Literature DB >> 26322176

Techniques to elucidate the conformation of prions.

Martin L Daus1.   

Abstract

Proteinaceous infectious particles (prions) are unique pathogens as they are devoid of any coding nucleic acid. Whilst it is assumed that prion disease is transmitted by a misfolded isoform of the cellular prion protein, the structural insight of prions is still vague and research for high resolution structural information of prions is still ongoing. In this review, techniques that may contribute to the clarification of the conformation of prions are presented and discussed.

Entities:  

Keywords:  Amyloid; Fourier-transform infrared spectroscopy; Neurodegenerative disease; Prion; Protein structure

Year:  2015        PMID： 26322176      PMCID： PMC4549762          DOI： 10.4331/wjbc.v6.i3.218

Source DB:  PubMed          Journal:  World J Biol Chem        ISSN： 1949-8454


  61 in total

Review 1.  Amide modes and protein conformation.

Authors:  J Bandekar
Journal:  Biochim Biophys Acta       Date:  1992-04-08

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

Review 3.  Elucidating the role of cofactors in mammalian prion propagation.

Authors:  Surachai Supattapone
Journal:  Prion       Date:  2014 Jan-Feb       Impact factor: 3.931

4.  Natural and synthetic prion structure from X-ray fiber diffraction.

Authors:  Holger Wille; Wen Bian; Michele McDonald; Amy Kendall; David W Colby; Lillian Bloch; Julian Ollesch; Alexander L Borovinskiy; Fred E Cohen; Stanley B Prusiner; Gerald Stubbs
Journal:  Proc Natl Acad Sci U S A       Date:  2009-09-28       Impact factor: 11.205

5.  Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain.

Authors:  D A Kocisko; P T Lansbury; B Caughey
Journal:  Biochemistry       Date:  1996-10-15       Impact factor: 3.162

6.  Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes.

Authors:  Gianluigi Zanusso; Alessia Farinazzo; Frances Prelli; Michele Fiorini; Matteo Gelati; Sergio Ferrari; Pier Giorgio Righetti; Nicolò Rizzuto; Blas Frangione; Salvatore Monaco
Journal:  J Biol Chem       Date:  2004-07-09       Impact factor: 5.157

7.  Protein misfolding cyclic amplification of infectious prions.

Authors:  Rodrigo Morales; Claudia Duran-Aniotz; Rodrigo Diaz-Espinoza; Manuel V Camacho; Claudio Soto
Journal:  Nat Protoc       Date:  2012-06-28       Impact factor: 13.491

8.  Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seeds.

Authors:  Martin L Daus; Katja Wagenführ; Achim Thomzig; Susann Boerner; Peter Hermann; Antje Hermelink; Michael Beekes; Peter Lasch
Journal:  J Biol Chem       Date:  2013-10-25       Impact factor: 5.157

9.  Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting disease.

Authors:  Martin L Daus; Johanna Breyer; Katja Wagenfuehr; Wiebke M Wemheuer; Achim Thomzig; Walter J Schulz-Schaeffer; Michael Beekes
Journal:  PLoS One       Date:  2011-04-01       Impact factor: 3.240

10.  Structural organization of mammalian prions as probed by limited proteolysis.

Authors:  Ester Vázquez-Fernández; Jana Alonso; Miguel A Pastrana; Adriana Ramos; Lothar Stitz; Enric Vidal; Irina Dynin; Benjamin Petsch; Christopher J Silva; Jesús R Requena
Journal:  PLoS One       Date:  2012-11-20       Impact factor: 3.240
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  1 in total

Review 1.  Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma.

Authors:  Martin L Daus
Journal:  Biology (Basel)       Date:  2016-01-04
  1 in total

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