Literature DB >> 1770176

The ultrastructural diversity of scrapie-associated fibrils isolated from experimental scrapie and Creutzfeldt-Jakob disease.

P P Liberski1, P Brown, S Y Xiao, D C Gajdusek.   

Abstract

Several different samples of scrapie-associated fibrils (SAF) were extracted in identical fashion from the brains of golden Syrian hamsters infected with the 263K strain of scrapie agent and NIH Swiss mice infected with the Fujisaki strain of Creutzfeldt-Jakob disease (CJD) agent. Based on a total of over 500 measurements in individual fibrils in different extracts, hamster fibrils were more abundant, thicker and had better defined substructure than mouse fibrils. Hamster protofibrils were usually either twisted helically or in parallel arrays, whereas mouse protofibrils were often twisted, occasionally parallel, or could not be morphologically defined. Thus, SAF preparations from scrapie-affected hamsters can be ultrastructurally distinguished from those of CJD-affected mice, an observation that presumably reflects differences in their respective host-encoded amyloid protein subunits.

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Year:  1991        PMID: 1770176     DOI: 10.1016/s0021-9975(08)80107-7

Source DB:  PubMed          Journal:  J Comp Pathol        ISSN: 0021-9975            Impact factor:   1.311


  8 in total

1.  Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.

Authors:  Victor Shashilov; Ming Xu; Natallia Makarava; Regina Savtchenko; Ilia V Baskakov; Igor K Lednev
Journal:  J Phys Chem B       Date:  2012-06-26       Impact factor: 2.991

2.  Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation.

Authors:  Leonid Breydo; Ying Sun; Natallia Makarava; Cheng-I Lee; Vera Novitskaia; Olga Bocharova; Joseph P Y Kao; Ilia V Baskakov
Journal:  Biochemistry       Date:  2007-01-23       Impact factor: 3.162

3.  Two amyloid States of the prion protein display significantly different folding patterns.

Authors:  Valeriy G Ostapchenko; Michael R Sawaya; Natallia Makarava; Regina Savtchenko; K Peter R Nilsson; David Eisenberg; Ilia V Baskakov
Journal:  J Mol Biol       Date:  2010-05-27       Impact factor: 5.469

4.  The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.

Authors:  Valeriy G Ostapchenko; Natallia Makarava; Regina Savtchenko; Ilia V Baskakov
Journal:  J Mol Biol       Date:  2008-09-04       Impact factor: 5.469

5.  Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.

Authors:  Jason C Sang; Ji-Eun Lee; Alexander J Dear; Suman De; Georg Meisl; Alana M Thackray; Raymond Bujdoso; Tuomas P J Knowles; David Klenerman
Journal:  Chem Sci       Date:  2019-03-25       Impact factor: 9.825

6.  A comparative study of modified confirmatory techniques and additional immuno-based methods for non-conclusive autolytic bovine spongiform encephalopathy cases.

Authors:  Rocío Sarasa; Dietmar Becher; Juan J Badiola; Marta Monzón
Journal:  BMC Vet Res       Date:  2013-10-18       Impact factor: 2.741

7.  N-terminal domain of prion protein directs its oligomeric association.

Authors:  Clare R Trevitt; Laszlo L P Hosszu; Mark Batchelor; Silvia Panico; Cassandra Terry; Andrew J Nicoll; Emmanuel Risse; William A Taylor; Malin K Sandberg; Huda Al-Doujaily; Jacqueline M Linehan; Helen R Saibil; David J Scott; John Collinge; Jonathan P Waltho; Anthony R Clarke
Journal:  J Biol Chem       Date:  2014-07-29       Impact factor: 5.157

8.  Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.

Authors:  Bruno Macedo; Ricardo Sant'Anna; Susanna Navarro; Yraima Cordeiro; Salvador Ventura
Journal:  Microb Cell Fact       Date:  2015-11-04       Impact factor: 5.328

  8 in total

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