Honors & Awards

  • Regina Casper Stanford Graduate Fellowship, Stanford University (2009-2013)
  • National Research Service Award (NRSA), National Eye Institute, National Institutes of Health (2013-2016)

Education & Certifications

  • Bachelor of Arts, Harvard University, Neurobiology (2009)

Stanford Advisors

Research & Scholarship

Lab Affiliations



All Publications

  • PirB regulates a structural substrate for cortical plasticity PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Djurisic, M., Vidal, G. S., Mann, M., Aharon, A., Kim, T., Santos, A. F., Zuo, Y., Huebener, M., Shatz, C. J. 2013; 110 (51): 20771-20776


    Experience-driven circuit changes underlie learning and memory. Monocular deprivation (MD) engages synaptic mechanisms of ocular dominance (OD) plasticity and generates robust increases in dendritic spine density on L5 pyramidal neurons. Here we show that the paired immunoglobulin-like receptor B (PirB) negatively regulates spine density, as well as the threshold for adult OD plasticity. In PirB(-/-) mice, spine density and stability are significantly greater than WT, associated with higher-frequency miniature synaptic currents, larger long-term potentiation, and deficient long-term depression. Although MD generates the expected increase in spine density in WT, in PirB(-/-) this increase is occluded. In adult PirB(-/-), OD plasticity is larger and more rapid than in WT, consistent with the maintenance of elevated spine density. Thus, PirB normally regulates spine and excitatory synapse density and consequently the threshold for new learning throughout life.

    View details for DOI 10.1073/pnas.1321092110

    View details for Web of Science ID 000328548600089

    View details for PubMedID 24302763

  • Human LilrB2 Is a beta-Amyloid Receptor and Its Murine Homolog PirB Regulates Synaptic Plasticity in an Alzheimer's Model SCIENCE Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., Shatz, C. J. 2013; 341 (6152): 1399-1404


    Soluble β-amyloid (Aβ) oligomers impair synaptic plasticity and cause synaptic loss associated with Alzheimer's disease (AD). We report that murine PirB (paired immunoglobulin-like receptor B) and its human ortholog LilrB2 (leukocyte immunoglobulin-like receptor B2), present in human brain, are receptors for Aβ oligomers, with nanomolar affinity. The first two extracellular immunoglobulin (Ig) domains of PirB and LilrB2 mediate this interaction, leading to enhanced cofilin signaling, also seen in human AD brains. In mice, the deleterious effect of Aβ oligomers on hippocampal long-term potentiation required PirB, and in a transgenic model of AD, PirB not only contributed to memory deficits present in adult mice, but also mediated loss of synaptic plasticity in juvenile visual cortex. These findings imply that LilrB2 contributes to human AD neuropathology and suggest therapeutic uses of blocking LilrB2 function.

    View details for DOI 10.1126/science.1242077

    View details for Web of Science ID 000324597200048

  • NKCC1 cotransporters: keeping an 'ion' them. journal of physiology Vidal Pérez-Treviño, G. S. 2011; 589: 781-782

    View details for DOI 10.1113/jphysiol.2010.203919

    View details for PubMedID 21486847

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