메뉴 건너뛰기




Volumn 116, Issue 2, 2007, Pages 75-82

Prion proteins: A biological role beyond prion diseases

Author keywords

Adaptive immunity; Aging; Alzheimer disease; Cognition; Down syndrome; Innate immunity; Lymphocytes; Neuroprotection; Primary progressive aphasia; Prion protein; Prnp; PrP; PrpC; PrPSc; Wilson disease

Indexed keywords

PRION PROTEIN;

EID: 34547475050     PISSN: 00016314     EISSN: 16000404     Source Type: Journal    
DOI: 10.1111/j.1600-0404.2007.00868.x     Document Type: Review
Times cited : (21)

References (103)
  • 1
    • 0022476747 scopus 로고
    • Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
    • Basler K, Oesch B, Scott M, et al. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 1986 46 : 417 28.
    • (1986) Cell , vol.46 , pp. 417-28
    • Basler, K.1    Oesch, B.2    Scott, M.3
  • 3
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan KM, Stahl N, Prusiner SB. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci 1992 1 : 1343 52.
    • (1992) Protein Sci , vol.1 , pp. 1343-52
    • Pan, K.M.1    Stahl, N.2    Prusiner, S.B.3
  • 4
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw MP, McDermott JR, Candy JM, Lakey JH. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem Biophys Res Commun 1995 214 : 993 9.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 993-9
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 5
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown DR, Qin K, Herms JW, et al. The cellular prion protein binds copper in vivo. Nature 1997 390 : 684 7.
    • (1997) Nature , vol.390 , pp. 684-7
    • Brown, D.R.1    Qin, K.2    Herms, J.W.3
  • 7
    • 0025212147 scopus 로고
    • Cellular isoform of the scrapie agent protein participates in lymphocyte activation
    • Cashman NR, Loertscher R, Nalbantoglu J, et al. Cellular isoform of the scrapie agent protein participates in lymphocyte activation. Cell 1990 61 : 185 92.
    • (1990) Cell , vol.61 , pp. 185-92
    • Cashman, N.R.1    Loertscher, R.2    Nalbantoglu, J.3
  • 8
    • 0033916257 scopus 로고    scopus 로고
    • Differential expression of cellular prion protein on human blood and tonsil lymphocytes
    • Antoine N, Cesbron JY, Coumans B, Jolois O, Zorzi W, Heinen E. Differential expression of cellular prion protein on human blood and tonsil lymphocytes. Haematologica 2000 85 : 475 80.
    • (2000) Haematologica , vol.85 , pp. 475-80
    • Antoine, N.1    Cesbron, J.Y.2    Coumans, B.3    Jolois, O.4    Zorzi, W.5    Heinen, E.6
  • 9
    • 0034088481 scopus 로고    scopus 로고
    • Differential constitutive and activation-dependent expression of prion protein in human peripheral blood leucocytes
    • Durig J, Giese A, Schulz-Schaeffer W, et al. Differential constitutive and activation-dependent expression of prion protein in human peripheral blood leucocytes. Br J Haematol 2000 108 : 488 95.
    • (2000) Br J Haematol , vol.108 , pp. 488-95
    • Durig, J.1    Giese, A.2    Schulz-Schaeffer, W.3
  • 10
    • 0035834915 scopus 로고    scopus 로고
    • The expression and potential function of cellular prion protein in human lymphocytes
    • Li R, Liu D, Zanusso G, et al. The expression and potential function of cellular prion protein in human lymphocytes. Cell Immunol 2001 207 : 49 58.
    • (2001) Cell Immunol , vol.207 , pp. 49-58
    • Li, R.1    Liu, D.2    Zanusso, G.3
  • 11
    • 0035895051 scopus 로고    scopus 로고
    • The normal cellular prion protein is strongly expressed by myeloid dendritic cells
    • Burthem J, Urban B, Pain A, Roberts DJ. The normal cellular prion protein is strongly expressed by myeloid dendritic cells. Blood 2001 98 : 3733 8.
    • (2001) Blood , vol.98 , pp. 3733-8
    • Burthem, J.1    Urban, B.2    Pain, A.3    Roberts, D.J.4
  • 13
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. Molecular biology of prion diseases. Science 1991 252 : 1515 22.
    • (1991) Science , vol.252 , pp. 1515-22
    • Prusiner, S.B.1
  • 14
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987 51 : 229 40.
