K. M. Ori-McKenney

The paper investigates how changes in macromolecular crowding affect microtubule modifications and associated proteins, revealing mechanisms for cellular adaptation to osmotic stress.

This study shows that tau family proteins form cohesive envelopes around microtubules, regulated by lattice spacing, which differentially affects motor protein movement and microtubule function.

This study reconstitutes kinesin-1 activation in vitro, revealing that KLC-based inhibition and cargo-adaptor binding regulate motor activity, with a third non-motor MAP required for robust motility.

This study shows that SARS-CoV-2 structural stability decreases with temperature, supporting the seasonal pattern of viral infectivity.

This study identifies autophosphorylation as a mechanism regulating DCLK1 kinase activity and microtubule binding affinity, offering insights into its role in cancer.

This study shows that combinations of microtubule-associated proteins (MAPs) influence motor-cargo transport directionality, suggesting a combinatorial MAP code that biases microtubule movement.

The paper shows microtubules regulate tau condensation, which spatially controls microtubule severing enzymes and motor movement.

The paper investigates how MAP7 and tau compete for microtubule binding and how this competition affects motor transport, revealing that MAP7 enhances kinesin-1 motility while inhibiting kinesin-3.