 0035524291 scopus 로고    scopus 로고
    • How does HIV cause depletion of CD4 lymphocytes? A mechanism involving virus signaling through its cellular receptors
    • Cloyd MW, Chen JJ, Adeqboyega P, Wang L. How does HIV cause depletion of CD4 lymphocytes? A mechanism involving virus signaling through its cellular receptors. Curr Mol Med 2001; 1: 545-550.
    • (2001) Curr Mol Med , vol.1 , pp. 545-550
    • Cloyd, M.W.1    Chen, J.J.2    Adeqboyega, P.3    Wang, L.4
  • 15
    • 0028305135 scopus 로고
    • A glycolipidanchored prion protein is endocytosed via clathrincoated pits
    • Shyng SL, Heuser JE, Harris DA. A glycolipidanchored prion protein is endocytosed via clathrincoated pits. J Cell Biol 1994; 125: 1239-1250.
    • (1994) J Cell Biol , vol.125 , pp. 1239-1250
    • Shyng, S.L.1    Heuser, J.E.2    Harris, D.A.3
  • 17
    • 0036068963 scopus 로고    scopus 로고
    • Mayhem of the multiple mechanisms: Modelling neurodegeneration in prion disease
    • Brown DR. Mayhem of the multiple mechanisms: modelling neurodegeneration in prion disease. J Neurochem 2002; 82: 209-215.
    • (2002) J Neurochem , vol.82 , pp. 209-215
    • Brown, D.R.1
  • 18
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • Caughey B. Interactions between prion protein isoforms: the kiss of death? Trends Biochem Sci 2001; 26: 235-242.
    • (2001) Trends Biochem Sci , vol.26 , pp. 235-242
    • Caughey, B.1
  • 19
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 1996; 347: 921-925.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 20
    • 0030775632 scopus 로고    scopus 로고
    • Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent
    • Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 1997; 389: 498-501.
    • (1997) Nature , vol.389 , pp. 498-501
    • Bruce, M.E.1    Will, R.G.2    Ironside, J.W.3
  • 21
    • 0030820354 scopus 로고    scopus 로고
    • The same prion strain causes vCJD and BSE
    • Hill AF, Desbruslais M, Joiner S, et al. The same prion strain causes vCJD and BSE. Nature 1997; 389: 448-450, 526.
    • (1997) Nature , vol.389 , pp. 448-450
    • Hill, A.F.1    Desbruslais, M.2    Joiner, S.3
  • 22
    • 0036090579 scopus 로고    scopus 로고
    • Clinical features of variant Creutzfeldt-Jakob disease
    • Henry C, Knight R. Clinical features of variant Creutzfeldt-Jakob disease. Rev Med Virol 2002; 12: 143-150.
    • (2002) Rev Med Virol , vol.12 , pp. 143-150
    • Henry, C.1    Knight, R.2
  • 23
    • 0036670751 scopus 로고    scopus 로고
    • Altering prion replication for therapy and diagnosis of transmissible spongiform encephalopathies
    • Soto C. Altering prion replication for therapy and diagnosis of transmissible spongiform encephalopathies. Biochem Soc Trans 2002; 30: 569-574.
    • (2002) Biochem Soc Trans , vol.30 , pp. 569-574
    • Soto, C.1
  • 24
    • 0036148226 scopus 로고    scopus 로고
    • Preparing to treat prions
    • Griffiths PD. Preparing to treat prions. Rev Med Virol 2002; 12: 1-3.
    • (2002) Rev Med Virol , vol.12 , pp. 1-3
    • Griffiths, P.D.1
  • 25
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. Self-replication and scrapie. Nature 1967; 215: 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 26
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339-1347.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 27
    • 0034537674 scopus 로고    scopus 로고
    • A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP
    • Meyer RK, Lustig A, Oesch B, Fatzer R, Zurbriggen A, Vandevelde M. A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP. J Biol Chem 2000; 275: 38081-38087.
    • (2000) J Biol Chem , vol.275 , pp. 38081-38087
    • Meyer, R.K.1    Lustig, A.2    Oesch, B.3    Fatzer, R.4    Zurbriggen, A.5    Vandevelde, M.6
  • 28
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90: 10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 29
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem 1991; 266: 18217-18223.
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 30
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in beta-sheet conformations of abnormal prion protein
    • Caughey B, Raymond GJ, Bessen RA. Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J Biol Chem 1998; 273: 32230-32235.
