Carli Opland

November 7, 2025

Carli received her Ph.D. in Neuroscience in 2024 and is continued as a postdoc in the lab through 2025. Before coming to UNC for graduate studies, Carli received a B.S. in Cellular and Molecular Biology at California State University, Northridge. She worked with Dr. Randy Cohen studying the neurodegeneration of Purkinje cells from excitotoxicity by GABA receptor activation in an ataxic rat model. After graduating in May 2015, Carli joined Dr. Daniel Geschwind’s lab at UCLA as a staff research associate where she investigated the effects of overexpression of specific genes known to be involved in neurogenesis such as NGN2, FGFR2, and SOX5 in primary human neural progenitor cells. Now in Todd Cohen’s lab at UNC Chapel Hill, Carli is evaluating the role of a particular post-translational modification, tau cleavage by caspases, and its implications for Alzheimer’s disease. Outside of the lab, Carli enjoys baking, hanging out with her cat, running, eating cheese, and making craft cocktails.

Shannon Rhoads

August 27, 2025

Shannon received her PhD from the Neuroscience Curriculum in 2025. She graduated from the University of Maryland in 2016 with a degree in Microbiology. She worked as a Lab Manager in Dr. Frank Shewmaker’s Lab at Uniformed Services University, where she examined the biophysical characteristics of the Amyotrophic Lateral Sclerosis (ALS)-associated protein FUS in cell culture. She continued her ALS research through a co-mentorship with Sarah Cohen and Todd Cohen, studying the impact of ALS pathology on organelle contacts and dynamics.

Julie Necarsulmer

September 27, 2024

Julie is an MD/PhD student who completed the first two years of the UNC School of Medicine curriculum and then joined the Cohen Lab and the Cell Biology and Physiology Department in 2019. She defended in 2023. Julie graduated from Pomona College in 2015, where she studied neuroelectrophysiology and the molecular mechanisms of memory impairment in Alzheimer’s Disease. After graduating and before moving to North Carolina, Julie spent two years in Baltimore’s Biomedical Research Center working as an IRTA Fellow at the NIH’s National Institute on Drug Abuse. While there, she worked to develop and characterize novel genome engineering tools, such as CRISPR/Cas9 and AAV vector technology, to manipulate the rodent central nervous system with regional and cell-type specificity. She also worked on developing models of Parkinson’s Disease and HIV-associated Neurocognitive disorders. In the Cohen lab, Julie researched the role of aberrant TDP-43 species in proteostasis impairment in ALS, FTLD, and other age-related TDP-43 proteinopathies using in vivo and in vitro approaches based on a novel mouse model of disease. She investigated the interactions of ALS/FTLD-associated mutations in non-TDP-43 genes on TDP-43 aggregation. When not in the lab or clinic, Julie likes to spend her time outside walking, running, hiking, and biking. She is also a big fan of wine and cheese boards, and peanut butter and jelly sandwiches.

Dr. Cohen on Radio in Vivo!

April 15, 2018

Dr. Cohen has been in the news a lot lately!  Here’s him on another radio show, called Radio in Vivo!  A great way to learn about Dr. Cohen’s inspiration and drive to enter Alzheimer’s disease research.  Click the picture or here to check it out.

 

Dr. Todd Cohen in a Podcast!

March 16, 2018

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)

March 16, 2018

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

Hanna Awarded an NSF Fellowship! UNC Biochemistry and Biophysics Spotlight

December 20, 2017
Hanna was one of two Biochemistry and Biophysics students to be awarded the National Science Foundation (NSF) Fellowship!  An excerpt from the full article on the UNC School of Medicine website can be found below:

Two biochemistry and biophysics grad students awarded NSF Fellowships

Congratulations to Candice Crilly and Hanna Trzeciakiewicz for receiving Predoctoral Fellowships from the National Science Foundation!

Two biochemistry and biophysics grad students awarded NSF Fellowships
click to enlarge(left to right) Hanna Trzeciakiewicz and Candice Crilly

The National Science Foundation predoctoral fellowships are designed to help ensure the vitality of the human resource base of science and engineering in the United States and reinforces its diversity.  The program recognizes and supports outstanding graduate students in NSF-supported science, technology, engineering, and mathematics disciplines who are pursuing research-based master’s and doctoral degrees at accredited US institutions.

The Tau Post-Translational Modification Puzzle

November 22, 2017

Can you solve it?

Microtubule associated-protein tau (tau for short) is a microtubule stabilizing protein most commonly found in neurons.  Tau helps regulate transport of other proteins by binding or falling off of microtubules.

Michala Kolarova, Francisco García-Sierra, Ales Bartos, Jan Ricny, and Daniela Ripova, “Structure and Pathology of Tau Protein in Alzheimer Disease,” International Journal of Alzheimer’s Disease, vol. 2012, Article ID 731526, 13 pages, 2012. doi:10.1155/2012/731526

The binding affinity and cellular localization of tau can vary, and is regulated by many post-translational modifications (PTMs), including ubiquitination, SUMOylation, acetylation, and phosphorylation.  These PTMs act like little switches on a microchip, and are attached and removed by enzymes like kinases, phosphatases, acetyltransferases, deacetylases and ubiquitin ligases that are in turn regulated by external stimuli including insulin signaling, glutamate, GABA, and neuropeptide receptors.

Mixing and matching of PTMs dynamically regulates neuronal polarization and dendritic branching.  When it goes awry, the cell makes too much aggregate-prone, hyperphosphorylated species of tau, a common hallmark of Alzheimer’s disease.  Hyperphosphorylated tau clumps with more tau to form tangles, which cause cell death and increase inflammation in the brain.  All the different PTMs and their relative effects on tau make for an incredibly complex profile, which we have taken to calling the “PTM code”.

Crack the Code!

Someone at BioMed took the time to build a huge database of tau PTMs.  Each one is mapped to the amino acid sequence of tau, and has the citation linked.  Check it out to see if you can solve the tau post translational modifcation puzzle, and crack the tau code!