Aberrant protein self-assembly is linked to over 30 human diseases, including neurodegenerative diseases, type-2 diabetes, systemic amyloidosis, and cancer. These proteinopathies are generally associated with the appearance of diverse, non-native assemblies of the disease-related proteins, ranging from dimers to amyloid deposits. In-between these extremes, a variety of structures exist, including soluble oligomers of different sizes and morphologies and insoluble precipitates displaying amorphous or fibrillar structures, including various strains that differ by the conformation and organization of monomers within the oligomer or fibril. In recent years, significant progress has been made in understanding the biophysical and structural properties of these diverse protein assemblies and in identifying the mechanisms by which they cause cytotoxicity. These mechanistic studies ranging from the atomic to the cellular to the organism level have been crucial to the development of novel disease-modifying strategies and molecules specifically abrogating pathological protein self-assembly.
In this Research Topic, we aim to highlight current knowledge on the mechanisms underpinning self-assembly of disease-related proteins and review recent studies on the inhibition of toxic protein aggregation. We encourage the submission of innovative perspectives, reviews and original research articles on this topic that will contribute to stimulate the discussion of novel therapeutic avenues to tackle a significant number of severe human diseases.
Subtopics:
- Mechanistic and structural studies of protein aggregation phenomena
- Cell and animal studies of toxic protein self-assembly
- Recent developments in inhibition of toxic protein self-assembly
This Research Topic will build around the scientific content that will be exchanged during the Strategies and tools for modulating pathologic protein self-assembly in proteinopathies
i3S workshop that will take place in Porto, Portugal, March 21-22, 2019. We welcome submissions from researchers in the field, whether they will be attending the workshop or not.
Aberrant protein self-assembly is linked to over 30 human diseases, including neurodegenerative diseases, type-2 diabetes, systemic amyloidosis, and cancer. These proteinopathies are generally associated with the appearance of diverse, non-native assemblies of the disease-related proteins, ranging from dimers to amyloid deposits. In-between these extremes, a variety of structures exist, including soluble oligomers of different sizes and morphologies and insoluble precipitates displaying amorphous or fibrillar structures, including various strains that differ by the conformation and organization of monomers within the oligomer or fibril. In recent years, significant progress has been made in understanding the biophysical and structural properties of these diverse protein assemblies and in identifying the mechanisms by which they cause cytotoxicity. These mechanistic studies ranging from the atomic to the cellular to the organism level have been crucial to the development of novel disease-modifying strategies and molecules specifically abrogating pathological protein self-assembly.
In this Research Topic, we aim to highlight current knowledge on the mechanisms underpinning self-assembly of disease-related proteins and review recent studies on the inhibition of toxic protein aggregation. We encourage the submission of innovative perspectives, reviews and original research articles on this topic that will contribute to stimulate the discussion of novel therapeutic avenues to tackle a significant number of severe human diseases.
Subtopics:
- Mechanistic and structural studies of protein aggregation phenomena
- Cell and animal studies of toxic protein self-assembly
- Recent developments in inhibition of toxic protein self-assembly
This Research Topic will build around the scientific content that will be exchanged during the Strategies and tools for modulating pathologic protein self-assembly in proteinopathies
i3S workshop that will take place in Porto, Portugal, March 21-22, 2019. We welcome submissions from researchers in the field, whether they will be attending the workshop or not.