    • (1987) Cell , vol.51 , pp. 229-40
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 16
    • 0842347567 scopus 로고    scopus 로고
    • Prion deposition in olfactory biopsy of sporadic Creutzfeldt-Jakob disease
    • Tabaton M, Monaco S, Cordone MP, et al. Prion deposition in olfactory biopsy of sporadic Creutzfeldt-Jakob disease. Ann Neurol 2004 55 : 294 6.
    • (2004) Ann Neurol , vol.55 , pp. 294-6
    • Tabaton, M.1    Monaco, S.2    Cordone, M.P.3
  • 17
    • 0030907147 scopus 로고    scopus 로고
    • Biopsy diagnosis of Creutzfeldt-Jakob disease by western blot: A case report
    • Castellani RJ, Parchi P, Madoff L, Gambetti P, Mckeever P. Biopsy diagnosis of Creutzfeldt-Jakob disease by western blot: a case report. Hum Pathol 1997 28 : 623 6.
    • (1997) Hum Pathol , vol.28 , pp. 623-6
    • Castellani, R.J.1    Parchi, P.2    Madoff, L.3    Gambetti, P.4    McKeever, P.5
  • 18
    • 33748857338 scopus 로고    scopus 로고
    • Pathogenesis of prion diseases: Current status and future outlook
    • Aguzzi A, Heikenwalder M. Pathogenesis of prion diseases: current status and future outlook. Nat Rev Microbiol 2006 4 : 765 75.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 765-75
    • Aguzzi, A.1    Heikenwalder, M.2
  • 19
    • 4644259154 scopus 로고    scopus 로고
    • Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes
    • Zanusso G, Farinazzo A, Prelli F, et al. Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes. J Biol Chem 2004 279 : 38936 42.
    • (2004) J Biol Chem , vol.279 , pp. 38936-42
    • Zanusso, G.1    Farinazzo, A.2    Prelli, F.3
  • 20
    • 0036178360 scopus 로고    scopus 로고
    • Two-dimensional mapping of three phenotype-associated isoforms of the prion protein in sporadic Creutzfeldt-Jakob disease
    • Zanusso G, Righetti PG, Ferrari S, et al. Two-dimensional mapping of three phenotype-associated isoforms of the prion protein in sporadic Creutzfeldt-Jakob disease. Electrophoresis 2002 23 : 347 55.
    • (2002) Electrophoresis , vol.23 , pp. 347-55
    • Zanusso, G.1    Righetti, P.G.2    Ferrari, S.3
  • 21
    • 0028351904 scopus 로고
    • Fatal familial insomnia and familial Creutzfeldt-Jakob disease: Different prion proteins determined by a DNA polymorphism
    • Monari L, Chen SG, Brown P, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism. Proc Natl Acad Sci USA 1994 91 : 2839 42.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2839-42
    • Monari, L.1    Chen, S.G.2    Brown, P.3
  • 23
    • 0025800143 scopus 로고
    • A 'unified theory' of prion propagation
    • Weissmann C. A 'unified theory' of prion propagation. Nature 1991 352 : 679 83.
    • (1991) Nature , vol.352 , pp. 679-83
    • Weissmann, C.1
  • 24
    • 28444431651 scopus 로고    scopus 로고
    • Clinical and differential diagnosis of Creutzfeldt-Jakob disease
    • Poser S, Zerr I, Schroeter A, et al. Clinical and differential diagnosis of Creutzfeldt-Jakob disease. Arch Virol Suppl 2000 16 : 153 9.
    • (2000) Arch Virol Suppl , vol.16 , pp. 153-9
    • Poser, S.1    Zerr, I.2    Schroeter, A.3
  • 25
    • 0345621492 scopus 로고    scopus 로고
    • Pathology of variant Creutzfeldt-Jakob disease
    • Ironside JW. Pathology of variant Creutzfeldt-Jakob disease. Arch Virol Suppl 2000 16 : 143 51.
    • (2000) Arch Virol Suppl , vol.16 , pp. 143-51
    • Ironside, J.W.1
  • 27
    • 33748743547 scopus 로고    scopus 로고
    • Gerstmann-Straussler-Scheinker disease. I. human diseases
    • Liberski PP, Budka H. Gerstmann-Straussler-Scheinker disease. I. human diseases. Folia Neuropathol 2004 42 (Suppl. B 120 40.
    • (2004) Folia Neuropathol , vol.42 , pp. 120-40
    • Liberski, P.P.1    Budka, H.2
  • 29
    • 0032747378 scopus 로고    scopus 로고
    • How to improve the clinical diagnosis of Creutzfeldt-Jakob disease
    • Poser S, Mollenhauer B, Kraubeta A, et al. How to improve the clinical diagnosis of Creutzfeldt-Jakob disease. Brain 1999 122 (Pt 12 2345 51.
