메뉴 건너뛰기




Volumn 36, Issue 6, 1998, Pages 1750-1755

Monoclonal antibody F89/160.1.5 Defines a conserved epitope on the ruminant prion protein

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 0031958479     PISSN: 00951137     EISSN: None     Source Type: Journal    
DOI: 10.1128/jcm.36.6.1750-1755.1998     Document Type: Article
Times cited : (147)

References (41)
  • 1
    • 0030918935 scopus 로고    scopus 로고
    • In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices
    • Bessen, R. A., G. J. Raymond, and B. Caughey. 1997. In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices. J. Biol. Chem. 272:15227-15231.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15227-15231
    • Bessen, R.A.1    Raymond, G.J.2    Caughey, B.3
  • 3
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie protein
    • Bolton, D. C., M. P. McKinley, and S. B. Prusiner. 1982. Identification of a protein that purifies with the scrapie protein. Science 218:1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 6
    • 0030250917 scopus 로고    scopus 로고
    • A neurotoxic prion protein fragment enhances proliferation of microglia but not astrocytes in culture
    • Brown, D. R., B. Schmidt, and H. A. Kretzschmar. 1996. A neurotoxic prion protein fragment enhances proliferation of microglia but not astrocytes in culture. Glia 18:59-67.
    • (1996) Glia , vol.18 , pp. 59-67
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 8
    • 0029999065 scopus 로고    scopus 로고
    • A new variant of prion disease
    • Collinge, J., and M. Rossor. 1996. A new variant of prion disease. Lancet 347:916-917.
    • (1996) Lancet , vol.347 , pp. 916-917
    • Collinge, J.1    Rossor, M.2
  • 9
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come, J. H., P. E. Fraser, and P. T. Lansbury. 1993. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl. Acad. Sci. USA 90:5959-5963.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 10
    • 0024307533 scopus 로고
    • Post-mortem immunodiagnosis of scrapie and bovine spongiform encephalopathy
    • Farquhar, C. F., R. A. Somerville, and L. A. Ritchie. 1989. Post-mortem immunodiagnosis of scrapie and bovine spongiform encephalopathy. J. Virol. Methods 24:215-222.
    • (1989) J. Virol. Methods , vol.24 , pp. 215-222
    • Farquhar, C.F.1    Somerville, R.A.2    Ritchie, L.A.3
  • 12
    • 0030599505 scopus 로고    scopus 로고
    • Immunolocalisation of the prion protein (PrP) in the brains of sheep with scrapie
    • Foster, J. D., M. Wilson, and N. Hunter. 1996. Immunolocalisation of the prion protein (PrP) in the brains of sheep with scrapie. Vet. Rec. 139:512-515.
    • (1996) Vet. Rec. , vol.139 , pp. 512-515
    • Foster, J.D.1    Wilson, M.2    Hunter, N.3
  • 13
    • 0027741445 scopus 로고
    • Diversity in the neuropathology of scrapie-like diseases in animals
    • Fraser, H. 1993. Diversity in the neuropathology of scrapie-like diseases in animals. Br. Med. Bull. 49:792-809.
    • (1993) Br. Med. Bull. , vol.49 , pp. 792-809
    • Fraser, H.1
  • 14
    • 0027731068 scopus 로고
    • Genetic control of nucleation and polymerization of host precursors to infectious amyloids in the transmissible amyloidoses of brain
    • Gajdusek, D. C. 1993. Genetic control of nucleation and polymerization of host precursors to infectious amyloids in the transmissible amyloidoses of brain. Br. Med. Bull. 49:913-931.
    • (1993) Br. Med. Bull. , vol.49 , pp. 913-931
    • Gajdusek, D.C.1
  • 15
    • 0003054593 scopus 로고    scopus 로고
    • Differing neurohistologic images of scrapie, transmissible mink encephalopathy, and chronic wasting disease of mule deer and elk
    • C. J. Gibbs, Jr. (ed.), Springer, New York, N.Y.
    • Hadlow, W. J. 1996. Differing neurohistologic images of scrapie, transmissible mink encephalopathy, and chronic wasting disease of mule deer and elk, p. 122-137. In C. J. Gibbs, Jr. (ed.), Bovine spongiform encephalopathy. The BSE dilemma. Springer, New York, N.Y.
