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Keyword
- efficiency of energy transfer1
- ETeff1
- FCS1
- fluorescence correlation spectroscopy1
- FRET1
- GMPCPP1
- guanosine-5'-[(α,β)-methyleno]triphosphate1
- MAP1
- microtubule dynamics1
- microtubule-associated protein1
- progressive supranuclear palsy1
- PSP1
- single-molecule FRET1
- smFRET1
- TAB1
- Tau protein1
- tauopathy1
- TIRF1
- TIRF assay buffer1
- TIRF microscopy1
- total internal reflection fluorescence1
Molecular Biophysics
1 Results
- Research ArticleOpen Access
The N-terminal disease–associated R5L Tau mutation increases microtubule shrinkage rate due to disruption of microtubule-bound Tau patches
Journal of Biological ChemistryVol. 298Issue 11102526Published online: September 23, 2022- Alisa Cario
- Sanjula P. Wickramasinghe
- Elizabeth Rhoades
- Christopher L. Berger
Cited in Scopus: 0Regulation of the neuronal microtubule cytoskeleton is achieved through the coordination of microtubule-associated proteins (MAPs). MAP-Tau, the most abundant MAP in the axon, functions to modulate motor motility, participate in signaling cascades, as well as directly mediate microtubule dynamics. Tau misregulation is associated with a class of neurodegenerative diseases, known as tauopathies, including progressive supranuclear palsy, Pick's disease, and Alzheimer's disease. Many disease-associated mutations in Tau are found in the C-terminal microtubule-binding domain.