메뉴 건너뛰기




Volumn 2, Issue C, 1997, Pages 99-111

Synaptic Aspects of the Cellular Prion Protein

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0002182423     PISSN: 15692590     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2590(08)60182-2     Document Type: Article
Times cited : (6)

References (57)
  • 1
    • 0027283062 scopus 로고
    • Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions
    • Askanas V., Bilak M., King Engel W., Leclerc A., and Tomé F. Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions. Neurosc. Lett. 159 (1993) 111-114
    • (1993) Neurosc. Lett. , vol.159 , pp. 111-114
    • Askanas, V.1    Bilak, M.2    King Engel, W.3    Leclerc, A.4    Tomé, F.5
  • 3
    • 0027731067 scopus 로고
    • Neuropathology of spongiform encephalopathies in humans
    • Bell J.E., and Ironside J.W. Neuropathology of spongiform encephalopathies in humans. Br. Med. Bull. 49 (1993) 738-777
    • (1993) Br. Med. Bull. , vol.49 , pp. 738-777
    • Bell, J.E.1    Ironside, J.W.2
  • 6
    • 0028931088 scopus 로고
    • Electronmicroscopic detection of prion-protein-fibers in brain from iatrogenic Creutzfeldt-Jakob disease
    • Billette de Villemeur T., Fournier J.-G., Escaig-Haye F., Robain O., and Brown P. Electronmicroscopic detection of prion-protein-fibers in brain from iatrogenic Creutzfeldt-Jakob disease. Lancet 345 (1995) 861-862
    • (1995) Lancet , vol.345 , pp. 861-862
    • Billette de Villemeur, T.1    Fournier, J.-G.2    Escaig-Haye, F.3    Robain, O.4    Brown, P.5
  • 7
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion protein in the endocytic pathway
    • Borchelt D.R., Taraboulos A., and Prusiner S.B. Evidence for synthesis of scrapie prion protein in the endocytic pathway. J. Biol. Chem. 267 (1992) 16188-16199
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 8
    • 0028356488 scopus 로고
    • Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous system
    • Borchelt D.R., Koliatsos V.E., Guarnieri M., Pardo C.A., Sisodia S.S., and Price D.L. Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous system. J. Biol. Chem. 269 (1994) 14711-14714
    • (1994) J. Biol. Chem. , vol.269 , pp. 14711-14714
    • Borchelt, D.R.1    Koliatsos, V.E.2    Guarnieri, M.3    Pardo, C.A.4    Sisodia, S.S.5    Price, D.L.6
  • 10
    • 0022639482 scopus 로고
    • Diagnosis of Creutzfeldt-Jakob disease by Western blot identification of marker protein in human brain tissue
    • Brown P., Coker-Vann M., Pomeroy K., Franko M., Asher D., Gibbs C., and Gajdusek D.C. Diagnosis of Creutzfeldt-Jakob disease by Western blot identification of marker protein in human brain tissue. N. Engl. J. Med. 314 (1986) 547-551
    • (1986) N. Engl. J. Med. , vol.314 , pp. 547-551
    • Brown, P.1    Coker-Vann, M.2    Pomeroy, K.3    Franko, M.4    Asher, D.5    Gibbs, C.6    Gajdusek, D.C.7
  • 11
    • 0025809862 scopus 로고
    • The new biology of spongiform encephalopathy: infectious amyloidoses with a genetic twist
    • Brown P., Goldfarb L.G., and Gajdusek D.C. The new biology of spongiform encephalopathy: infectious amyloidoses with a genetic twist. Lancet. 337 (1991) 1019-1022
    • (1991) Lancet. , vol.337 , pp. 1019-1022
    • Brown, P.1    Goldfarb, L.G.2    Gajdusek, D.C.3
  • 13
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler H., Fischer M., and Lang Y. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356 (1992) 577-658
    • (1992) Nature , vol.356 , pp. 577-658
    • Büeler, H.1    Fischer, M.2    Lang, Y.3
  • 15
    • 0023860332 scopus 로고
    • Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines
    • Caughey B., Race R.E., and Chesebro B. Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines. J. Gen. Virol. 69 (1988) 711-716
    • (1988) J. Gen. Virol. , vol.69 , pp. 711-716
    • Caughey, B.1    Race, R.E.2    Chesebro, B.3
  • 16
    • 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., and Raymond G.J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease and phospholipase sensitive. J. Biol. Chem. 266 (1991) 18217-18223
    • (1991) J. Biol. Chem. , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 17
    • 0027394220 scopus 로고
    • Synaptic degeneration is the primary neuropathological feature in prion disease: A reliminary study
    • Clinton J., Forsyth C., Royston M.C., and Roberts G.W. Synaptic degeneration is the primary neuropathological feature in prion disease: A reliminary study. Neuroreport. 4 (1993) 65-68
    • (1993) Neuroreport. , vol.4 , pp. 65-68
    • Clinton, J.1    Forsyth, C.2    Royston, M.C.3    Roberts, G.W.4
  • 20
    • 0023235753 scopus 로고
    • Changes in the localization of brain prion proteins during scrapie infection
