Electron microscopy in prion research: Tubulovesicular structures are not composed of prion protein (PrP) but they may be intimately associated with PrP amyloid fibrils

被引：0
|
作者：
Liberski, PP [1 ]
Jeffrey, M [1 ]
Goodsir, C [1 ]
机构：
[1] Med Acad Lodz, Chair Oncol, Labs Tumor Biol, Lab Electron Microscopy & Neuropathol, Lodz, Poland
来源：
PRIONS AND BRAIN DISEASES IN ANIMALS AND HUMANS | 1998年 / 295卷
关键词：
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
引用
收藏
页码：77 / 86
页数：10
相关论文
共 38 条
  • [1] Tubulovesicular structures are intimately associated with amyloid fibrils but are devoid of prion protein (PrP)
    Liberski, PP
    BRAIN PATHOLOGY, 1998, 8 (01) : 225 - 225
  • [2] Immunogold electron microscopy studies of tubulovesicular structures: They are not composed of prion protein (PrP)
    Liberski, PP
    Jeffrey, M
    Goodsir, C
    TRANSMISSIBLE SUBACUTE SPONGIFORM ENCEPHALOPATHIES: PRION DISEASES, 1996, : 137 - 142
  • [3] Tubulovesicular structures are not labeled using antibodies to prion protein (PrP) with the immunogold electron microscopy techniques
    P. P. Liberski
    M. Jeffrey
    C. Goodsir
    Acta Neuropathologica, 1997, 93 : 260 - 264
  • [4] Tubulovesicular structures are not labeled using antibodies to prion protein (PrP) with the immunogold electron microscopy techniques
    Liberski, PP
    Jeffrey, M
    Goodsir, C
    ACTA NEUROPATHOLOGICA, 1997, 93 (03) : 260 - 264
  • [5] The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro
    Ryo P. Honda
    Kazuo Kuwata
    Scientific Reports, 7
  • [6] The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro
    Honda, Ryo P.
    Kuwata, Kazuo
    SCIENTIFIC REPORTS, 2017, 7
  • [7] Structures of amyloid fibrils formed by the prion protein derived peptides PrP(244-249) and PrP(245-250)
    Yau, Jason
    Sharpe, Simon
    JOURNAL OF STRUCTURAL BIOLOGY, 2012, 180 (02) : 290 - 302
  • [8] Prion protein amyloid: Separation of scrapie infectivity from PrP polymers
    Wille, H
    Baldwin, MA
    Cohen, FE
    DeArmond, SJ
    Prusiner, SB
    Masters
    Goldgaber
    Maeda
    NATURE AND ORIGIN OF AMYLOID FIBRILS, 1996, 199 : 181 - 201
  • [9] Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel
    Moore, RC
    Lee, IY
    Silverman, GL
    Harrison, PM
    Strome, R
    Heinrich, C
    Karunaratne, A
    Pasternak, SH
    Chishti, MA
    Liang, Y
    Mastrangelo, P
    Wang, K
    Smit, AFA
    Katamine, S
    Carlson, GA
    Cohen, FE
    Prusiner, SB
    Melton, DW
    Tremblay, P
    Hood, LE
    Westaway, D
    JOURNAL OF MOLECULAR BIOLOGY, 1999, 292 (04) : 797 - 817
  • [10] A special report I. Prion protein (PrP) - amyloid plaques in the transmissible spongiform encephalopathies, or prion diseases revisited
    Liberski, PP
    Bratosiewicz, J
    Walis, A
    Kordek, R
    Jeffrey, M
    Brown, P
    FOLIA NEUROPATHOLOGICA, 2001, 39 (04) : 217 - 235
1234