Literature DB >> 25444937

Prion and prion-like diseases in animals.

Patricia Aguilar-Calvo1, Consolación García1, Juan Carlos Espinosa1, Olivier Andreoletti2, Juan María Torres3.   

Abstract

Transmissible spongiform encephalopaties (TSEs) are fatal neurodegenerative diseases characterized by the aggregation and accumulation of the misfolded prion protein in the brain. Other proteins such as β-amyloid, tau or Serum Amyloid-A (SAA) seem to share with prions some aspects of their pathogenic mechanism; causing a variety of so called prion-like diseases in humans and/or animals such as Alzheimer's, Parkinson's, Huntington's, Type II diabetes mellitus or amyloidosis. The question remains whether these misfolding proteins have the ability to self-propagate and transmit in a similar manner to prions. In this review, we describe the prion and prion-like diseases affecting animals as well as the recent findings suggesting the prion-like transmissibility of certain non-prion proteins.
Copyright © 2014 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Amyloid; Amyloidosis; Prion; Prion-like transmission; Protein misfolding; Protein self-templating

Mesh:

Substances:

Year:  2014        PMID: 25444937     DOI: 10.1016/j.virusres.2014.11.026

Source DB:  PubMed          Journal:  Virus Res        ISSN: 0168-1702            Impact factor:   3.303


  21 in total

1.  Infectious Prions in the Pregnancy Microenvironment of Chronic Wasting Disease-Infected Reeves' Muntjac Deer.

Authors:  Amy V Nalls; Erin McNulty; Clare E Hoover; Laura A Pulscher; Edward A Hoover; Candace K Mathiason
Journal:  J Virol       Date:  2017-07-12       Impact factor: 5.103

2.  Anti-prion Protein Antibody 6D11 Restores Cellular Proteostasis of Prion Protein Through Disrupting Recycling Propagation of PrPSc and Targeting PrPSc for Lysosomal Degradation.

Authors:  Joanna E Pankiewicz; Sandrine Sanchez; Kent Kirshenbaum; Regina B Kascsak; Richard J Kascsak; Martin J Sadowski
Journal:  Mol Neurobiol       Date:  2018-07-09       Impact factor: 5.590

Review 3.  Dual role of ribosome-associated chaperones in prion formation and propagation.

Authors:  Yury O Chernoff; Denis A Kiktev
Journal:  Curr Genet       Date:  2016-03-11       Impact factor: 3.886

4.  S. pombe placed on the prion map.

Authors:  Jacqueline Hayles
Journal:  Microb Cell       Date:  2017-02-03

5.  The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe.

Authors:  Theodora Sideri; Yoko Yashiroda; David A Ellis; María Rodríguez-López; Minoru Yoshida; Mick F Tuite; Jürg Bähler
Journal:  Microb Cell       Date:  2017-01

6.  Met166 -Glu168 residues in human PrP β2-α2 loop account for evolutionary resistance to prion infection.

Authors:  Juan Carlos Espinosa; Alba Marín-Moreno; Patricia Aguilar-Calvo; Juan María Torres
Journal:  Neuropathol Appl Neurobiol       Date:  2020-12-22       Impact factor: 8.090

Review 7.  Silent Prions and Covert Prion Transmission.

Authors:  Candace K Mathiason
Journal:  PLoS Pathog       Date:  2015-12-10       Impact factor: 6.823

Review 8.  Prions, prion-like prionoids, and neurodegenerative disorders.

Authors:  Ashok Verma
Journal:  Ann Indian Acad Neurol       Date:  2016 Apr-Jun       Impact factor: 1.383

9.  Inactivation of Prions and Amyloid Seeds with Hypochlorous Acid.

Authors:  Andrew G Hughson; Brent Race; Allison Kraus; Laura R Sangaré; Lori Robins; Bradley R Groveman; Eri Saijo; Katie Phillips; Luis Contreras; Virkamal Dhaliwal; Matteo Manca; Gianluigi Zanusso; Daniel Terry; Jeffrey F Williams; Byron Caughey
Journal:  PLoS Pathog       Date:  2016-09-29       Impact factor: 6.823

10.  Canine D163-PrP polymorphic variant does not provide complete protection against prion infection in small ruminant PrP context.

Authors:  Alba Marín-Moreno; Juan Carlos Espinosa; Patricia Aguilar-Calvo; Natalia Fernández-Borges; José Luis Pitarch; Lorenzo González; Juan María Torres
Journal:  Sci Rep       Date:  2021-07-12       Impact factor: 4.379

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.