    • DeArmond S., Mobley W., DeMott D., Barry R., Beckstead J., and Prusiner S.B. Changes in the localization of brain prion proteins during scrapie infection. Neurology 87 (1987) 1271-1280
    • (1987) Neurology , vol.87 , pp. 1271-1280
    • DeArmond, S.1    Mobley, W.2    DeMott, D.3    Barry, R.4    Beckstead, J.5    Prusiner, S.B.6
  • 21
    • 0028922696 scopus 로고
    • Etiology and pathogenesis of prion diseases
    • DeArmond S.J., and Prusiner S.B. Etiology and pathogenesis of prion diseases. Am. J. Pathol. 146 (1995) 785-811
    • (1995) Am. J. Pathol. , vol.146 , pp. 785-811
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 23
    • 0025826175 scopus 로고
    • Immunoreactivity of cerebral amyloidosis is enhanced by protein denaturation treatments
    • Doi-Yi R., Kitamoto T., and Tateishi J. Immunoreactivity of cerebral amyloidosis is enhanced by protein denaturation treatments. Acta. Neuropathol. 82 (1991) 260-265
    • (1991) Acta. Neuropathol. , vol.82 , pp. 260-265
    • Doi-Yi, R.1    Kitamoto, T.2    Tateishi, J.3
  • 24
    • 0029112533 scopus 로고
    • Ultrastuctural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus
    • Fournier J.G., Escaig-Haye F., Billette de Villemeur T., and Robain O. Ultrastuctural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus. C.R. Acad. Sci. 318 (1995) 339-344
    • (1995) C.R. Acad. Sci. , vol.318 , pp. 339-344
    • Fournier, J.G.1    Escaig-Haye, F.2    Billette de Villemeur, T.3    Robain, O.4
  • 25
    • 0027731068 scopus 로고
    • Genetic control of nucleation and polymerization of host precursors to infectious amyloids in the transmissable amyloidoses in brain
    • Gajdusek D.C. Genetic control of nucleation and polymerization of host precursors to infectious amyloids in the transmissable amyloidoses in brain. Br. Med. Bull. 49 (1993) 913-931
    • (1993) Br. Med. Bull. , vol.49 , pp. 913-931
    • Gajdusek, D.C.1
  • 26
    • 0023566948 scopus 로고
    • Evidence for a secretory form of the cellular prion protein
    • Hay B., Prusiner S.B., and Lingappa V.R. Evidence for a secretory form of the cellular prion protein. Biochemistry. 26 (1987) 8110-8115
    • (1987) Biochemistry. , vol.26 , pp. 8110-8115
    • Hay, B.1    Prusiner, S.B.2    Lingappa, V.R.3
  • 27
    • 0028040838 scopus 로고
    • Prion protein immunocytochemistry: Reliable protocols for investigation of Creutzfeldt-Jakob disease
    • Hayward P.A.R., Bell J.E., and Ironside J.W. Prion protein immunocytochemistry: Reliable protocols for investigation of Creutzfeldt-Jakob disease. Neuropathol. Appl. Neurobiol. 20 (1994) 375-383
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 375-383
    • Hayward, P.A.R.1    Bell, J.E.2    Ironside, J.W.3
  • 28
    • 0027252644 scopus 로고
    • Localization of the mRNA for a chicken prion protein by in situ hybridization
    • Harris D.A., Lele P., and Snider W.D. Localization of the mRNA for a chicken prion protein by in situ hybridization. Proc. Natl. Acad. Sci. USA 90 (1993) 4209-4313
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4209-4313
    • Harris, D.A.1    Lele, P.2    Snider, W.D.3
  • 29
    • 0028263412 scopus 로고
    • Murine scrapie-infected neurons in vivo release excess prion protein into the extracellular space
    • Jeffrey M., Goodsir C.M., Bruce M.E., Mc Bride P.A., Fowler N., and Scott J.R. Murine scrapie-infected neurons in vivo release excess prion protein into the extracellular space. Neurosci. Lett. 174 (1994) 39-42
    • (1994) Neurosci. Lett. , vol.174 , pp. 39-42
    • Jeffrey, M.1    Goodsir, C.M.2    Bruce, M.E.3    Mc Bride, P.A.4    Fowler, N.5    Scott, J.R.6
  • 30
    • 0026751775 scopus 로고
    • Abnomal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt-Jakob disease
    • Kitamoto T., Shin R.W., Doh-ura K., Tomokane N., Miyazono M., Muramoto T., and Tateishi J. Abnomal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt-Jakob disease. Am. J. Pathol. 140 (1992) 1285-1294
    • (1992) Am. J. Pathol. , vol.140 , pp. 1285-1294
    • Kitamoto, T.1    Shin, R.W.2    Doh-ura, K.3    Tomokane, N.4    Miyazono, M.5    Muramoto, T.6    Tateishi, J.7
  • 34
    • 0027353373 scopus 로고
    • Prions and molecular chaperones
    • Liautard J.P. Prions and molecular chaperones. Arch. Virol. 7 (1993) 227-243
    • (1993) Arch. Virol. , vol.7 , pp. 227-243
    • Liautard, J.P.1
  • 36
    • 0027511905 scopus 로고
    • The role of synaptic proteins in the pathogenesis of disorders of the central nervous system
    • Masliah E., and Terry R. The role of synaptic proteins in the pathogenesis of disorders of the central nervous system. Brain Pathol. 3 (1993) 77-85
