a(CHEBI:"D-ribose") increases p(HBP:"Tau aggregates")
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.
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.