When amyloids become prions

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Sabate, Raimon

Description

The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer's disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion), it is necessary to find an underlying cause of the different capacity to infect that each of the proteins prone to form amyloids has. As proposed here, both the intrinsic cytotoxicity and the number of nuclei of aggregation per cell could be key factors in this transmission capacity of each amyloid.

Citations (0)

Mentions (0)

Metrics

Dataset Index

0.3

FAIR Score

85%

Citations

0

Mentions

0

Metrics Over Time

Publication Details

DOI

Publisher

Taylor & Francis

Assigned Domain

Subfield

Molecular Biology

Field

Biochemistry, Genetics and Molecular Biology

Domain

Life Sciences

Confidence Score

100%

Source

Open Alex

Keywords

110309 Infectious DiseasesFOS: Health sciencesCancerChemistryNeuroscienceMolecular BiologyCell BiologyBiochemistry

Normalization Factors

FT

13.46

CTw

1.00

MTw

1.00