image the same structure for multiple days without loss of image quality. As proof-of-principle experiments, we imaged oligomeric and fibrillar structures formed during different stages of amyloid-b aggregation as well as the structural remodeling of amyloid fibrils by the anti-amyloid compound epigallocatechin gallate (EGCG). TAB promises to directly image native amyloid in cells and tissues using standard probes at nanometer resolution and at the same time record amyloid dynamics over time scales of minutes to days.
Previously, we have shown that bulk microtubule (MT) movement correlates with neurite elongation, and blocking either dynein activity or MT assembly inhibits both processes. However, whether the contributions of MT dynamics and dynein activity to neurite elongation are separate or interdependent is unclear. Here, we investigated the underlying mechanism by testing the roles of dynein and MT assembly in neurite elongation of Aplysia and chick neurites using time-lapse imaging, fluorescent speckle microscopy, superresolution imaging and biophysical analysis. Pharmacologically inhibiting either dynein activity or MT assembly reduced neurite elongation rates as well as bulk and individual MT anterograde translocation. Simultaneously suppressing both processes did not have additive effects, suggesting a shared mechanism of action. Single-molecule switching nanoscopy revealed that inhibition of MT assembly decreased the association of dynein with MTs. Finally, inhibiting MT assembly prevented the rise in tension induced by dynein inhibition. Taken together, our results suggest that MT assembly is required for dynein-driven MT translocation and neurite outgrowth.
COVID took over the world starting in 2020. Everyone quickly “knew” about the novel coronavirus, but how much do they actually know about the virus behind COVID-19? This classroom activity gives students real-world practice in evaluating actual genetic sequences from SARS-CoV-2 and working with genome alignments to identify mutations and cluster different emergence patterns. This activity works through alignments, mutations/variants, protein folding, structure and function, and medical/immunology implications of the different variants. There are seven parts to this activity, and each one can be incorporated alone into a lesson or collectively used for a lab, case study, or other supplemental activity to strengthen learning objectives in genetics, biology, immunology, and public health. This learning activity is scalable to different levels and has successfully been incorporated into K–12 education as well as college and graduate education.
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