    • (1996) Bovine Spongiform Encephalopathy. The BSE Dilemma , pp. 122-137
    • Hadlow, W.J.1
  • 16
    • 0028069275 scopus 로고
    • Hydrated autoclave pretreatment enhancement of prion protein immunoreactivity in formalin-fixed bovine spongiform encephalopathy-affected brain
    • Haritani, M., Y. I. Spencer, and G. A. H. Wells. 1992. Hydrated autoclave pretreatment enhancement of prion protein immunoreactivity in formalin-fixed bovine spongiform encephalopathy-affected brain. Acta Neuropathol. 87:86-90.
    • (1992) Acta Neuropathol. , vol.87 , pp. 86-90
    • Haritani, M.1    Spencer, Y.I.2    Wells, G.A.H.3
  • 18
    • 0023390305 scopus 로고
    • Formic acid pretreatment enhances immunostaining of cerebral and systemic amyloids
    • Kitamoto, T., K. Ogomori, J. Tateishi, and S. B. Prusiner. 1987. Formic acid pretreatment enhances immunostaining of cerebral and systemic amyloids. Lab. Invest. 57:230-236.
    • (1987) Lab. Invest. , vol.57 , pp. 230-236
    • Kitamoto, T.1    Ogomori, K.2    Tateishi, J.3    Prusiner, S.B.4
  • 21
    • 0027074778 scopus 로고
    • PrP protein is associated with follicular dendritic cells of spleens and lymph nodes in uninfected and scrapie-infected mice
    • McBride, P. A., P. Eickelenboom, G. Kraal, H. Fraser, and M. E. Bruce. 1992. PrP protein is associated with follicular dendritic cells of spleens and lymph nodes in uninfected and scrapie-infected mice. J. Pathol. 168:413-418.
    • (1992) J. Pathol. , vol.168 , pp. 413-418
    • McBride, P.A.1    Eickelenboom, P.2    Kraal, G.3    Fraser, H.4    Bruce, M.E.5
  • 22
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley, M. P., D. C. Bolton, and S. B. Prusiner. 1983. A protease-resistant protein is a structural component of the scrapie prion. Cell 35:57-62.
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 24
    • 0028472795 scopus 로고
    • Detection of prion protein in formalin-fixed brain by hydrated autoclaving immunohistochemistry for the diagnosis of scrapie in sheep
    • Miller, J. M., A. L. Jenny, W. D. Taylor, R. E. Race, D. R. Ernst, J. B. Katz, and R. Rubenstein. 1994. Detection of prion protein in formalin-fixed brain by hydrated autoclaving immunohistochemistry for the diagnosis of scrapie in sheep. J. Vet. Diagn. Invest. 6:366-368.
    • (1994) J. Vet. Diagn. Invest. , vol.6 , pp. 366-368
    • Miller, J.M.1    Jenny, A.L.2    Taylor, W.D.3    Race, R.E.4    Ernst, D.R.5    Katz, J.B.6    Rubenstein, R.7
  • 27
    • 0002154049 scopus 로고    scopus 로고
    • Allelic frequencies of an ovine scrapie susceptibility gene
    • O'Rourke, K. I., R. P. Melco, and J. R. Mickelson. 1996. Allelic frequencies of an ovine scrapie susceptibility gene. Anim. Biotechnol. 7:155-162.
    • (1996) Anim. Biotechnol. , vol.7 , pp. 155-162
    • O'Rourke, K.I.1    Melco, R.P.2    Mickelson, J.R.3
  • 28
    • 0029655389 scopus 로고    scopus 로고
    • Human prion diseases and neurodegeneration
    • Prusiner, S. B. 1996. Human prion diseases and neurodegeneration. Curr. Top. Microbiol. Immunol. 207:1-17.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.207 , pp. 1-17
    • Prusiner, S.B.1
  • 31
    • 0001958074 scopus 로고    scopus 로고
    • The diagnosis of bovine spongiform encephalopathy and scrapie by the detection of fibrils and the abnormal protein isoform
    • H. F. Baker and R. M. Ridley (ed.), Humana Press, Totowa, N.J.
