Dr. Todd Cohen in a Podcast!
Dr. Todd Cohen was featured in “The News and Notes Podcast” by Jeffrey C. McAndrew, where they discussed new, promising discoveries in ALS and what a typical day is like in the Cohen Lab at UNC Chapel Hill.
Press play to listen in on the conversation!
Or click here for the full podcast webpage
Inspiring Stories in Inclusion Body Myositis (sIBM)
Dr. Todd Cohen and the efforts of the Cohen Lab were mentioned in the Oshkosh Herald! The story below features the efforts of Gary Beyer, a patient with sporadic Inclusion Body Myositis (sIBM), a muscle weakening disease that is similar in molecular origin to Amyotropic Lateral Sclerosis (ALS).
The article also mentions a Podcast Conversation with Dr. Todd Cohen on similar subjects
To read the full story, click the pdf link below!
Click here to download- Oshkosh Newsletter page 3
TDP-43 in Amyotrophic Lateral Sclerosis
TDP-43 mediated neurodegeneration in Amyotrophic Lateral Sclerosis (ALS)
Like tau acetylation and phosphorylation in Alzheimer’s Disease, TDP-43 modifications similarly promote aberrant pathology seen in diseased brain and spinal cord of ALS and FTLD-TDP patients. Understanding such post-translational mechanisms could lead to better therapeutic avenues to pursue for ALS, FTD and other diseases characterized by TDP-43 pathology.
Tau in Alzheimer’s Disease
Tau-mediated neurodegeneration in Alzheimer’s disease
Our Research Mission
Our Research Mission in Todd Cohen’s Lab at UNC Chapel Hill
One-liner: To identify the pathogenic mechanisms underlying neurodegenerative disease.
Although distinct, many of these diseases share common underlying pathogenic mechanisms. We seek to uncover the molecular pathways that promote protein aggregation and the formation of amyloid deposits that cause neurodegeneration and cognitive impairments.
Using a combination of biochemistry, genetics, and cell biology, we have identified several post-translational mechanisms including lysine acetylation, phosphorylation, and cysteine disulfide modifications that critically regulate many disease-associated proteins in the brain including the tau protein in AD and the TDP-43 protein present in ALS and FTLD patients. We have pioneered the concept that lysine acetylation, in particular, is an unanticipated, yet critical modification that promotes the evolution and maturation of pathological aggregates in a spectrum of neurodegenerative diseases.
This raises the intriguing possibility of modification-targeted therapeutics to combat normal ageing mechanisms and a broad range of neurodegenerative diseases. Ultimately, by uncovering the mechanistic details that regulate normal and aberrant protein functions in the diseased brain, can we begin to uncover the molecular platform for future drug-based therapies against these debilitating diseases.
Relevance:
Although clinically and pathologically distinct, the disorders shown below share a common underlying pathogenic mechanism in which normally soluble proteins become abnormally sequestered into protein aggregates that can exert toxic loss and gain of functions in a tissue-specific manner.
Current research projects:
1) Tau-mediated neurodegeneration in Alzheimer’s disease
