Isn't your competent? doctor closely following this research? NO? So your incompetent board of directors isn't setting correct goals for stroke recovery and Alzheimers and Parkinsons prevention?
1. A documented 33% dementia chance post-stroke from an Australian study? May 2012.
2. Then this study came out and seems to have a range from 17-66%. December 2013.`
3. A 20% chance in this research. July 2013.
4. Dementia Risk Doubled in Patients Following Stroke September 2018
Parkinson’s Disease May Have Link to Stroke March 2017
A much better explanation in this post:
Tubulin May Prevent Against Alzheimer’s and Parkinson’s March 2026
The latest here:
One protein may prevent brain process linked to Alzheimer's and Parkinson's
Scientists have identified a protein that may help stop the brain changes linked to Alzheimer’s and Parkinson’s disease.
In a study published in Nature Communications, researchers at Baylor College of Medicine found that tubulin—a protein best known for building the cell’s internal “railway tracks”—can prevent harmful protein clumps from forming in brain cells.
Alzheimer’s disease is closely associated with the buildup of tau protein, while Parkinson’s is linked to alpha-synuclein. In both cases, these proteins can misfold and stick together, forming toxic aggregates that damage neurons and contribute to memory loss, cognitive decline and movement problems.
For years, scientists have focused on stopping or clearing these clumps, but the new research suggests a different approach may be more effective—encouraging the proteins to behave normally rather than blocking them entirely.
Ram Bishnoi, MD, MBA, associate professor of psychiatry and behavioral neurosciences, said the study provides “a concrete, testable mechanism” for how this might work.
“Tubulin, the building block of microtubules, acts as a molecular switch that determines whether tau and α-synuclein [a brain protein] become toxic or stay useful,” Bishnoi told Newsweek.
The team found that tubulin interacts with tau and α-synuclein inside tiny cellular compartments known as condensates—droplets where both healthy and harmful versions of the proteins operate.
“When tubulin is present, it gets pulled into the condensates where tau and α-synuclein accumulates, and it competes for binding sites in a way that keeps both these proteins in functional shapes,” Bishnoi said.
When tubulin is lacking, these structures change in a way that triggers harmful clumping of tau and α‑synuclein.
Bishnoi added that reducing tubulin levels in cell models led to a sharp increase in harmful protein buildup and visible neuron loss, underscoring its protective role.
Rather than eliminating condensates—which also play important roles in healthy cells—the findings suggest the key factor is whether tubulin is present.
“It’s not the condensate itself that’s good or bad, it’s whether tubulin is in the room,” Bishnoi said.
This shift in understanding could reshape how neurodegenerative diseases are treated. Instead of trying to remove harmful protein deposits altogether, scientists may be able to steer them toward beneficial behavior.
The idea that tau and α-synuclein have normal roles in the brain is well established, and concerns about disrupting healthy function by blocking them entirely are not new. But Bishnoi said this study strengthens the case for a more balanced approach.
“Instead of asking how do we dissolve the tau aggregates, it asks how do we keep tubulin levels high enough to win the competition,” he said. Essentially, the question becomes how do we keep tubulin levels high enough to prevent them forming in the first place.
The findings also align with clinical observations that microtubule networks decline early in Alzheimer’s disease, suggesting this could be an upstream target for intervention.
However, the findings are based on laboratory and cell-model experiments and will need to be confirmed in animal models and human studies.
“Microtubule-targeting drugs are also notoriously hard to develop safely since microtubules are essential cellular structures all over the body,” Bishnoi said. “Animal studies are the obvious next step.”
Even so, he said the work provides a clearer direction for future research.
“This is a mechanistic insight that strengthens the case for a ‘redirect rather than demolish’ strategy,” he said, adding that tubulin should be seen as a potential lever—not a proven treatment.
