Articles tagged with Microtubules
Researchers used a two-dimensional optical force clamp to control and observe individual kinesin molecules, revealing that applying forces from the rear has no effect on its speed. This surprising finding challenges the existing hand-over-hand model of kinesin's movement.
Researchers found that tau protein is necessary for beta-amyloid to cause brain cell degeneration in Alzheimer's disease. Tau-depleted neurons showed rapid microtubule turnover, suggesting potential resistance to neurodegeneration.
Researchers at Howard Hughes Medical Institute developed a new parallel focusing method to solve the Poisson-Boltzmann equation, enabling efficient simulation of complex biomolecules. This approach allows for high-resolution modeling of molecules like microtubules and ribosomes, providing insights into their collective properties and p...
Researchers created atomic-resolution maps of microtubules and ribosomes to understand their functions in transporting drugs like taxol. The maps revealed areas that play a key role in intracellular transport, with potential binding sites for such drugs.
Kinesin proteins use a unique 'head-over-head' mechanism to propel themselves forward, allowing them to transport vital cargo through the cell. Researchers have discovered that this process is controlled by the breakdown of ATP and involves a rocking motion that allows kinesin to complete long-distance walks in a few seconds.
Researchers at Harvard Medical School have identified a new class of mitosis inhibitors, including the molecule monastrol, which disrupts the mitotic spindle apparatus and arrests cell division. This discovery offers a promising lead for developing more specific and effective chemotherapies.
Researchers have discovered that plakin proteins bind to all three components of the cytoskeleton, providing an integrated bracing system that gives cells their strength and flexibility. This finding sheds new light on how nerve axons maintain their rigidity and allow for the transport of neurotransmitter-filled vesicles.
A study reveals that mutant tau proteins disrupt microtubule assembly, leading to neuronal death in frontotemporal dementia and parkinsonism (FTDP-17). This discovery suggests a primary role for tau tangles in disease progression, pointing to potential therapeutic strategies involving tau-stabilizing drugs.