Publications by authors named "A Hewetson"
Background: Point-of-care ultrasound (POCUS) education has become an essential component of medical school curricula. Ultrasound represents a highly effective teaching modality to reinforce anatomical knowledge gained during cadaveric dissections. At Texas Tech University Health Sciences Center-School of Medicine (TTUHSC-SOM), POCUS was incorporated into the pre-clerkship curriculum especially during the first year of medical school anatomy course.
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- Research indicates that amyloids have important biological functions, particularly in the mouse epididymis, where specific cystatins form an amyloid matrix.
- The study investigates how these amyloids assemble, focusing on cross-seeding between different cystatin members to enhance amyloid formation.
- Findings reveal that CRES3 can create stable amyloid structures that not only help in forming additional CRES amyloids but also interact with other amyloid precursors like Aβ, suggesting a conserved mechanism for regulating amyloid assembly across different proteins.
Maturation of the functional mouse CRES amyloid from globular form.
Proc Natl Acad Sci U S A
July 2020
Article Synopsis
- The study investigates the assembly of functional amyloids in the epididymal lumen, focusing on a cystatin-rich matrix that aids in sperm maturation and protection.
- Researchers developed a purification protocol for a mouse protein called CRES, using advanced techniques like X-ray crystallography and NMR to observe its transition from a single protein unit to a complex amyloid structure.
- Findings reveal that CRES monomers have a distinct structural fold and can assemble through two mechanisms, providing insights into how functional amyloids form and emphasizing their diverse assembly processes.
Article Synopsis
- An amyloid matrix with family 2 cystatins, notably the reproductive cystatin CRES, is essential for sperm maturation and protection in the mouse epididymal lumen.
- Research focused on purifying CRES to study its aggregation from a single unit to amyloid under conditions mimicking those in the epididymis.
- Unlike most amyloids, CRES forms unique antiparallel β-sheet-rich structures and its early oligomers might play a crucial role in assembling functional amyloids.
Background: We previously demonstrated the normal mouse epididymal lumen contains a non-pathological amyloid matrix that surrounds spermatozoa and plays important roles in sperm maturation and protection.
Objective: The objective herein was to present a review of this work, including studies showing the amyloid structures of four members of the CRES (cystatin-related epididymal spermatogenic) subgroup are integral and essential components of the amyloid matrix.
Methods: We used conformation-dependent reagents that recognize the cross-β-sheet structure characteristic of amyloid, including thioflavin S (ThS), thioflavin T (ThT), anti-amyloid antibodies, and X-ray diffraction, as well as negative-stain transmission electron microscopy (TEM) to visualize amyloid structures in the epididymal lumen.