    • (1999) Brain , vol.122 , Issue.12 , pp. 2345-51
    • Poser, S.1    Mollenhauer, B.2    Kraubeta, A.3
  • 30
    • 33751395467 scopus 로고    scopus 로고
    • Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep
    • Picard-Hagen N, Gayrard V, Viguie C, Moudjou M, Imbs C, Toutain PL. Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep. J Gen Virol 2006 87 (Pt 12 3723 7.
    • (2006) J Gen Virol , vol.87 , Issue.12 , pp. 3723-7
    • Picard-Hagen, N.1    Gayrard, V.2    Viguie, C.3    Moudjou, M.4    Imbs, C.5    Toutain, P.L.6
  • 31
    • 33747689817 scopus 로고    scopus 로고
    • CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease
    • Sanchez-Juan P, Green A, Ladogana A, et al. CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology 2006 67 : 637 43.
    • (2006) Neurology , vol.67 , pp. 637-43
    • Sanchez-Juan, P.1    Green, A.2    Ladogana, A.3
  • 32
    • 33644877815 scopus 로고    scopus 로고
    • Diagnostic value of 14-3-3beta immunoblot and T-tau/P-tau ratio in clinically suspected Creutzfeldt-Jakob disease
    • Blennow K, Johansson A, Zetterberg H. Diagnostic value of 14-3-3beta immunoblot and T-tau/P-tau ratio in clinically suspected Creutzfeldt-Jakob disease. Int J Mol Med 2005 16 : 1147 9.
    • (2005) Int J Mol Med , vol.16 , pp. 1147-9
    • Blennow, K.1    Johansson, A.2    Zetterberg, H.3
  • 33
    • 33645750334 scopus 로고    scopus 로고
    • Emerging pharmacotherapies for Creutzfeldt-Jakob disease
    • Korth C, Peters PJ. Emerging pharmacotherapies for Creutzfeldt-Jakob disease. Arch Neurol 2006 63 : 497 501.
    • (2006) Arch Neurol , vol.63 , pp. 497-501
    • Korth, C.1    Peters, P.J.2
  • 34
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D, Williamson RA, Kaneko K, et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 2001 412 : 739 43.
    • (2001) Nature , vol.412 , pp. 739-43
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3
  • 35
    • 0037422133 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit prion replication and delay the development of prion disease
    • White AR, Enever P, Tayebi M, et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 2003 422 : 80 83.
    • (2003) Nature , vol.422 , pp. 80-83
    • White, A.R.1    Enever, P.2    Tayebi, M.3
  • 37
    • 0038783253 scopus 로고    scopus 로고
    • Specific inhibition of pathological prion protein accumulation by small interfering RNAs
    • Daude N, Marella M, Chabry J. Specific inhibition of pathological prion protein accumulation by small interfering RNAs. J Cell Sci 2003 116 (Pt 13 2775 9.
    • (2003) J Cell Sci , vol.116 , Issue.13 , pp. 2775-9
    • Daude, N.1    Marella, M.2    Chabry, J.3
  • 38
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth C, May BC, Cohen FE, Prusiner SB. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci USA 2001 98 : 9836 41.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9836-41
    • Korth, C.1    May, B.C.2    Cohen, F.E.3    Prusiner, S.B.4
  • 40
    • 14644389457 scopus 로고    scopus 로고
    • A possible pharmacological explanation for quinacrine failure to treat prion diseases: Pharmacokinetic investigations in a ovine model of scrapie
    • Gayrard V, Picard-Hagen N, Viguie C, Laroute V, Andreoletti O, Toutain PL. A possible pharmacological explanation for quinacrine failure to treat prion diseases: pharmacokinetic investigations in a ovine model of scrapie. Br J Pharmacol 2005 144 : 386 93.
    • (2005) Br J Pharmacol , vol.144 , pp. 386-93
    • Gayrard, V.1    Picard-Hagen, N.2    Viguie, C.3    Laroute, V.4    Andreoletti, O.5    Toutain, P.L.6
  • 41
    • 0032843132 scopus 로고    scopus 로고
    • Molecular genetics of human prion diseases in Germany
    • Windl O, Giese A, Schulz-Schaeffer W, et al. Molecular genetics of human prion diseases in Germany. Hum Genet 1999 105 : 244 52.
