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The products include kinases, phosphatases, phosphodiesterases, histone deacetylases, sirtuins, and other cellular proteins involved in signal transduction.
Neurofibrillary tangles made tau infamous.
Yet it’s the invisible oligomers that do the most harm.
Neurofibrillary tangles are one of the most recognizable hallmarks of Alzheimer’s disease. They’re large, visible under a microscope, and easy to stain, which made them the natural suspects for decades. If you could clear the tangles, the thinking went, you could halt the disease.
But visibility doesn’t equal toxicity. The real culprits emerge earlier.
Research now shows that small soluble tau oligomers appear long before tangles ever form. These oligomers are mobile, slipping between neurons and disrupting synapses. Even more concerning, they spread in a prion-like fashion, templating normal tau into misfolded states and propagating pathology across brain circuits.
By the time tangles accumulate, much of the neuronal damage is already done. The tangles may be less the cause and more the grave markers of a process that began years earlier.
So, what does this mean for therapy?
This shift has major implications for drug development. If we continue to chase tangles, we may always be arriving too late. The real therapeutic window lies in stopping tau oligomers and seeds before they wreak havoc.
Antibodies, small molecules, and other strategies need to be designed with this in mind: targeting the toxic species of tau, not just the visible ones.
Takeaway: Clearing tangles ≠ halting disease. To truly alter the course of Alzheimer’s, therapies must confront pathological tau, the early stage drivers of pathology hiding long before tangles appear.
What do you think: are tangles the main target, or do they still have a role in therapy?
Read more in the article in the comments
08/15/2025
Ever wondered what it’s like to work at the frontline of kinase research? Here’s a peek into a day in the life of Ivan, a UBC co-op student at SCB.
Q: Why did you choose this co-op?
SCB is the top manufacturer of kinases. It’s the perfect place to experience peak kinase research.
But the secret, more personal answer? I wanted to try industry work. I’m returning to UBC to do my honours anyways, so I want to use co-op to get industry experience.
Q: What do you do at SCB?
I run kinase assays – from plating/welling to assaying activity.
One of my key projects is determining the Km value for human kinases (Michaelis constant). I focus on helping to build a comprehensive database for customers for 300 of these commonly used human kinases.
I also:
- Optimize conditions (e.g., SB10 where signal/background ratio = 10)
- Perform IC50 screenings against inhibitors
- Troubleshoot assays (sometimes it’s just kinase-dependent)
Q: What’s a typical day like?
Half the day is spent preparing assays, the other half running them (3–4 hours), plus time reading papers and learning more about kinase science.
Q: What’s been your peak experience so far?
The discussions. Talking through experiments and ideas has been the most fun and rewarding part. The researchers & advisors here are pretty chill. (That, or they don’t know how to say no when I walk up to bother them)
Q: Things you’ve learned?
- Electronic pipettes aren’t always your friend. I wasted a whole 96 well plate because of them
- How kinase activity is actually measured. The people here actually know their stuff.
-How to prioritize reagent use when supplies are limited. Some stuff, like buffers, you can actually dilute as long as you can put it in there
Q: Things that I could improve?
- Better experiment documentation
- More efficient cleanups
- Improved box organization and labeling (30 minutes to find a specific enzyme makes me wish I shouldn’t have even started the assay)
Passionate about science and looking to make an impact? Join us at SCB and help push the boundaries of kinase research.
Click here to claim your Sponsored Listing.
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