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Data · dataset · 2015

When amyloids become prions

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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).

Description

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.

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Health sciences
Inferred from text
Disease 75%

Related

Provenance · 1 source records, 12 field assertions
SourceKeyLast seenRaw
DataCite10.6084/m9.figshare.1263973.v214 d agoJSON v1
FieldAssertionExtractorEvidence
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concepts[disease].local:disease:cancermapping · DataCitevocabulary-mapper@1.0.0keywords['Cancer']
concepts[disease].local:disease:diseaseenrichment · DataCitekeyword-concept-rules@1.0.0title+description (75%)
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concepts[field].local:field:chemistrymapping · DataCitevocabulary-mapper@1.0.0keywords['Chemistry']
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