    • (1999) Hum Genet , vol.105 , pp. 244-52
    • Windl, O.1    Giese, A.2    Schulz-Schaeffer, W.3
  • 42
    • 0026496257 scopus 로고
    • Fatal familial insomnia and familial Creutzfeldt-Jakob disease: Disease phenotype determined by a DNA polymorphism
    • Goldfarb LG, Petersen RB, Tabaton M, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism. Science 1992 258 : 806 8.
    • (1992) Science , vol.258 , pp. 806-8
    • Goldfarb, L.G.1    Petersen, R.B.2    Tabaton, M.3
  • 43
    • 0026849545 scopus 로고
    • Linkage of the Indiana kindred of Gerstmann-Straussler-Scheinker disease to the prion protein gene
    • Dlouhy SR, Hsiao K, Farlow MR, et al. Linkage of the Indiana kindred of Gerstmann-Straussler-Scheinker disease to the prion protein gene. Nat Genet 1992 1 : 64 7.
    • (1992) Nat Genet , vol.1 , pp. 64-7
    • Dlouhy, S.R.1    Hsiao, K.2    Farlow, M.R.3
  • 44
    • 0037372585 scopus 로고    scopus 로고
    • PRNP Val129 homozygosity increases risk for early-onset Alzheimer's disease
    • Dermaut B, Croes EA, Rademakers R, et al. PRNP Val129 homozygosity increases risk for early-onset Alzheimer's disease. Ann Neurol 2003 53 : 409 12.
    • (2003) Ann Neurol , vol.53 , pp. 409-12
    • Dermaut, B.1    Croes, E.A.2    Rademakers, R.3
  • 45
    • 0842325637 scopus 로고    scopus 로고
    • Polymorphisms within the prion (PrP) and prion-like protein (Doppel) genes in AD
    • Golanska E, Hulas-Bigoszewska K, Rutkiewicz E, et al. Polymorphisms within the prion (PrP) and prion-like protein (Doppel) genes in AD. Neurology 2004 62 : 313 5.
    • (2004) Neurology , vol.62 , pp. 313-5
    • Golanska, E.1    Hulas-Bigoszewska, K.2    Rutkiewicz, E.3
  • 46
    • 0038796590 scopus 로고    scopus 로고
    • The 129 codon polymorphism of the prion protein gene influences earlier cognitive performance in Down syndrome subjects
    • Del Bo R, Comi GP, Giorda R, et al. The 129 codon polymorphism of the prion protein gene influences earlier cognitive performance in Down syndrome subjects. J Neurol 2003 250 : 688 92.
    • (2003) J Neurol , vol.250 , pp. 688-92
    • Del Bo, R.1    Comi, G.P.2    Giorda, R.3
  • 47
    • 28644447668 scopus 로고    scopus 로고
    • Prion protein codon 129 genotype prevalence is altered in primary progressive aphasia
    • Li X, Rowland LP, Mitsumoto H, et al. Prion protein codon 129 genotype prevalence is altered in primary progressive aphasia. Ann Neurol 2005 58 : 858 64.
    • (2005) Ann Neurol , vol.58 , pp. 858-64
    • Li, X.1    Rowland, L.P.2    Mitsumoto, H.3
  • 48
    • 33645130155 scopus 로고    scopus 로고
    • Prion protein gene codon 129 modulates clinical course of neurological Wilson disease
    • Grubenbecher S, Stuve O, Hefter H, Korth C. Prion protein gene codon 129 modulates clinical course of neurological Wilson disease. Neuroreport 2006 17 : 549 52.
    • (2006) Neuroreport , vol.17 , pp. 549-52
    • Grubenbecher, S.1    Stuve, O.2    Hefter, H.3    Korth, C.4
  • 49
    • 33745825195 scopus 로고    scopus 로고
    • Influence of homozygosity for methionine at codon 129 of the human prion gene on the onset of neurological and hepatic symptoms in Wilson disease
    • Merle U, Stremmel W, Gessner R. Influence of homozygosity for methionine at codon 129 of the human prion gene on the onset of neurological and hepatic symptoms in Wilson disease. Arch Neurol 2006 63 : 982 5.
    • (2006) Arch Neurol , vol.63 , pp. 982-5
    • Merle, U.1    Stremmel, W.2    Gessner, R.3
  • 51
    • 0031752715 scopus 로고    scopus 로고
    • Polymorphism of the prion protein is associated with cognitive impairment in the elderly: The EVA study
    • Berr C, Richard F, Dufouil C, Amant C, Alperovitch A, Amouyel P. Polymorphism of the prion protein is associated with cognitive impairment in the elderly: the EVA study. Neurology 1998 51 : 734 7.
