Publication Name	World Journal of Biological Chemistry
Manuscript ID	17542
Country	Germany

Received	2015-03-12 09:21
Peer-Review Started	2015-03-16 20:15
To Make the First Decision	2015-04-27 15:31
Return for Revision	2015-04-30 15:27
Revised	2015-05-04 15:17
Second Decision	2015-06-08 11:30
Accepted by Journal Editor-in-Chief	2015-06-08 21:38
Accepted by Executive Editor-in-Chief	2015-06-16 16:53
Articles in Press	2015-06-16 16:53
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript	2015-08-11 17:28
Publish the Manuscript Online	2015-08-26 11:07

ISSN	1949-8454 (online)
Open Access	This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
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Category	Biochemistry & Molecular Biology
Manuscript Type	Minireviews
Article Title	Techniques to elucidate the conformation of prions
Manuscript Source	Invited Manuscript
All Author List	Martin L Daus
Funding Agency and Grant Number	Funding Agency Grant Number Alberta Prion Research Institute, Canada European Metrology Research Programme Researcher Grant: HLT10-BiOrigin (Metrology for the Biomolecular Origin of Disease)
Corresponding Author	Dr. Martin L Daus, ZBS6 - Proteomics and Spectroscopy, Robert Koch-Institute, Seestrasse 10, 13353 Berlin, Germany. dausm@rki.de
Key Words	Prion; Amyloid; Neurodegenerative disease; Protein structure; Fourier-transform infrared spectroscopy
Core Tip	Prions (proteinaceous infectious particles) are misfolded isoforms of cellular proteins that cause neurodegenerative diseases in mammals and humans. Several structural models are available for prions but a 3D-structure does still not exist. More structural information is demanded for the understanding of the conversion process and finally for the design of efficient therapeutic approaches. In this review, techniques that may contribute to the clarification of the conformation of prions are presented.
Publish Date	2015-08-26 11:07
Citation	Daus ML. Techniques to elucidate the conformation of prions. World J Biol Chem 2015; 6(3): 218-222
URL	http://www.wjgnet.com/1949-8454/full/v6/i3/218.htm
DOI	http://dx.doi.org/10.4331/wjbc.v6.i3.218

Full Article (PDF)	WJBC-6-218.pdf
Full Article (Word)	WJBC-6-218.doc
Manuscript File	17542-Review.doc
Answering Reviewers	17542-Answering reviewers.pdf
Audio Core Tip	17542-Audio core tip.MP3
Conflict-of-Interest Disclosure Form	17542-Conflict-of-interest statement.pdf
Copyright License Agreement	17542-Copyright assignment.pdf
Peer-review Report	17542-Peer-review(s).pdf
Journal Editor-in-Chief Review Report	17542-Journal editor-in-chief review report.pdf
Scientific Misconduct Check	17542-Scientific misconduct check.pdf
Scientific Editor Work List	17542-Scientific editor work list.pdf