@article{a879205f47b84c96924501c704fc1110,
title = "Modulating the microtubule-tau interactions in biomotility systems by altering the chemical environment",
abstract = "Obstacles in microtubule mediated neuronal transport can trigger dementia. We use bio-motility assays, that simulate the neuron chemistry in axonopathy, to screen chemicals, that retain the microtubule dynamics in healthy neuronal activity. Tau protein inhibits microtubule activity and leads to oligomerization. Iron(iii) untangles, whereas mono-sodium-glutamate destabilizes the microtubule oligomer.",
author = "S. Bhattacharyya and K. Kim and H. Nakazawa and M. Umetsu and W. Teizer",
note = "Funding Information: We gratefully acknowledge support from the World Premier International Research Center Initiative (WPI), MEXT, Japan. We would like to thank Dr Aurelien Sikora and Prof. Izumi Kumagai's students, especially Mr Aruto Sugiyama, Mr Takuma Sujino and Ms Rui Todokoro for the development of the kinesin plasmid. We also sincerely thank Dr Natsuhiko Yoshinaga for suggesting the method for particle tracking analysis. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2016.",
year = "2016",
month = dec,
doi = "10.1039/c6ib00182c",
language = "English",
volume = "8",
pages = "1296--1300",
journal = "Integrative biology : quantitative biosciences from nano to macro",
issn = "1757-9694",
publisher = "Royal Society of Chemistry",
number = "12",
}