    • Stack, M. J., P. Keyes, and A. C. Scott. 1996. The diagnosis of bovine spongiform encephalopathy and scrapie by the detection of fibrils and the abnormal protein isoform, p. 85-103. In H. F. Baker and R. M. Ridley (ed.), Prion diseases. Humana Press, Totowa, N.J.
    • (1996) Prion Diseases , pp. 85-103
    • Stack, M.J.1    Keyes, P.2    Scott, A.C.3
  • 32
    • 0000541257 scopus 로고
    • Principles of neuropatholology
    • B. A. Summers, J. F. Cummings, and A. de Lahunta (ed.), Mosby-Year Book Inc., St. Louis, Mo
    • Summers, B. A., J. F. Cummings, and A. de Lahunta. 1995. Principles of neuropatholology. In B. A. Summers, J. F. Cummings, and A. de Lahunta (ed.), In Veterinary neuropathology. Mosby-Year Book Inc., St. Louis, Mo.
    • (1995) Veterinary Neuropathology
    • Summers, B.A.1    Cummings, J.F.2    De Lahunta, A.3
  • 35
    • 0026897686 scopus 로고
    • Recently described scrapie-like encephalopathies of animals: Case definitions
    • Wells, G. A. H., and I. S. McGill. 1992. Recently described scrapie-like encephalopathies of animals: case definitions. Res. Vet. Sci. 53:1-10.
    • (1992) Res. Vet. Sci. , vol.53 , pp. 1-10
    • Wells, G.A.H.1    McGill, I.S.2
  • 36
    • 0028241751 scopus 로고
    • Configurations and topographic distribution of PrP in the central nervous system in bovine spongiform encephalopathy: An immunohistochemical study
    • Wells, G. A. H., Y. I. Spencer, and M. Haritani. 1994. Configurations and topographic distribution of PrP in the central nervous system in bovine spongiform encephalopathy: an immunohistochemical study Ann. N. Y. Acad. Sci. 724:350-352.
    • (1994) Ann. N. Y. Acad. Sci. , vol.724 , pp. 350-352
    • Wells, G.A.H.1    Spencer, Y.I.2    Haritani, M.3
  • 37
    • 1642304262 scopus 로고    scopus 로고
    • The essential lesion profile of bovine spongiform encephalopathy (BSE) in cattle is unaffected by breed or route of infection
    • Wells, G. A. H., and M. M. Simmons. 1996. The essential lesion profile of bovine spongiform encephalopathy (BSE) in cattle is unaffected by breed or route of infection. Neuropathol. Appl. Neurobiol. 22:453.
    • (1996) Neuropathol. Appl. Neurobiol. , vol.22 , pp. 453
    • Wells, G.A.H.1    Simmons, M.M.2
  • 39
    • 0018871326 scopus 로고
    • Chronic wasting disease of captive mule deer: A spongiform encephalopathy
    • Williams, E. S., and S. Young. 1980. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis. 16:89-98.
    • (1980) J. Wildl. Dis. , vol.16 , pp. 89-98
    • Williams, E.S.1    Young, S.2
  • 40
    • 0031568454 scopus 로고    scopus 로고
    • Neuropathology of scrapie: A study of the distribution patterns of brain lesions in 222 cases of natural scrapie in sheep, 1982-1991
    • Wood, J. L. N., I. S. McGill, S. H. Done, and R. Bradley. 1997. Neuropathology of scrapie: a study of the distribution patterns of brain lesions in 222 cases of natural scrapie in sheep, 1982-1991. Vet. Rec. 140:167-174.
    • (1997) Vet. Rec. , vol.140 , pp. 167-174
    • Wood, J.L.N.1    McGill, I.S.2    Done, S.H.3    Bradley, R.4
  • 41
    • 0000080286 scopus 로고
    • Production of monoclonal antibodies
    • J. E. Coligan (ed.), Wiley Intersciences, New York, N.Y.
    • Yokoyama, W. M. 1994. Production of monoclonal antibodies, p. 2.2.1-2.5.17. In J. E. Coligan (ed.), Current protocols in immunology. Wiley Intersciences, New York, N.Y.
    • (1994) Current Protocols in Immunology , pp. 221-2517
    • Yokoyama, W.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.