Amyloid: The Journal of Protein Folding Disorders is a respected, peer-reviewed scientific publication. It serves as a dedicated platform for the dissemination of research findings related to amyloid and associated diseases. Its primary focus is to advance the understanding of amyloidosis and other conditions linked to protein misfolding.
Understanding Amyloid
Amyloid refers to abnormal protein deposits that can accumulate in various tissues and organs. These deposits are characterized by their misfolded structure, which causes them to aggregate into insoluble fibrils. The accumulation of these amyloid fibrils can disrupt normal organ function and lead to a range of diseases.
Different types of proteins can form amyloid deposits, and the specific protein involved often dictates the associated disease. For example, amyloid-beta protein is linked to Alzheimer’s disease, while alpha-synuclein is associated with Parkinson’s disease. Systemic amyloidosis involves the widespread deposition of amyloid in multiple organs, impacting conditions like AL amyloidosis or ATTR amyloidosis. The formation of these deposits is a complex process involving protein misfolding and aggregation.
Key Research Areas
The Amyloid journal publishes a broad spectrum of research, covering both basic scientific inquiry and clinical applications related to amyloid. A significant area of focus is the molecular structure and formation of amyloid fibrils, investigating how proteins misfold and aggregate into these harmful structures. Researchers also explore the mechanisms by which amyloid deposits cause cellular damage and organ dysfunction.
The journal features studies on diagnostic methods for amyloid diseases, including advanced imaging techniques and biomarker identification to detect amyloid deposits early. Therapeutic strategies are another prominent research area, encompassing drug development aimed at preventing amyloid formation or promoting its clearance, as well as immunotherapies designed to target and remove existing deposits. Clinical studies related to different forms of amyloidosis are regularly published, providing insights into disease progression, patient outcomes, and the effectiveness of various treatments.
Accessing Journal Articles
Readers can access content published in Amyloid: The Journal of Protein Folding Disorders through several avenues. The primary method for many institutions is through an institutional subscription, which provides access to the full range of published articles. Individual researchers can also obtain access through personal subscriptions to the journal.
For those without a subscription, pay-per-article options are typically available. The journal also participates in open-access initiatives, meaning some articles or archives may be freely accessible to the public, often through platforms like PubMed Central. The publisher’s website, Taylor & Francis Online, serves as the central hub for navigating and finding specific issues or articles, offering search functions and organized archives. The journal is a hybrid open-access publication, meaning authors can choose to make their articles freely available, sometimes for an Article Publishing Charge (APC), though agreements with institutions or funders may cover these costs.
The Journal’s Contribution
Amyloid: The Journal of Protein Folding Disorders holds a recognized position within the field of amyloid research. It contributes to advancing scientific understanding by providing a forum for new discoveries regarding amyloid formation, toxicity, and disease mechanisms. The journal fosters collaboration among researchers globally, enabling the sharing of diverse perspectives and methodologies.
The peer-review process implemented by the journal ensures the quality and credibility of the published research. The journal’s international scope means it draws contributions and readership from across the globe, reflecting the worldwide effort to combat amyloid-related diseases. The research published in Amyloid ultimately informs clinical practice, guiding the development of diagnostic tools and therapeutic approaches for patients affected by amyloidosis.