    • (1998) Neurology , vol.51 , pp. 734-7
    • Berr, C.1    Richard, F.2    Dufouil, C.3    Amant, C.4    Alperovitch, A.5    Amouyel, P.6
  • 52
    • 0041843758 scopus 로고    scopus 로고
    • Early cognitive decline is associated with prion protein codon 129 polymorphism
    • Croes EA, Dermaut B, Houwing-Duistermaat JJ, et al. Early cognitive decline is associated with prion protein codon 129 polymorphism. Ann Neurol 2003 54 : 275 6.
    • (2003) Ann Neurol , vol.54 , pp. 275-6
    • Croes, E.A.1    Dermaut, B.2    Houwing-Duistermaat, J.J.3
  • 53
    • 10744222194 scopus 로고    scopus 로고
    • Surgical outcome in mesial temporal sclerosis correlates with prion protein gene variant
    • Walz R, Castro RM, Velasco TR, et al. Surgical outcome in mesial temporal sclerosis correlates with prion protein gene variant. Neurology 2003 61 : 1204 10.
    • (2003) Neurology , vol.61 , pp. 1204-10
    • Walz, R.1    Castro, R.M.2    Velasco, T.R.3
  • 54
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H, Fischer M, Lang Y, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992 356 : 577 82.
    • (1992) Nature , vol.356 , pp. 577-82
    • Bueler, H.1    Fischer, M.2    Lang, Y.3
  • 55
    • 0033215478 scopus 로고    scopus 로고
    • Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
    • Moore RC, Lee IY, Silverman GL, et al. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol 1999 292 : 797 817.
    • (1999) J Mol Biol , vol.292 , pp. 797-817
    • Moore, R.C.1    Lee, I.Y.2    Silverman, G.L.3
  • 56
    • 13344282734 scopus 로고    scopus 로고
    • Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene
    • Sakaguchi S, Katamine S, Nishida N, et al. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996 380 : 528 31.
    • (1996) Nature , vol.380 , pp. 528-31
    • Sakaguchi, S.1    Katamine, S.2    Nishida, N.3
  • 57
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson JC, Clarke AR, Hooper ML, Aitchison L, McConnell I, Hope J. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 1994 8 : 121 7.
    • (1994) Mol Neurobiol , vol.8 , pp. 121-7
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 58
    • 0033049539 scopus 로고    scopus 로고
    • A mouse prion protein transgene rescues mice deficient for the prion protein gene from purkinje cell degeneration and demyelination
    • Nishida N, Tremblay P, Sugimoto T, et al. A mouse prion protein transgene rescues mice deficient for the prion protein gene from purkinje cell degeneration and demyelination. Lab Invest 1999 79 : 689 97.
    • (1999) Lab Invest , vol.79 , pp. 689-97
    • Nishida, N.1    Tremblay, P.2    Sugimoto, T.3
  • 59
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • Rossi D, Cozzio A, Flechsig E, et al. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J 2001 20 : 694 702.
    • (2001) EMBO J , vol.20 , pp. 694-702
    • Rossi, D.1    Cozzio, A.2    Flechsig, E.3
  • 60
    • 0034282872 scopus 로고    scopus 로고
    • Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss
    • Silverman GL, Qin K, Moore RC, et al. Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored 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 : 26834 41.
    • (2000) J Biol Chem , vol.275 , pp. 26834-41
    • Silverman, G.L.1    Qin, K.2    Moore, R.C.3
  • 61
    • 0141738255 scopus 로고    scopus 로고
    • PrP knock-out and PrP transgenic mice in prion research
    • Weissmann C, Flechsig E. PrP knock-out and PrP transgenic mice in prion research. Br Med Bull 2003 66 : 43 60.
    • (2003) Br Med Bull , vol.66 , pp. 43-60
    • Weissmann, C.1    Flechsig, E.2
  • 62
    • 0028876414 scopus 로고
    • Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent
    • Race RE, Priola SA, Bessen RA, et al. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron 1995 15 : 1183 91.
    • (1995) Neuron , vol.15 , pp. 1183-91
    • Race, R.E.1    Priola, S.A.2    Bessen, R.A.3
  • 63
    • 0030684056 scopus 로고    scopus 로고
    • Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie
    • Raeber AJ, Race RE, Brandner S, et al. Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie. EMBO J 1997 16 : 6057 65.