Reference
Lucas, L., Tsoi, P.S., Quan, M.D., Choi, K.-J., Ferreon, J.C. and Ferreon, A.C.M. (2026). Tubulin transforms Tau and α-synuclein condensates from pathological to physiological. Nature Communications. [online] doi:https://doi.org/10.1038/s41467-026-69618-3.
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Scientists have identified a protein that may help stop the brain changes linked to Alzheimer’s and Parkinson’s disease.
In a study published in Nature Communications, researchers at Baylor College of Medicine found that tubulin—a protein best known for building the cell’s internal “railway tracks”—can prevent harmful protein clumps from forming in brain cells.
Alzheimer’s disease is closely associated with the buildup of tau protein, while Parkinson’s is linked to alpha-synuclein. In both cases, these proteins can misfold and stick together, forming toxic aggregates that damage neurons and contribute to memory loss, cognitive decline and movement problems.
For years, scientists have focused on stopping or clearing these clumps, but the new research suggests a different approach may be more effective—encouraging the proteins to behave normally rather than blocking them entirely.
Ram Bishnoi, MD, MBA, associate professor of psychiatry and behavioral neurosciences, said the study provides “a concrete, testable mechanism” for how this might work.
“Tubulin, the building block of microtubules, acts as a molecular switch that determines whether tau and α-synuclein [a brain protein] become toxic or stay useful,” Bishnoi told Newsweek.
The team found that tubulin interacts with tau and α-synuclein inside tiny cellular compartments known as condensates—droplets where both healthy and harmful versions of the proteins operate.
“When tubulin is present, it gets pulled into the condensates where tau and α-synuclein accumulates, and it competes for binding sites in a way that keeps both these proteins in functional shapes,” Bishnoi said.
When tubulin is lacking, these structures change in a way that triggers harmful clumping of tau and α‑synuclein.
Bishnoi added that reducing tubulin levels in cell models led to a sharp increase in harmful protein buildup and visible neuron loss, underscoring its protective role.
Rather than eliminating condensates—which also play important roles in healthy cells—the findings suggest the key factor is whether tubulin is present.
“It’s not the condensate itself that’s good or bad, it’s whether tubulin is in the room,” Bishnoi said.
This shift in understanding could reshape how neurodegenerative diseases are treated. Instead of trying to remove harmful protein deposits altogether, scientists may be able to steer them toward beneficial behavior.
The idea that tau and α-synuclein have normal roles in the brain is well established, and concerns about disrupting healthy function by blocking them entirely are not new. But Bishnoi said this study strengthens the case for a more balanced approach.
“Instead of asking how do we dissolve the tau aggregates, it asks how do we keep tubulin levels high enough to win the competition,” he said. Essentially, the question becomes how do we keep tubulin levels high enough to prevent them forming in the first place.
The findings also align with clinical observations that microtubule networks decline early in Alzheimer’s disease, suggesting this could be an upstream target for intervention.
However, the findings are based on laboratory and cell-model experiments and will need to be confirmed in animal models and human studies.
“Microtubule-targeting drugs are also notoriously hard to develop safely since microtubules are essential cellular structures all over the body,” Bishnoi said. “Animal studies are the obvious next step.”
Even so, he said the work provides a clearer direction for future research.
“This is a mechanistic insight that strengthens the case for a ‘redirect rather than demolish’ strategy,” he said, adding that tubulin should be seen as a potential lever—not a proven treatment.
Reference
Lucas, L., Tsoi, P.S., Quan, M.D., Choi, K.-J., Ferreon, J.C. and Ferreon, A.C.M. (2026). Tubulin transforms Tau and α-synuclein condensates from pathological to physiological. Nature Communications. [online] doi:https://doi.org/10.1038/s41467-026-69618-3.
Related Articles
- Families Who Live the Longest Share Something in Common
- Forever Chemicals Linked to MS in Women, Study Suggests
- Doctors Told Me I Had Cancer in My Jaw at 22—But Worse Was Still to Come
Start your unlimited Newsweek trial
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