Literature DB >> 12127750

Cyclic amplification of protein misfolding: application to prion-related disorders and beyond.

Claudio Soto1, Gabriela P Saborio, Laurence Anderes.   

Abstract

Diverse human disorders, including the majority of neurodegenerative diseases, are thought to arise from the misfolding and aggregation of protein. We have recently described a novel technology to amplify cyclically misfolded proteins in vitro. This procedure, named protein misfolding cyclic amplification (PMCA), is conceptually analogous to DNA amplification by PCR and has tremendous implications for research and diagnosis. The PMCA concept has been proved on the amplification of prions implicated in the pathogenesis of transmissible spongiform encephalopathies. In this article we describe the rational behind PMCA and some of the many potential applications of this novel technology.

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Year:  2002        PMID: 12127750     DOI: 10.1016/s0166-2236(02)02195-1

Source DB:  PubMed          Journal:  Trends Neurosci        ISSN: 0166-2236            Impact factor:   13.837


  48 in total

1.  Sonication of proteins causes formation of aggregates that resemble amyloid.

Authors:  Peter B Stathopulos; Guenter A Scholz; Young-Mi Hwang; Jessica A O Rumfeldt; James R Lepock; Elizabeth M Meiering
Journal:  Protein Sci       Date:  2004-09-30       Impact factor: 6.725

Review 2.  De novo mammalian prion synthesis.

Authors:  Federico Benetti; Giuseppe Legname
Journal:  Prion       Date:  2009-10-26       Impact factor: 3.931

3.  Cell-free propagation of prion strains.

Authors:  Joaquín Castilla; Rodrigo Morales; Paula Saá; Marcelo Barria; Pierluigi Gambetti; Claudio Soto
Journal:  EMBO J       Date:  2008-09-18       Impact factor: 11.598

4.  Detection of chronic wasting disease prions in salivary, urinary, and intestinal tissues of deer: potential mechanisms of prion shedding and transmission.

Authors:  Nicholas J Haley; Candace K Mathiason; Scott Carver; Mark Zabel; Glenn C Telling; Edward A Hoover
Journal:  J Virol       Date:  2011-04-27       Impact factor: 5.103

5.  The real-time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases.

Authors:  Matthias Schmitz; Maria Cramm; Franc Llorens; Dominik Müller-Cramm; Steven Collins; Ryuichiro Atarashi; Katsuya Satoh; Christina D Orrù; Bradley R Groveman; Saima Zafar; Walter J Schulz-Schaeffer; Byron Caughey; Inga Zerr
Journal:  Nat Protoc       Date:  2016-10-13       Impact factor: 13.491

6.  In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate.

Authors:  Bonto Faburay; Dongseob Tark; Anumantha G Kanthasamy; Juergen A Richt
Journal:  Prion       Date:  2014       Impact factor: 3.931

7.  Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.

Authors:  Ronald A Shikiya; Thomas E Eckland; Alan J Young; Jason C Bartz
Journal:  Prion       Date:  2014       Impact factor: 3.931

8.  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

9.  Prion protein self-peptides modulate prion interactions and conversion.

Authors:  Alan Rigter; Jan Priem; Drophatie Timmers-Parohi; Jan P M Langeveld; Fred G van Zijderveld; Alex Bossers
Journal:  BMC Biochem       Date:  2009-11-30       Impact factor: 4.059

10.  Detection of sub-clinical CWD infection in conventional test-negative deer long after oral exposure to urine and feces from CWD+ deer.

Authors:  Nicholas J Haley; Candace K Mathiason; Mark D Zabel; Glenn C Telling; Edward A Hoover
Journal:  PLoS One       Date:  2009-11-24       Impact factor: 3.240

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