    • (1998) J Biol Chem , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 31
    • 0037071874 scopus 로고    scopus 로고
    • A change in the conformation of prions accompanies the emergence of a new prion strain
    • Peretz D, Williamson RA, Legname G, et al. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 2002; 34: 921-932.
    • (2002) Neuron , vol.34 , pp. 921-932
    • Peretz, D.1    Williamson, R.A.2    Legname, G.3
  • 32
    • 0035753223 scopus 로고    scopus 로고
    • Strain variations and species barriers
    • Hill AF, Collinge J. Strain variations and species barriers. Contrib Microbiol 2001; 7: 48-57.
    • (2001) Contrib Microbiol , vol.7 , pp. 48-57
    • Hill, A.F.1    Collinge, J.2
  • 33
    • 0037447071 scopus 로고    scopus 로고
    • Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene
    • Korth C, Kaneko K, Groth D, et al. Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene. Proc Natl Acad Sci USA 2003; 100: 4784-4789.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4784-4789
    • Korth, C.1    Kaneko, K.2    Groth, D.3
  • 34
    • 0034282971 scopus 로고    scopus 로고
    • Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease
    • Raymond GJ, Bossers A, Raymond LD, et al. Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease. EMBO J 2000; 19: 4425-4430.
    • (2000) EMBO J , vol.19 , pp. 4425-4430
    • Raymond, G.J.1    Bossers, A.2    Raymond, L.D.3
  • 35
    • 0035102994 scopus 로고    scopus 로고
    • Blood simple prion diagnostics
    • Aguzzi A. Blood simple prion diagnostics. Nat Med 2001; 7: 289-290.
    • (2001) Nat Med , vol.7 , pp. 289-290
    • Aguzzi, A.1
  • 36
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • 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: 15922-15928.
    • (1993) J Biol Chem , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 37
    • 0037031821 scopus 로고    scopus 로고
    • Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein
    • Magalhaes AC, Silva JA, Lee KS, et al. Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein. J Biol Chem 2002; 277: 33311-33318.
    • (2002) J Biol Chem , vol.277 , pp. 33311-33318
    • Magalhaes, A.C.1    Silva, J.A.2    Lee, K.S.3
  • 38
    • 0035069622 scopus 로고    scopus 로고
    • The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions
    • Negro A, Ballarin C, Bertoli A, Massimino ML, Sorgato MC. The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions. Mol Cell Neurosci 2001; 17: 521-538.
    • (2001) Mol Cell Neurosci , vol.17 , pp. 521-538
    • Negro, A.1    Ballarin, C.2    Bertoli, A.3    Massimino, M.L.4    Sorgato, M.C.5
  • 39
    • 0034899833 scopus 로고    scopus 로고
    • Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum
    • Laine J, Marc ME, Sy MS, Axelrad H. Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum. Eur J Neurosci 2001; 14: 47-56.
    • (2001) Eur J Neurosci , vol.14 , pp. 47-56
    • Laine, J.1    Marc, M.E.2    Sy, M.S.3    Axelrad, H.4
  • 40
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. Molecular biology of prion diseases. Science 1991; 252: 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 41
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma J, Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci USA 2001; 98: 14955-14960.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 42
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 2002; 298: 1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 43
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J 2001; 20: 5383-5391.
    • (2001) EMBO J , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 44
    • 0035834680 scopus 로고    scopus 로고
    • Mutant prion proteins are partially retained in the endoplasmic reticulum
    • Ivanova L, Barmada S, Kummer T, Harris DA. Mutant prion proteins are partially retained in the endoplasmic reticulum. J Biol Chem 2001; 276: 42409-42421.
    • (2001) J Biol Chem , vol.276 , pp. 42409-42421
    • Ivanova, L.1    Barmada, S.2    Kummer, T.3    Harris, D.A.4
  • 45
    • 0037415754 scopus 로고    scopus 로고
    • Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells
    • Cohen E, Taraboulos A. Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells. EMBO J 2003; 22: 404-417.
    • (2003) EMBO J , vol.22 , pp. 404-417
    • Cohen, E.1    Taraboulos, A.2
  • 46
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi B, Stewart RS, Adles C, et al. Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J Biol Chem 2003; 278: 21732-21743.
    • (2003) J Biol Chem , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3
  • 47
    • 0037064026 scopus 로고    scopus 로고
    • Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells
    • Beranger F, Mange A, Goud B, Lehmann S. Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J Biol Chem 2002; 277: 38972-38977.
