Publications by authors named "Dylan Lasher"

Article Synopsis
  • - Tau is a disordered protein that binds to negatively charged microtubules in neurons, helping to stabilize them, but abnormal interactions are linked to neurodegenerative diseases like Alzheimer's.
  • - Researchers studied how tau interacts with anionic liposomes (mimicking axon membranes) using microscopy, revealing different complex formations at low salt concentrations.
  • - Increasing salt concentrations disintegrated tau self-assemblies while keeping tau-liposome complexes stable, suggesting that tau's charged regions may play a key role in its interaction with neuron membranes.
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Tau, an intrinsically disordered neuronal protein and polyampholyte with an overall positive charge, is a microtubule (MT) associated protein, which binds to anionic domains of MTs and suppresses their dynamic instability. Aberrant tau-MT interactions are implicated in Alzheimer's and other neurodegenerative diseases. Here, we studied the interactions between full length human protein tau and other negatively charged binding substrates, as revealed by differential-interference-contrast (DIC) and fluorescence microscopy.

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