In September 2025, the Kissick Family Foundation, in partnership with the Milken Institute Science Philanthropy Accelerator for Research and Collaboration (SPARC), awarded four two-year grants to basic and early-stage translational research teams through the Kissick Family Foundation Frontotemporal Dementia (FTD) Grant Program. These philanthropic grants provide $2 million in new funding for FTD research, bringing the cumulative total to nearly $6 million to advance scientific understanding of the neurodegenerative disorder.
 

Research Projects Supported by the Kissick Family Foundation FTD Grant Program (2025 Cohort) 

Karen Duff, PhD, UK Dementia Research Institute, University College London, England, UK
Co-Investigator: Ule Jernej, PhD, UK Dementia Research Institute, Kings College London, England, UK
Project: TRIM11 as a Therapeutic Agent for Sporadic FTD

About half of FTD cases are driven by abnormal forms of a protein called tau, which clump together and damage brain cells. The Duff team is testing whether a protein known as TRIM11 can be harnessed to remove these harmful clumps in a safe and controlled way. TRIM11 is already known to help clear abnormal tau, but the team aims to understand exactly how it works and how to regulate its activity. Their approach involves using TRIM11 as part of a potential gene therapy—keeping the protein switched off under normal conditions and activating it only when abnormal tau appears. This could reduce unwanted side effects by targeting treatment precisely where and when it’s needed.

Timothy Miller, MD, PhD, Washington University in St. Louis, MO, USA 
Co-Investigators:
Yuna Ayala, PhD, Saint Louis University School of Medicine, MO, USA
Paul Kotzbauer, MD, PhD, Washington University School of Medicine, MO, USA
Mingzhou Zhou, PhD, Washington University School of Medicine, MO, USA
Project: Developing a Misfolded TDP-43 Molecular Degrader

Abnormal forms of a protein called TDP-43 are a major driver of FTD, forming toxic clumps that damage brain cells. Currently, there is no way to stop or remove these harmful buildups. The Miller team is developing small molecules designed to recognize and eliminate only the abnormal form of TDP-43, while sparing the healthy version of the protein—essential for normal cell function. If successful, this work could lead to one of the first therapies that directly targets a root cause of FTD, paving the way for a new class of precision treatments for neurodegenerative disease.

Mercedes Prudencio, PhD, Mayo Clinic Jacksonville, FL, USA
Co-Investigator: Yongjie Zhang, PhD, Mayo Clinic Jacksonville, FL, USA
Project: The Role of ANXA11 in FTLD-TDP

In approximately half of all FTD cases, abnormal forms of the TDP-43 protein clump together in the brain. Recent studies identified another protein, ANXA11, which often clumps together with TDP-43, potentially worsening disease progression. Prudencio’s research team is investigating how frequently this occurs and what role ANXA11 plays in driving FTD by analyzing more than 300 human brains from individuals with FTD. By uncovering how ANXA11 contributes to toxic protein buildup, this project may reveal a new molecular driver of FTD, which could lead to the development of new strategies for slowing, preventing, or halting disease progression.
 

Wilfried Rossoll, PhD, Mayo Clinic Jacksonville, FL, USA
Project: Uncovering the TDP-43 Aggregate Proteome and Its Role in FTLD Pathogenesis

In a major subtype of FTD, TDP-43 forms protein clumps inside brain cells, disrupting their function. However, these aggregates do not consist of TDP-43 alone—many other proteins are also trapped within them. The Rossoll team is using state-of-the-art proteomics methods—capable of detecting and measuring thousands of proteins at once—to identify which proteins are drawn into these clumps and how they contribute to brain cell damage. By mapping the “protein partners” of TDP-43, this research seeks to uncover hidden drivers of disease and point the way to new treatment strategies that could slow, halt, or even reverse the course of FTD.