    • (2002) J Biol Chem , vol.277 , pp. 38972-38977
    • Beranger, F.1    Mange, A.2    Goud, B.3    Lehmann, S.4
  • 49
    • 0029962468 scopus 로고    scopus 로고
    • Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
    • Vey M, Pilkuhn S, Wille H, et al. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci USA 1996; 93: 14945-14949.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14945-14949
    • Vey, M.1    Pilkuhn, S.2    Wille, H.3
  • 50
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N, Stein R, Yanai A, Friedlander G, Taraboulos A. Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J Biol Chem 1997; 272: 6324-6331.
    • (1997) J Biol Chem , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 51
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko K, Vey M, Scott M, Pilkuhn S, Cohen FE, Prusiner SB. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc Natl Acad Sci USA 1997; 94: 2333-2338.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 52
    • 0036500554 scopus 로고    scopus 로고
    • Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes
    • Baron GS, Wehrly K, Dorward DW, Chesebro B, Caughey B. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J 2002; 21: 1031-1040.
    • (2002) EMBO J , vol.21 , pp. 1031-1040
    • Baron, G.S.1    Wehrly, K.2    Dorward, D.W.3    Chesebro, B.4    Caughey, B.5
  • 53
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, Schmid SL. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Cell Biol 1994; 127: 915-934.
    • (1994) J Cell Biol , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 54
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh P, McIntosh DP, Schnitzer JE. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J Cell Biol 1998; 141: 101-114.
    • (1998) J Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 55
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt DR, Taraboulos A, Prusiner SB. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J Biol Chem 1992; 267: 16188-16199.
    • (1992) J Biol Chem , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 56
    • 0026326210 scopus 로고
    • Ultrastructural localization of scrapie prion proteins in cytoplasmic vesicles of infected cultured cells
    • McKinley MP, Taraboulos A, Kenaga L, et al. Ultrastructural localization of scrapie prion proteins in cytoplasmic vesicles of infected cultured cells. Lab Invest 1991; 65: 622-630.
    • (1991) Lab Invest , vol.65 , pp. 622-630
    • McKinley, M.P.1    Taraboulos, A.2    Kenaga, L.3
  • 57
    • 0029346911 scopus 로고
    • The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain
    • Arnold JE, Tipler C, Laszlo L, Hope J, Landon M, Mayer RJ. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J Pathol 1995; 176: 403-411.
    • (1995) J Pathol , vol.176 , pp. 403-411
    • Arnold, J.E.1    Tipler, C.2    Laszlo, L.3    Hope, J.4    Landon, M.5    Mayer, R.J.6
  • 58
    • 0029054937 scopus 로고
    • The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrincoated pits
    • Shyng SL, Moulder KL, Lesko A, Harris DA. The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrincoated pits. J Biol Chem 1995; 270: 14793-14800.
    • (1995) J Biol Chem , vol.270 , pp. 14793-14800
    • Shyng, S.L.1    Moulder, K.L.2    Lesko, A.3    Harris, D.A.4
  • 59
    • 0034790685 scopus 로고    scopus 로고
    • Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells
    • Lee KS, Magalhaes AC, Zanata SM, Brentani RR, Martins VR, Prado MA. Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells. J Neurochem 2001; 79: 79-87.
    • (2001) J Neurochem , vol.79 , pp. 79-87
    • Lee, K.S.1    Magalhaes, A.C.2    Zanata, S.M.3    Brentani, R.R.4    Martins, V.R.5    Prado, M.A.6
  • 60
    • 0033695126 scopus 로고    scopus 로고
    • Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice
    • Flechsig E, Shmerling D, Hegyi I, et al. Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 2000; 27: 399-408.
    • (2000) Neuron , vol.27 , pp. 399-408
    • Flechsig, E.1    Shmerling, D.2    Hegyi, I.3
  • 61
    • 0035805643 scopus 로고    scopus 로고
    • Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain
    • Horiuchi M, Baron GS, Xiong LW, Caughey B. Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain. J Biol Chem 2001; 276: 15489-15497.
    • (2001) J Biol Chem , vol.276 , pp. 15489-15497
    • Horiuchi, M.1    Baron, G.S.2    Xiong, L.W.3    Caughey, B.4
  • 62
    • 0036791019 scopus 로고    scopus 로고
    • Dominant-negative inhibition of prion replication in transgenic mice
    • Perrier V, Kaneko K, Safar J, et al. Dominant-negative inhibition of prion replication in transgenic mice. Proc Natl Acad Sci USA 2002; 99: 13079-13084.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13079-13084
    • Perrier, V.1    Kaneko, K.2    Safar, J.3
  • 63
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling GC, Scott M, Mastrianni J, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995; 83: 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3
  • 65
    • 0035798377 scopus 로고    scopus 로고
    • Chaperonin-mediated de novo generation of prion protein aggregates
    • Stockel J, Hartl FU. Chaperonin-mediated de novo generation of prion protein aggregates. J Mol Biol 2001; 313: 861-872.
