First In Vivo Look at Amyloidosis Sparked by Dural Grafts
Researchers characterize widespread cerebral amyloid angiopathy and cortical plaques found in three living people who received dural grafts as children.
NEWS
Secreted APP Binds GABA-B Receptors, Blocks Neurotransmitter Release
In presynapses, binding sequesters synaptic vesicles.
Tau, More than Aβ, Affects Sleep Early in Alzheimer’s
During deep sleep, people with AD pathology, particularly tau tangles, have less low-frequency slow-wave brain activity, which is important for memory consolidation.
Do Alzheimer’s Biomarkers Vary by Race?
The largest study so far to compare brain scans and CSF among African-Americans and Caucasians finds differences, but participant numbers remain small.
CryoEM γ-Secretase Structures Nail APP, Notch Binding
First look at substrate interactions reveals similarities but some surprises.
New PET Tracer Selectively Lights Up Activated Microglia in Brain
The ligand binds the microglia-specific CSF1 receptor in animal and postmortem studies; human trials are forthcoming.
Without TREM2, Plaques Grow Fast in Mice, Have Less ApoE
Absent the receptor, microglia ignore Aβ seeds and new plaques, which then absorb little ApoE and stay diffuse.
Autophagy, Inflammation, Degeneration: Parsing an Unholy Trinity
In a fly model of neurodegeneration, CDK5 slams autophagy, which leads to a runaway immune response that shoves aging neurons over the edge.
Virtual Exhibit Hall
Alzforum encourages users to visit the Virtual Exhibit Hall, where companies showcase their newest initiatives, products, and services. We welcome Dash Genomics, Inc. and Abcam, which join our other exhibitors — Biogen, BioLegend, BrainXell, NanoString Technologies, and the Jackson Laboratory.
SPOTLIGHT
Seeing Double: Two γ-secretase Structures Capture APP, Notch Binding
High-resolution cryoEM structures show that APP and Notch bind γ-secretase in broadly similar ways and that both undergo an identical molecular contortion that allows proteolysis. Nonetheless, subtle differences between the substrates may open the door to specific inhibitors of APP processing. The structures also reveal that AD mutations in presenilin and APP cluster at the enzyme-substrate interface, reinforcing the idea that altered APP processing causes AD.
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