    • (1993) Brain Pathol. , vol.3 , pp. 77-85
    • Masliah, E.1    Terry, R.2
  • 38
    • 0001585073 scopus 로고
    • Nerve growth factor increase mRNA levels for the prion protein and the beta-amyloid protein precursor in developing hamster brain
    • Mobley W.C., Neve R.L., Prusiner S.B., and Mc Kinley M.P. Nerve growth factor increase mRNA levels for the prion protein and the beta-amyloid protein precursor in developing hamster brain. Proc. Natl. Acad. Sci. USA 85 (1988) 9811-9815
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9811-9815
    • Mobley, W.C.1    Neve, R.L.2    Prusiner, S.B.3    Mc Kinley, M.P.4
  • 39
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moser M., Colello R.J., Pott U., and Oesch B. Developmental expression of the prion protein gene in glial cells. Neuron 14 (1995) 509-517
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 42
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 44
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S.B. Molecular biology of prion diseases. Science 252 (1991) 1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 45
    • 0022971602 scopus 로고
    • Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues
    • Robakis N.K., Sawh P.R., Wolfe G.C., Rubenstein R., Carp R.I., and Innis M.A. Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues. Proc. Natl. Acad. Sci. USA 83 (1986) 6377-6381
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6377-6381
    • Robakis, N.K.1    Sawh, P.R.2    Wolfe, G.C.3    Rubenstein, R.4    Carp, R.I.5    Innis, M.A.6
  • 46
    • 0025976060 scopus 로고
    • Differences in the membrane interaction of scrapie amyloid precursor proteins in normal and scrapie-or Creutzfeldt-Jakob disease-infected brains
    • Safar J., Ceroni M., Gajdusek D.C., and Gibbs C.J. Differences in the membrane interaction of scrapie amyloid precursor proteins in normal and scrapie-or Creutzfeldt-Jakob disease-infected brains. J. Infec. Dis. 163 (1991) 488-494
    • (1991) J. Infec. Dis. , vol.163 , pp. 488-494
    • Safar, J.1    Ceroni, M.2    Gajdusek, D.C.3    Gibbs, C.J.4
  • 47
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation and unfolding of scrapie amyloid (prion) protein
    • Safar J., Roller P.P., Gajdusek D.C., and Gibbs Jr. C.J. Conformational transitions, dissociation and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268 (1993) 20276-20284
    • (1993) J. Biol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 48
    • 0028075620 scopus 로고
    • Abnormal accumulation of prion protein mRNA in muscle fibers of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy
    • Sarkozi E., Askanas V., and King Engel W. Abnormal accumulation of prion protein mRNA in muscle fibers of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy. Am. J. Pathol. 145 (1994) 1280-1284
    • (1994) Am. J. Pathol. , vol.145 , pp. 1280-1284
    • Sarkozi, E.1    Askanas, V.2    King Engel, W.3
  • 51
    • 0026683652 scopus 로고
    • A soluble form of prion protein in human cerebrospinal fluid: Implications for prion-related encephalopathies
    • Tagliavini F., Prelli F., Porro M., Salmona M., Bugiani O., and Frangione B. A soluble form of prion protein in human cerebrospinal fluid: Implications for prion-related encephalopathies. Biochem. Biophys. Res. Commun. 184 (1992) 1398-1404
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1398-1404
    • Tagliavini, F.1    Prelli, F.2    Porro, M.3    Salmona, M.4    Bugiani, O.5    Frangione, B.6
  • 53
    • 0021369407 scopus 로고
    • Amyloid plaques in the brain of mice with Creutzfeldt-Jakob disease
    • Tateishi J., Nagara J.H., Hikita K., and Sato Y. Amyloid plaques in the brain of mice with Creutzfeldt-Jakob disease. Ann. Neurol. 15 (1984) 278-280
    • (1984) Ann. Neurol. , vol.15 , pp. 278-280
    • Tateishi, J.1    Nagara, J.H.2    Hikita, K.3    Sato, Y.4
  • 54
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., DeArmond S.J., and Prusiner S.B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83 (1995) 79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 55
    • 0025800143 scopus 로고
    • A unified theory of prion propagation
    • Weissmann C. A unified theory of prion propagation. Nature 352 (1991) 679-683
    • (1991) Nature , vol.352 , pp. 679-683
    • Weissmann, C.1
  • 56
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway D., DeArmond S.J., Cayetano-Canlas J., Groth D., Foster D., Yang S.L., Torchia M., Carlson G.A., and Prusiner S.B. Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76 (1994) 117-129
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1    DeArmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.