Honors & Awards

  • Engineering Coterminal Fellowship, Stanford University School of Engineering (2022-2023)
  • Departmental Honors, Stanford University Department of Biology (2022)
  • Major Grant, Stanford University VPUE (2021)

Education & Certifications

  • B.S. with Honors, Stanford University, Biology (2022)

Service, Volunteer and Community Work

  • Undergraduate Volunteer, Pacific Free Clinic, Cardinal Free Clinics, Stanford University School of Medicine (1/2019 - 1/2022)


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Lab Affiliations

All Publications

  • Drp1/p53 interaction mediates p53 mitochondrial localization and dysfunction in septic cardiomyopathy. Journal of molecular and cellular cardiology Mukherjee, R., Tetri, L. H., Li, S. J., Fajardo, G., Ostberg, N. P., Tsegay, K. B., Gera, K., Cornell, T. T., Bernstein, D., Mochly-Rosen, D., Haileselassie, B. 2023; 177: 28-37


    Previous studies have implicated p53-dependent mitochondrial dysfunction in sepsis induced end organ injury, including sepsis-induced myocardial dysfunction (SIMD). However, the mechanisms behind p53 localization to the mitochondria have not been well established. Dynamin-related protein 1 (Drp1), a mediator of mitochondrial fission, may play a role in p53 mitochondrial localization. Here we examined the role of Drp1/p53 interaction in SIMD using in vitro and murine models of sepsis.H9c2 cardiomyoblasts and BALB/c mice were exposed to lipopolysaccharide (LPS) to model sepsis phenotype. Pharmacologic inhibitors of Drp1 activation (ψDrp1) and of p53 mitochondrial binding (pifithrin μ, PFTμ) were utilized to assess interaction between Drp1 and p53, and the subsequent downstream impact on mitochondrial morphology and function, cardiomyocyte function, and sepsis phenotype.Both in vitro and murine models demonstrated an increase in physical Drp1/p53 interaction following LPS treatment, which was associated with increased p53 mitochondrial localization, and mitochondrial dysfunction. This Drp1/p53 interaction was inhibited by ΨDrp1, suggesting that this interaction is dependent on Drp1 activation. Treatment of H9c2 cells with either ΨDrp1 or PFTμ inhibited the LPS mediated localization of Drp1/p53 to the mitochondria, decreased oxidative stress, improved cellular respiration and ATP production. Similarly, treatment of BALB/c mice with either ΨDrp1 or PFTμ decreased LPS-mediated mitochondrial localization of p53, mitochondrial ROS in cardiac tissue, and subsequently improved cardiomyocyte contractile function and survival.Drp1/p53 interaction and mitochondrial localization is a key prodrome to mitochondrial damage in SIMD and inhibiting this interaction may serve as a therapeutic target.

    View details for DOI 10.1016/j.yjmcc.2023.01.008

    View details for PubMedID 36841153

  • Synaptic protein interaction networks encode experience by assuming stimulus-specific and brain-region-specific states CELL REPORTS Lautz, J. D., Tsegay, K. B., Zhu, Z., Gniffke, E. P., Welsh, J. P., Smith, S. P. 2021; 37 (9): 110076


    A core network of widely expressed proteins within the glutamatergic post-synapse mediates activity-dependent synaptic plasticity throughout the brain, but the specific proteomic composition of synapses differs between brain regions. Here, we address the question, how does proteomic composition affect activity-dependent protein-protein interaction networks (PINs) downstream of synaptic activity? Using quantitative multiplex co-immunoprecipitation, we compare the PIN response of in vivo or ex vivo neurons derived from different brain regions to activation by different agonists or different forms of eyeblink conditioning. We report that PINs discriminate between incoming stimuli using differential kinetics of overlapping and non-overlapping PIN parameters. Further, these "molecular logic rules" differ by brain region. We conclude that although the PIN of the glutamatergic post-synapse is expressed widely throughout the brain, its activity-dependent dynamics show remarkable stimulus-specific and brain-region-specific diversity. This diversity may help explain the challenges in developing molecule-specific drug therapies for neurological disorders.

    View details for DOI 10.1016/j.celrep.2021.110076

    View details for Web of Science ID 000725673200001

    View details for PubMedID 34852231

    View details for PubMedCentralID PMC8722361

  • A Repurposed Drug Screen Identifies Compounds That Inhibit the Binding of the COVID-19 Spike Protein to ACE2 FRONTIERS IN PHARMACOLOGY Tsegay, K. B., Adeyemi, C. M., Gniffke, E. P., Sather, D., Walker, J. K., Smith, S. P. 2021; 12: 685308


    Repurposed drugs that block the interaction between the SARS-CoV-2 spike protein and its receptor ACE2 could offer a rapid route to novel COVID-19 treatments or prophylactics. Here, we screened 2,701 compounds from a commercial library of drugs approved by international regulatory agencies for their ability to inhibit the binding of recombinant, trimeric SARS-CoV-2 spike protein to recombinant human ACE2. We identified 56 compounds that inhibited binding in a concentration-dependent manner, measured the IC50 of binding inhibition, and computationally modeled the docking of the best inhibitors to the Spike-ACE2 binding interface. The best candidates were Thiostrepton, Oxytocin, Nilotinib, and Hydroxycamptothecin with IC50's in the 4-9 μM range. These results highlight an effective screening approach to identify compounds capable of disrupting the Spike-ACE2 interaction, as well as identify several potential inhibitors of the Spike-ACE2 interaction.

    View details for DOI 10.3389/fphar.2021.685308

    View details for Web of Science ID 000667197500001

    View details for PubMedID 34194331

    View details for PubMedCentralID PMC8236845