    • (1997) EMBO J , vol.16 , pp. 6057-65
    • Raeber, A.J.1    Race, R.E.2    Brandner, S.3
  • 64
    • 0031759918 scopus 로고    scopus 로고
    • PrP expression in B lymphocytes is not required for prion neuroinvasion
    • Klein MA, Frigg R, Raeber AJ, et al. PrP expression in B lymphocytes is not required for prion neuroinvasion. Nat Med 1998 4 : 1429 33.
    • (1998) Nat Med , vol.4 , pp. 1429-33
    • Klein, M.A.1    Frigg, R.2    Raeber, A.J.3
  • 65
    • 0033616564 scopus 로고    scopus 로고
    • Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication
    • Raeber AJ, Sailer A, Hegyi I, et al. Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication. Proc Natl Acad Sci USA 1999 96 : 3987 92.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3987-92
    • Raeber, A.J.1    Sailer, A.2    Hegyi, I.3
  • 66
    • 33644839257 scopus 로고    scopus 로고
    • Overexpression of cellular prion protein induces an antioxidant environment altering T cell development in the thymus
    • Jouvin-Marche E, Attuil-Audenis V, Aude-Garcia C, et al. Overexpression of cellular prion protein induces an antioxidant environment altering T cell development in the thymus. J Immunol 2006 176 : 3490 97.
    • (2006) J Immunol , vol.176 , pp. 3490-97
    • Jouvin-Marche, E.1    Attuil-Audenis, V.2    Aude-Garcia, C.3
  • 67
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, Rulicke T, Raeber A, et al. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 1996 15 : 1255 64.
    • (1996) EMBO J , vol.15 , pp. 1255-64
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3
  • 68
    • 0025270288 scopus 로고
    • The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells
    • Brown HR, Goller NL, Rudelli RD, et al. The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathol (Berl) 1990 80 : 1 6.
    • (1990) Acta Neuropathol (Berl) , vol.80 , pp. 1-6
    • Brown, H.R.1    Goller, N.L.2    Rudelli, R.D.3
  • 69
    • 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 : 696 703.
    • (2002) Mamm Genome , vol.13 , pp. 696-703
    • Makrinou, E.1    Collinge, J.2    Antoniou, M.3
  • 72
    • 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, Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J Cell Biol 2005 169 : 341 54.
    • (2005) J Cell Biol , vol.169 , pp. 341-54
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Schachner, M.4
  • 73
    • 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, Schachner M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol Cell Neurosci 2003 22 : 227 33.
    • (2003) Mol Cell Neurosci , vol.22 , pp. 227-33
    • Chen, S.1    Mange, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 74
    • 0346729697 scopus 로고    scopus 로고
    • Neuroprotective functions of prion protein
    • Roucou X, Gains M, LeBlanc AC. Neuroprotective functions of prion protein. J Neurosci Res 2004 75 : 153 61.
    • (2004) J Neurosci Res , vol.75 , pp. 153-61
    • Roucou, X.1    Gains, M.2    Leblanc, A.C.3
  • 75
    • 0033566067 scopus 로고    scopus 로고
    • Prions prevent neuronal cell-line death
    • Kuwahara C, Takeuchi AM, Nishimura T, et al. Prions prevent neuronal cell-line death. Nature 1999 400 : 225 6.
    • (1999) Nature , vol.400 , pp. 225-6
    • Kuwahara, C.1    Takeuchi, A.M.2    Nishimura, T.3
  • 76
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Bounhar Y, Zhang Y, Goodyer CG, LeBlanc A. Prion protein protects human neurons against Bax-mediated apoptosis. J Biol Chem 2001 276 : 39145 9.
    • (2001) J Biol Chem , vol.276 , pp. 39145-9
    • Bounhar, Y.1    Zhang, Y.2    Goodyer, C.G.3    Leblanc, A.4
  • 78
    • 12844257374 scopus 로고    scopus 로고
    • Cellular prion protein neuroprotective function: Implications in prion diseases
    • Roucou X, LeBlanc AC. Cellular prion protein neuroprotective function: implications in prion diseases. J Mol Med 2005 83 : 3 11.
    • (2005) J Mol Med , vol.83 , pp. 3-11
    • Roucou, X.1    Leblanc, A.C.2
  • 79
    • 33746417936 scopus 로고    scopus 로고
    • Doppel-induced apoptosis and counteraction by cellular prion protein in neuroblastoma and astrocytes
    • Qin K, Zhao L, Tang Y, Bhatta S, Simard JM, Zhao RY. Doppel-induced apoptosis and counteraction by cellular prion protein in neuroblastoma and astrocytes. Neuroscience 2006 141 : 1375 88.
