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PubMed: 19517062

Title
D-Ribosylated Tau forms globular aggregates with high cytotoxicity.
Journal
Cellular and molecular life sciences : CMLS
Volume
66
Issue
None
Pages
2559-71
Date
2009-08-01
Authors
Chen L | He R | Wang X | Wei Y

Evidence 281300dd22
JSON

Tau is rapidly glycated in the presence of D-ribose, resulting in oligomerization and polymerization with Glycated derivatives appearing after 24 h. Advanced glycation end-products (AGEs) were formed during initial stages of glycation. Thioflavin T-positive (ThT-positive) aggregations (day 4) indicated the globular-like features. Atomic force microscopy revealed that the surface morphology of ribosylated Tau40 was globular-like.

a(CHEBI:"D-ribose") increases p(HBP:"Tau aggregates") View Subject | View Object

Appears in Networks:

a(CHEBI:"D-ribose") increases p(HGNC:MAPT, pmod(HBP:glycation)) View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:glycation)) increases a(CHEBI:"advanced glycation end-product") View Subject | View Object

Appears in Networks:

Evidence 38bc3f23ce
JSON

D-ribosylated Tau aggregates were highly toxic to SHSY5Y cells and resulted in both apoptosis and necrosis

p(HBP:"Tau aggregates") increases bp(GO:"apoptotic process") View Subject | View Object

Appears in Networks:

p(HBP:"Tau aggregates") increases bp(GO:"necrotic cell death") View Subject | View Object

Appears in Networks:

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