    • (2001) J Mol Biol , vol.313 , pp. 861-872
    • Stockel, J.1    Hartl, F.U.2
  • 66
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro Y, Machado F, Juliano L, et al. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J Biol Chem 2001; 276: 49400-49409.
    • (2001) J Biol Chem , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3
  • 67
    • 0036371353 scopus 로고    scopus 로고
    • PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1
    • Derrington E, Gabus C, Leblanc P, et al. PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C R Acad Sci III 2002; 325: 17-23.
    • (2002) C R Acad Sci III , vol.325 , pp. 17-23
    • Derrington, E.1    Gabus, C.2    Leblanc, P.3
  • 68
    • 0028420936 scopus 로고
    • Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis
    • Priola SA, Caughey B. Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis. Mol Neurobiol 1994; 8: 113-120.
    • (1994) Mol Neurobiol , vol.8 , pp. 113-120
    • Priola, S.A.1    Caughey, B.2
  • 69
    • 0037113169 scopus 로고    scopus 로고
    • Cell-surface prion protein interacts with glycosaminoglycans
    • Pan T, Wong BS, Liu T, Li R, Petersen RB, Sy MS. Cell-surface prion protein interacts with glycosaminoglycans. Biochem J 2002; 368: 81-90.
    • (2002) Biochem J , vol.368 , pp. 81-90
    • Pan, T.1    Wong, B.S.2    Liu, T.3    Li, R.4    Petersen, R.B.5    Sy, M.S.6
  • 70
    • 0035253848 scopus 로고    scopus 로고
    • Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein
    • Wong C, Xiong LW, Horiuchi M, et al. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. EMBO J 2001; 20: 377-386.
    • (2001) EMBO J , vol.20 , pp. 377-386
    • Wong, C.1    Xiong, L.W.2    Horiuchi, M.3
  • 71
    • 17944363361 scopus 로고    scopus 로고
    • The 37-kDa/ 67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein
    • Gauczynski S, Peyrin JM, Haik S, et al. The 37-kDa/ 67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J 2001; 20: 5863-5875.
    • (2001) EMBO J , vol.20 , pp. 5863-5875
    • Gauczynski, S.1    Peyrin, J.M.2    Haik, S.3
  • 72
    • 0034628999 scopus 로고    scopus 로고
    • Cellular prion protein binds laminin and mediates neuritogenesis
    • Graner E, Mercadante AF, Zanata SM, et al. Cellular prion protein binds laminin and mediates neuritogenesis. Brain Res Mol Brain Res 2000; 76: 85-92.
    • (2000) Brain Res Mol Brain Res , vol.76 , pp. 85-92
    • Graner, E.1    Mercadante, A.F.2    Zanata, S.M.3
  • 73
    • 0034613113 scopus 로고    scopus 로고
    • Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein
    • Graner E, Mercadante AF, Zanata SM, Martins VR, Jay DG, Brentani RR. Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein. FEBS Lett 2000; 482: 257-260.
    • (2000) FEBS Lett , vol.482 , pp. 257-260
    • Graner, E.1    Mercadante, A.F.2    Zanata, S.M.3    Martins, V.R.4    Jay, D.G.5    Brentani, R.R.6
  • 75
    • 0035938902 scopus 로고    scopus 로고
    • Plasminogen binds to disease-associated prion protein of multiple species
    • Maissen M, Roeckl C, Glatzel M, Goldmann W, Aguzzi A. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 2001; 357: 2026-2028.
    • (2001) Lancet , vol.357 , pp. 2026-2028
    • Maissen, M.1    Roeckl, C.2    Glatzel, M.3    Goldmann, W.4    Aguzzi, A.5
  • 76
    • 0037018914 scopus 로고    scopus 로고
    • Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner
    • Ellis V, Daniels M, Misra R, Brown D. Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry 2002; 41: 6891-6896.
    • (2002) Biochemistry , vol.41 , pp. 6891-6896
    • Ellis, V.1    Daniels, M.2    Misra, R.3    Brown, D.4
  • 77
    • 0035861987 scopus 로고    scopus 로고
    • Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein
    • Schmitt-Ulms G, Legname G, Baldwin MA, et al. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J Mol Biol 2001; 314: 1209-1225.