    • (2006) Neuroscience , vol.141 , pp. 1375-88
    • Qin, K.1    Zhao, L.2    Tang, Y.3    Bhatta, S.4    Simard, J.M.5    Zhao, R.Y.6
  • 80
    • 12144288766 scopus 로고    scopus 로고
    • Neuron-specific mRNA complexity responses during hippocampal apoptosis after traumatic brain injury
    • Marciano PG, Brettschneider J, Manduchi E, et al. Neuron-specific mRNA complexity responses during hippocampal apoptosis after traumatic brain injury. J Neurosci 2004 24 : 2866 76.
    • (2004) J Neurosci , vol.24 , pp. 2866-76
    • Marciano, P.G.1    Brettschneider, J.2    Manduchi, E.3
  • 82
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D, Hegyi I, Fischer M, et al. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 1998 93 : 203 14.
    • (1998) Cell , vol.93 , pp. 203-14
    • Shmerling, D.1    Hegyi, I.2    Fischer, M.3
  • 85
    • 0345687168 scopus 로고    scopus 로고
    • NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
    • Schneider B, Mutel V, Pietri M, Ermonval M, Mouillet-Richard S, Kellermann O. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc Natl Acad Sci USA 2003 100 : 13326 31.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13326-31
    • Schneider, B.1    Mutel, V.2    Pietri, M.3    Ermonval, M.4    Mouillet-Richard, S.5    Kellermann, O.6
  • 86
    • 0030890097 scopus 로고    scopus 로고
    • Mossy fibre reorganization in the hippocampus of prion protein null mice
    • Colling SB, Khana M, Collinge J, Jefferys JG. Mossy fibre reorganization in the hippocampus of prion protein null mice. Brain Res 1997 755 : 28 35.
    • (1997) Brain Res , vol.755 , pp. 28-35
    • Colling, S.B.1    Khana, M.2    Collinge, J.3    Jefferys, J.G.4
  • 87
    • 15844421385 scopus 로고    scopus 로고
    • Altered circadian activity rhythms and sleep in mice devoid of prion protein
    • Tobler I, Gaus SE, Deboer T, et al. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996 380 : 639 42.
    • (1996) Nature , vol.380 , pp. 639-42
    • Tobler, I.1    Gaus, S.E.2    Deboer, T.3
  • 89
    • 20244371991 scopus 로고    scopus 로고
    • Mice devoid of prion protein have cognitive deficits that are rescued by reconstitution of PrP in neurons
    • Criado JR, Sanchez-Alavez M, Conti B, et al. Mice devoid of prion protein have cognitive deficits that are rescued by reconstitution of PrP in neurons. Neurobiol Dis 2005 19 : 255 65.
    • (2005) Neurobiol Dis , vol.19 , pp. 255-65
    • Criado, J.R.1    Sanchez-Alavez, M.2    Conti, B.3
  • 90
    • 0029971378 scopus 로고    scopus 로고
    • Hippocampal slices from prion protein null mice: Disrupted Ca(2+)-activated K+ currents
    • Colling SB, Collinge J, Jefferys JG. Hippocampal slices from prion protein null mice: disrupted Ca(2+)-activated K+ currents. Neurosci Lett 1996 209 : 49 52.
    • (1996) Neurosci Lett , vol.209 , pp. 49-52
    • Colling, S.B.1    Collinge, J.2    Jefferys, J.G.3
  • 92
    • 0032806450 scopus 로고    scopus 로고
    • Increased sensitivity to seizures in mice lacking cellular prion protein
    • Walz R, Amaral OB, Rockenbach IC, et al. Increased sensitivity to seizures in mice lacking cellular prion protein. Epilepsia 1999 40 : 1679 82.
    • (1999) Epilepsia , vol.40 , pp. 1679-82
    • Walz, R.1    Amaral, O.B.2    Rockenbach, I.C.3
  • 93
    • 33646695909 scopus 로고    scopus 로고
    • Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury
    • Weise J, Sandau R, Schwarting S, et al. Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury. Stroke 2006 37 : 1296 300.
    • (2006) Stroke , vol.37 , pp. 1296-300
    • Weise, J.1    Sandau, R.2    Schwarting, S.3
  • 94
    • 26944460813 scopus 로고    scopus 로고
    • Female-specific neuroprotection against transient brain ischemia observed in mice devoid of prion protein is abolished by ectopic expression of prion protein-like protein
    • Sakurai-Yamashita Y, Sakaguchi S, Yoshikawa D, et al. Female-specific neuroprotection against transient brain ischemia observed in mice devoid of prion protein is abolished by ectopic expression of prion protein-like protein. Neuroscience 2005 136 : 281 7.
