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.
authors: WPI-Advanced Institute for Materials Research (WPI-AIMR), Tohoku University, Sendai, Japan.
authors: S
authors: S
authors: Bhattacharyya
authors: WPI-Advanced Institute for Materials Research (WPI-AIMR), Tohoku University, Sendai, Japan.
authors: K
authors: K
authors: Kim
authors: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan.
authors: H
authors: H
authors: Nakazawa
authors: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan.
authors: M
authors: M
authors: Umetsu
authors: WPI-Advanced Institute for Materials Research (WPI-AIMR), Tohoku University, Sendai, Japan and Department of Physics and Astronomy, Texas A&M University, College Station, TX, USA. teizer@physics.tamu.edu and Materials Science and Engineering, Texas A&M University, College Station, TX, USA.
authors: W
authors: W
authors: Teizer
mesh_terms: D002465:Cell Movement; D016547:Kinesins / Q000737:chemistry*; D008870:Microtubules / Q000737:chemistry*; D020409:Molecular Motor Proteins / Q000737:chemistry*; D009474:Neurons / Q000737:chemistry*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D020409:Molecular Motor Proteins; D016875:tau Proteins; D016547:Kinesins