789 South Limestone Street
(859) 218-3859


Sanders-Brown Center on Aging, University of Kentucky


Maj-Linda Selenica, PhD

Dr. Selenica performed her graduate studies in Sweden where she studied the role of amyloid beta and tau proteins in Alzheimer Disease. Directly after her PHD, she received a postdoctoral fellowship at the laboratory of Drs. Dave Morgan and Marcia Gordon, University of South Florida, where she studied therapeutic approaches in tauopathy utilizing mouse models of AD/FTD.

Dr. Selenica joined College of Pharmacy at University of South Florida (2013) as a founding faculty member and basic scientist. As an independent PI, Dr. Selenica focuses in the pathological mechanisms behind TDP-43 and tauopathy in neurodegenerative disorders. In 2019 Selenica lab relocated to the University of Kentucky, Sanders-Brown Center (SBCoA), where they joined the Alzheimer’s disease Center (UK-ADC) and a collaborative group of neuroscientist and neurologist experts focused on Aging and dementia.

Research Focus

Our Laboratory research is focused on molecular pathways and therapeutic approaches of Alzheimer’s Disease, Frontotemporal Dementia (FTD) and related dementias. We have expanded beyond our knowledge on tauopathy and study the molecular mechanisms involved in TDP-43 proteinopathy in the multi-etiology of AD, LATE and FTD disease spectrum. Our laboratory has developed a comprehensive research program to study the impact of TDP-43 and tau proteins in neuropathology, neuroinflammation, blood brain barrier permeability and cellular stress. Specifically, we study mechanistic pathways (hypusinated Eif5a) and post-translation modifications (acetylation, citrullination) that regulate TDP-43 pathology in cellular and animal models.

Alzheimer Disease (AD)

Aging is the most significant risk factor for the progression of Alzheimer’s disease (AD). However, among the hallmark neuropathological factors, heightened tau phosphorylation levels are key indicators of disease progression and represent promising therapeutic targets for AD.
Our laboratory uses in vivo viral gene delivery approach to examine the impact of tau species on synaptic plasticity, neurodegeneration, and cognitive function in young adult and middle-aged mouse cohorts.

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Limbic-predominant age-related TDP-43 encephalopathy (LATE)

TDP-43 (transactive response DNA binding protein of 43 kDa) proteinopathies have a profound impact in the progresssion of neuropahtological changes of Limbic-predominant age-related TDP-43 encephalopathy (LATE-NC). LATE-NC affects close to 1/3 of advanced age dementia patients and strongly correlates with dementia severity, presenting a serious public health risk.
Our laboratory have discovered that citrulline (citR) induced by peptidyl arginine deiminases (PADs) is a common and irreversible post-translational modification (PTM) of TDP-43 protein. 

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Glial and innate immune activation are hallmarks of AD and TDP-43 proteinopathies although contribution to the etiopathology of the diseases is unclear. Microglia, are found in a highly activated state in the diseased brain as indicated by morphological alterations, proliferation, cell surface receptors, and secretion of cytokines and chemokines. In disease models, microglial activation can precede the emergence of TDP-43, Aβ and tau pathology, suggesting that inflammation is an early event.
Our laboratory investigates the role of inflammation in disease progression in tau and TDP-43 animal models

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Lab Milestones

Total funding to date, CoI + PI

Number of publications

Primary and Corresponding

Our Methodology

The laboratory uttilizes cutting edge technology and novel assays to measure TDP-43 protein aggregation and accumulation


We utilize imaging techniques for immunohistochemical analysis of tissue paired with cellular confocol microscopy 

Animal Models

Our laboratory utilizes transgenic animal models of tauopathy and TDP-43 proteinopathy for basic and therapeutic research

Cellular Mechanisms

We utilize several cellular models to investigate hypusine eIF5A mechanism  and stress granule in proteinopathy 

Interested in joining our team?