    • (2005) Neuroscience , vol.136 , pp. 281-7
    • Sakurai-Yamashita, Y.1    Sakaguchi, S.2    Yoshikawa, D.3
  • 95
    • 25644433562 scopus 로고    scopus 로고
    • Overexpression of PrPC by adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model
    • Shyu WC, Lin SZ, Chiang MF, et al. Overexpression of PrPC by adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model. J Neurosci 2005 25 : 8967 77.
    • (2005) J Neurosci , vol.25 , pp. 8967-77
    • Shyu, W.C.1    Lin, S.Z.2    Chiang, M.F.3
  • 96
    • 26944462341 scopus 로고    scopus 로고
    • Aggravation of ischemic brain injury by prion protein deficiency: Role of ERK-1/-2 and STAT-1
    • Spudich A, Frigg R, Kilic E, et al. Aggravation of ischemic brain injury by prion protein deficiency: role of ERK-1/-2 and STAT-1. Neurobiol Dis 2005 20 : 442 9.
    • (2005) Neurobiol Dis , vol.20 , pp. 442-9
    • Spudich, A.1    Frigg, R.2    Kilic, E.3
  • 97
    • 33750372639 scopus 로고    scopus 로고
    • Prion protein expression by mouse dendritic cells is restricted to the nonplasmacytoid subsets and correlates with the maturation state
    • Martinez Del Hoyo G, Lopez-Bravo M, Metharom P, Ardavin C, Aucouturier P. Prion protein expression by mouse dendritic cells is restricted to the nonplasmacytoid subsets and correlates with the maturation state. J Immunol 2006 177 : 6137 42.
    • (2006) J Immunol , vol.177 , pp. 6137-42
    • Martinez Del Hoyo, G.1    Lopez-Bravo, M.2    Metharom, P.3    Ardavin, C.4    Aucouturier, P.5
  • 98
    • 33744905327 scopus 로고    scopus 로고
    • Functional implication of cellular prion protein in antigen-driven interactions between T cells and dendritic cells
    • Ballerini C, Gourdain P, Bachy V, et al. Functional implication of cellular prion protein in antigen-driven interactions between T cells and dendritic cells. J Immunol 2006 176 : 7254 62.
    • (2006) J Immunol , vol.176 , pp. 7254-62
    • Ballerini, C.1    Gourdain, P.2    Bachy, V.3
  • 100
    • 0033624049 scopus 로고    scopus 로고
    • Age-related expression of the cellular prion protein in human peripheral blood leukocytes
    • Politopoulou G, Seebach JD, Schmugge M, Schwarz HP, Aguzzi A. Age-related expression of the cellular prion protein in human peripheral blood leukocytes. Haematologica 2000 85 : 580 87.
    • (2000) Haematologica , vol.85 , pp. 580-87
    • Politopoulou, G.1    Seebach, J.D.2    Schmugge, M.3    Schwarz, H.P.4    Aguzzi, A.5
  • 101
    • 1342329324 scopus 로고    scopus 로고
    • Prion protein is a component of the multimolecular signaling complex involved in T cell activation
    • Mattei V, Garofalo T, Misasi R, et al. Prion protein is a component of the multimolecular signaling complex involved in T cell activation. FEBS Lett 2004 560 : 14 8.
    • (2004) FEBS Lett , vol.560 , pp. 14-8
    • Mattei, V.1    Garofalo, T.2    Misasi, R.3
  • 102
    • 10044234042 scopus 로고    scopus 로고
    • The normal cellular form of prion protein modulates T cell responses
    • Bainbridge J, Walker KB. The normal cellular form of prion protein modulates T cell responses. Immunol Lett 2005 96 : 147 50.
    • (2005) Immunol Lett , vol.96 , pp. 147-50
    • Bainbridge, J.1    Walker, K.B.2
  • 103
    • 0030850688 scopus 로고    scopus 로고
    • T-lymphocyte activation and the cellular form of the prion protein
    • Mabbott NA, Brown KL, Manson J, Bruce ME. T-lymphocyte activation and the cellular form of the prion protein. Immunology 1997 92 : 161 5.
    • (1997) Immunology , vol.92 , pp. 161-5
    • Mabbott, N.A.1    Brown, K.L.2    Manson, J.3    Bruce, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.