    • (2001) J Mol Biol , vol.314 , pp. 1209-1225
    • Schmitt-Ulms, G.1    Legname, G.2    Baldwin, M.A.3
  • 78
    • 0030940607 scopus 로고    scopus 로고
    • Identification of candidate proteins binding to prion protein
    • Yehiely F, Bamborough P, Da Costa M, et al. Identification of candidate proteins binding to prion protein. Neurobiol Dis 1997; 3: 339-355.
    • (1997) Neurobiol Dis , vol.3 , pp. 339-355
    • Yehiely, F.1    Bamborough, P.2    Da Costa, M.3
  • 79
    • 17944377091 scopus 로고    scopus 로고
    • Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor
    • Hundt C, Peyrin JM, Haik S, et al. Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO J 2001; 20: 5876-5886.
    • (2001) EMBO J , vol.20 , pp. 5876-5886
    • Hundt, C.1    Peyrin, J.M.2    Haik, S.3
  • 80
    • 18444397736 scopus 로고    scopus 로고
    • Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection
    • Zanata SM, Lopes MH, Mercadante AF, et al. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J 2002; 21: 3307-3316.
    • (2002) EMBO J , vol.21 , pp. 3307-3316
    • Zanata, S.M.1    Lopes, M.H.2    Mercadante, A.F.3
  • 82
    • 0031466157 scopus 로고    scopus 로고
    • Complementary hydropathy identifies a cellular prion protein receptor
    • Martins VR, Graner E, Garcia-Abreu J, et al. Complementary hydropathy identifies a cellular prion protein receptor. Nat Med 1997; 3: 1376-1382.
    • (1997) Nat Med , vol.3 , pp. 1376-1382
    • Martins, V.R.1    Graner, E.2    Garcia-Abreu, J.3
  • 83
    • 0032557457 scopus 로고    scopus 로고
    • Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides
    • Chabry J, Caughey B, Chesebro B. Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J Biol Chem 1998; 273: 13203-13207.
    • (1998) J Biol Chem , vol.273 , pp. 13203-13207
    • Chabry, J.1    Caughey, B.2    Chesebro, B.3
  • 84
    • 0031036746 scopus 로고    scopus 로고
    • Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
    • Lassle M, Blatch GL, Kundra V, Takatori T, Zetter BR. Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J Biol Chem 1997; 272: 1876-1884.
    • (1997) J Biol Chem , vol.272 , pp. 1876-1884
    • Lassle, M.1    Blatch, G.L.2    Kundra, V.3    Takatori, T.4    Zetter, B.R.5
  • 85
    • 0035977053 scopus 로고    scopus 로고
    • PrPC directly interacts with proteins involved in signaling pathways
    • Spielhaupter C, Schatzl HM. PrPC directly interacts with proteins involved in signaling pathways. J Biol Chem 2001, 276: 44604-44612.
    • (2001) J Biol Chem , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schatzl, H.M.2
  • 86
    • 0035914466 scopus 로고    scopus 로고
    • Neurotrophin p75 receptor is involved in neuronal damage by prion peptide-(106-126)
    • Della-Bianca V, Rossi F, Armato U, et al. Neurotrophin p75 receptor is involved in neuronal damage by prion peptide-(106-126). J Biol Chem 2001; 276: 38929-38933.
    • (2001) J Biol Chem , vol.276 , pp. 38929-38933
    • Della-Bianca, V.1    Rossi, F.2    Armato, U.3
  • 87
  • 88
    • 0034668789 scopus 로고    scopus 로고
    • Bovine prion protein as a modulator of protein kinase CK2
    • Meggio F, Negro A, Sarno S, et al. Bovine prion protein as a modulator of protein kinase CK2. Biochem J 2000; 352: 191-196.
    • (2000) Biochem J , vol.352 , pp. 191-196
    • Meggio, F.1    Negro, A.2    Sarno, S.3
  • 89
    • 0034623960 scopus 로고    scopus 로고
    • The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome
    • Jin T, Gu Y, Zanusso G, et al. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J Biol Chem 2000; 275: 38699-38704.
    • (2000) J Biol Chem , vol.275 , pp. 38699-38704
    • Jin, T.1    Gu, Y.2    Zanusso, G.3
  • 91
    • 0028911161 scopus 로고
    • The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system
    • Kurschner C, Morgan JI. The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Brain Res Mol Brain Res 1995; 30: 165-168.
    • (1995) Brain Res Mol Brain Res , vol.30 , pp. 165-168
    • Kurschner, C.1    Morgan, J.I.2


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