Special Issue "Amyloid Hetero-Aggregation"
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".
Deadline for manuscript submissions: closed (30 June 2021).
Interests: biodiagnostics; amyloid; protein misfolding; neuroinflammation; cellular toxicity; neurodegenerative diseases; blood serum; CSF; bioimaging
Special Issues and Collections in MDPI journals
Special Issue in Diagnostics: Biomarkers in Blood
Special Issue in Diagnostics: Biomarkers in Blood 2016
Interests: amyloid, protein misfolding, protein aggregation, protein-protein interaction, protein−lipid interaction, lipid membranes, vesicles, blood serum and CSF, neurodegenerative diseases
This Special Issue will address the molecular and cellular mechanisms of amyloid hetero-aggregation, deposition, and toxicity of various proteins – human, bacterial, and viral. Studies conducted in vitro, in vivo, and ex vivo materials are welcome. Amyloid formation is a widespread phenomenon due to in the generic property of polypeptide chains that self-assemble into cross-β-sheet superstructures and are manifested in numerous amyloid-related diseases, as well as in functional amyloids. The amyloid cascade lies at the center of amyloid disease pathology, involved in up to 50 human diseases, though it is still debated if this is the cause or a consequence of disease. Amyloid formation in neurodegenerative disease and others is often associated with inflammation as a common denominator of those diseases. For example, inflammation triggers the massive production of proinflammatory S100A9 that spontaneously form amyloids and co-aggregates into hetero-amyloids together with Abeta or alpha-synuclein in Alzheimer’s or Parkinson’s disease, respectively. These events initiate the whole pathological amyloid cascade. Recently, the comorbidity of amyloid diseases was also shown to be linked to the co-aggregation of different amyloidogenic proteins. Since amyloids formed by individual polypeptides are highly polymorphic, their co-aggregates add up to the complexity and heterogeneity of the amyloid mixture. Despite the key clinical importance of amyloid formation, the mechanisms of co-aggregation of different amyloid species remain elusive. There is an unmet need to understand the architecture and mechanisms of self-assembly leading to the formation of hetero-aggregates composed of various amyloid polypeptides. Your research and review articles on this subject are very welcome in this issue.
Dr. Ludmilla A. Morozova-Roche
Dr. Himanshu Chaudhary
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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.
- human proteins
- bacterial amyloids
- viral proteins