Literature DB >> 16691009

Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies.

Suzette A Priola1, Ina Vorberg.   

Abstract

The transmissible spongiform encephalopathies (TSE), or prion diseases, are a group of rare, fatal, and transmissible neurodegenerative diseases of mammals for which there are no known viral or bacterial etiological agents. The bovine form of these diseases, bovine spongiform encephalopathy (BSE), has crossed over into humans to cause variant Creutzfeldt-Jakob disease. As a result, BSE and the TSE diseases are now considered a significant threat to human health. Understanding the basic mechanisms of TSE pathogenesis is essential for the development of effective TSE diagnostic tests and anti-TSE therapeutic regimens. This review provides an overview of the molecular mechanisms that underlie this enigmatic group of diseases.

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Year:  2006        PMID： 16691009     DOI： 10.1385/MB:33:1:71

Source DB:  PubMed          Journal:  Mol Biotechnol        ISSN： 1073-6085            Impact factor:   2.695


  149 in total

Review 1.  Prion protein and species barriers in the transmissible spongiform encephalopathies.

Authors:  S A Priola
Journal:  Biomed Pharmacother       Date:  1999       Impact factor: 6.529

2.  Anchorless prion protein results in infectious amyloid disease without clinical scrapie.

Authors:  Bruce Chesebro; Matthew Trifilo; Richard Race; Kimberly Meade-White; Chao Teng; Rachel LaCasse; Lynne Raymond; Cynthia Favara; Gerald Baron; Suzette Priola; Byron Caughey; Eliezer Masliah; Michael Oldstone
Journal:  Science       Date:  2005-06-03       Impact factor: 47.728

3.  A novel progressive spongiform encephalopathy in cattle.

Authors:  G A Wells; A C Scott; C T Johnson; R F Gunning; R D Hancock; M Jeffrey; M Dawson; R Bradley
Journal:  Vet Rec       Date:  1987-10-31       Impact factor: 2.695

4.  Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease.

Authors:  M S Palmer; A J Dryden; J T Hughes; J Collinge
Journal:  Nature       Date:  1991-07-25       Impact factor: 49.962

5.  Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.

Authors:  M Gasset; M A Baldwin; R J Fletterick; S B Prusiner
Journal:  Proc Natl Acad Sci U S A       Date:  1993-01-01       Impact factor: 11.205

6.  Altered circadian activity rhythms and sleep in mice devoid of prion protein.

Authors:  I Tobler; S E Gaus; T Deboer; P Achermann; M Fischer; T Rülicke; M Moser; B Oesch; P A McBride; J C Manson
Journal:  Nature       Date:  1996-04-18       Impact factor: 49.962

7.  Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.

Authors:  B Caughey; G J Raymond; D A Kocisko; P T Lansbury
Journal:  J Virol       Date:  1997-05       Impact factor: 5.103

8.  Mice devoid of PrP are resistant to scrapie.

Authors:  H Büeler; A Aguzzi; A Sailer; R A Greiner; P Autenried; M Aguet; C Weissmann
Journal:  Cell       Date:  1993-07-02       Impact factor: 41.582

9.  Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins.

Authors:  D A Butler; M R Scott; J M Bockman; D R Borchelt; A Taraboulos; K K Hsiao; D T Kingsbury; S B Prusiner
Journal:  J Virol       Date:  1988-05       Impact factor: 5.103

Review 10.  Epidemiology and control of bovine spongiform encephalopathy (BSE).

Authors:  R Bradley; J W Wilesmith
Journal:  Br Med Bull       Date:  1993-10       Impact factor: 4.291
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  8 in total

1.  Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent.

Authors:  Christopher S Greil; Ina M Vorberg; Anne E Ward; Kimberly D Meade-White; David A Harris; Suzette A Priola
Journal:  Virology       Date:  2008-08-08       Impact factor: 3.616

2.  A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner.

Authors:  Young Pyo Choi; Suzette A Priola
Journal:  J Virol       Date:  2013-08-21       Impact factor: 5.103

3.  The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.

Authors:  Luis Fonseca-Ornelas; Markus Zweckstetter
Journal:  Protein Sci       Date:  2016-06-01       Impact factor: 6.725

Review 4.  The role of genetics in chronic wasting disease of North American cervids.

Authors:  Stacie J Robinson; Michael D Samuel; Katherine I O'Rourke; Chad J Johnson
Journal:  Prion       Date:  2012-04-01       Impact factor: 3.931

Review 5.  Prion protein misfolding and disease.

Authors:  Roger A Moore; Lara M Taubner; Suzette A Priola
Journal:  Curr Opin Struct Biol       Date:  2009-01-20       Impact factor: 6.809

6.  Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro.

Authors:  Leah M Kyle; Theodore R John; Hermann M Schätzl; Randolph V Lewis
Journal:  PLoS One       Date:  2013-06-25       Impact factor: 3.240

7.  Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes.

Authors:  Young Pyo Choi; Mark W Head; James W Ironside; Suzette A Priola
Journal:  Am J Pathol       Date:  2014-09-30       Impact factor: 4.307

8.  Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity.

Authors:  Andrew G Timmes; Roger A Moore; Elizabeth R Fischer; Suzette A Priola
Journal:  PLoS One       Date:  2013-07-30       Impact factor: 3.240
  8 in total

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