Special Issue "Prions"
A special issue of Pathogens (ISSN 2076-0817).
Deadline for manuscript submissions: closed (30 April 2013).
Interests: prions; prion diseases; neurodegenerative disorders; protein misfolding disorders; protein aggregations; neuroscience; alzheimer’s disease; and glycosylation
Interests: prions; prion diseases
Interests: prion diseases; endogenous retrovirus; oxidative stress; protein citrullination; autophagy and neurodegenerative disorders
Prions are infectious proteinaceous pathogens responsible for a group of fatal transmissible spongiform encephalopathies or prion diseases in animals and humans. An infectious scrapie form of prion protein (termed PrPSc) is the only known component in prions. PrPSc is derived from the cellular PrP (PrPC) through a conformational transition triggered by PrP mutation, exogenous PrPSc infection, or unknown reasons. Animal prion diseases mainly include scrapie, bovine spongiform encephalopathy, and chronic wasting disease, whereas human prion diseases include Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker disease, fatal familial insomnia, kuru, and variably protease-sensitive prionopathy. Unlike other infectious agents such as bacteria, viruses, and fungi, which contain genomes composed of either DNA or RNA, prions may be the only known infectious pathogens that are devoid of nucleic acids. Although prion diseases are rare, it is crucial to keep updated on the development of prions because of the unique properties of prions, no cure for prion diseases yet, and their potential for renewed outbreaks of disease in animals, humans, or both.
Both original research and review articles focusing on molecular mechanisms underlying the prion formation and pathogenesis of prion diseases are welcomed. Especially, we seek manuscripts that report emerging atypical prions and prion diseases as well as innovative strategies and methods for the determination of prions and treatment of prion diseases. Potential topics include, but are not limited to:
- Atypical prions and prion diseases
- Prion-like mechanisms in other diseases
- Co-factors in prion formation
- Diagnostic assays
- Strategies for development of vaccination and treatment
We look forward to your contributions and to a valuable edition that will promote further developments in this exciting field.
Thank you for your collaboration.
Wen-Quan Zou, MD, PhD
Xiao-Ping Dong, MD, PhD
Yong-Sun Kim, MD, PhD
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Pathogens is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1400 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- prion diseases
- prion formation
- bovine spongiform encephalopathy
- chronic wasting disease
- creutzfeldt-Jakob disease
- Gerstmann-Sträussler-Scheinker disease
- variably protease-sensitive prionopathy
- oxidative stress
- insoluble prion protein