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Connor Wander – Pharmacology

June 27, 2017


Connor graduated from Virginia Tech with a B.S. in Biology and Biochemistry in 2014, and joined the lab as a technician for two years.  Now a fifth-year PhD Candidate in the Cohen and Song Labs at UNC Chapel Hill, Connor studies astrocytes and inhibitory networks in Alzheimer’s Disease.  Connor is also interested in the interactions between the environment, genetics, and behavior in mood disorders and neurodegenerative diseases.  He manages the lab website and a science communication website,  Straight from a Scientist (SFS).  Outside of the lab, he enjoys hiking, swimming, graphic design, gaming, Brazilian Jiu Jitsu, paintball and caring for his various reptiles.




Hanna Trzeciakiewicz – Biochemistry and Biophysics

June 27, 2017

Hanna is a fifth year PhD candidate and NSF-GRFP fellow. She received a B.S. in Biochemistry (and minor in Spanish Language) from Oakland University in Michigan, where she was an undergraduate research assistant in Dr. Sanela Martic’s biochemistry laboratory investigating the misfolding and aggregation of the tau protein. After, she joined the Biological and Biomedical Sciences Program, the department of Biochemistry and Biophysics, and the Cohen lab at the University of North Carolina at Chapel Hill. She has been investigating many facets of tau protein biochemistry.

TDP-43 in Amyotrophic Lateral Sclerosis

June 22, 2017

 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

June 22, 2017

Tau-mediated neurodegeneration in Alzheimer’s disease

 Tau acetylation causes increased tau aggregation in vitro and promotes the formation of tau tangles observed in AD brain (Cohen et al., Nat Commun, 2011).

Read More →

Our Research Mission

June 22, 2017

Our Research Mission in Todd Cohen’s Lab at UNC Chapel Hill

One-liner: To identify the pathogenic mechanisms underlying neurodegenerative disease. 

 AD vs control

More specifically: 

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.

We utilize a multidisciplinary approach from the “bottom-up”, starting at the protein level and progressing towards more relevant models to answer fundamental questions about protein function and aggregation in neurodegenerative disease.
Approach summary


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

 Tau acetylation causes increased tau aggregation in vitro and promotes the formation of tau tangles observed in AD brain (Cohen et al., Nat Commun, 2011).

Read More →

Celebrating Publications!

June 9, 2017



The Cohen Lab recently celebrated the submission of two new publications:


A Dual Pathogenic Mechanism Links Tau Acetylation to Sporadic Tauopathy in Scientific Reports

Trzeciakiewicz H, Tseng JH, Wander CM, Madden V, Tripathy A, Yuan CX, Cohen TJ.




Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program in Nature Communications (Come back soon or contact us for a link!)

Ping Wang, Connor Wander, Chao-Xing Yuan, Michael Bereman, and Todd Cohen


With many more to come!

Celebrating publications is a tradition in the scientific community.  In Todd Cohen’s words, “Research isn’t all that gratifying.  You work for years in the lab about something nobody knows about and finally submit a paper… months later it hopefully gets accepted.  You have to take the opportunity to celebrate”. (Or he said something similar).

There are no upcoming events at this time.



Welcome to The Todd Cohen Lab at UNC Chapel Hill Website

June 1, 2016

Welcome to the new website for Todd Cohen’s Lab at UNC Chapel Hill!  We will be incrementally moving our online presence to this web address. You can find our old googlesites website here.

This is the digital home for Todd Cohen’s lab in the Department of Neurology at UNC Chapel Hill, not to be confused with Jessica Cohen’s Lab from Psychology and Neuroscience!


Learn more about the research being done in the Todd Cohen Lab at UNC Chapel Hill here.


This website will provide us with a unique platform for discussion and public interaction.  The forum section of the website is under construction, but check back soon!  Any burning questions for Todd Cohen’s Lab at UNC can be asked here.



Stay tuned for more updates!  Any feedback is appreciated as well!  Leave a comment below and tell us what you think.