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)

    Location

    1835 Cunningham Ave, San Jose, CA 95122

Lab Affiliations


All Publications


  • 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

    Abstract

    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

    Abstract

    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