Dr. Lee was raised in Cupertino, California. Dr. Lee studied genetics and performed research in biochemistry at UC Davis. Dr. Lee spent the next decade training in the east coast, most notably at the University of Pennsylvania. She now returns to the west coast at Stanford in the Division of Comprehensive Otolaryngology.
Dr. Lee's clinical interests includes sinusitis, Eustachian tube dysfunction, head and neck tumors and chronic ear disorders amongst others. Her research focus is in improving and developing education for the next generation of otolaryngologists.

Clinical Focus

  • Otolaryngology
  • Chronic sinusitis
  • Eustachian tube dysfunction
  • Salivary gland tumors
  • Endocrine tumors

Academic Appointments

  • Clinical Assistant Professor, Otolaryngology - Head & Neck Surgery Divisions

Professional Education

  • Medical Education: Albert Einstein College of Medicine (2008) NY
  • Residency: University of Pennsylvania Otolaryngology Residency (2013) PA
  • Internship: University of Pennsylvania Otolaryngology Residency (2009) PA
  • Board Certification: Otolaryngology, American Board of Otolaryngology (2014)

Research & Scholarship

Current Research and Scholarly Interests

Development of treatment outcomes of Eustachian tube balloon dilation


  • Simulation Education, Stanford Hospital and Clinics

    Development of high fidelity complex scenario based simulation to improve patient care


    Palo Alto, CA


All Publications

  • Triglyceride Levels and Fracture Risk in Midlife Women: Study of Women's Health Across the Nation Journal of Clinical Endocrinology and Metabolism Chang, P., Gold, E. B., Cauley, J., Johnson, W. O., Karvonen-Guitierrez, C., Jackson, E., Ruppert, K., Lee, J. S. 2016: 3297–3305


    Unfavorable lipid levels contribute to cardiovascular disease and may also harm bone health.Our objective was to investigate relationships between fasting plasma lipid levels and incident fracture in midlife women undergoing the menopausal transition.This was a 13-year prospective, longitudinal study of multiethnic women in five US communities, with near-annual assessments.At baseline, 2062 premenopausal or early perimenopausal women who had no history of fracture were included.Fasting plasma total cholesterol, triglycerides (TG), low-density lipoprotein cholesterol, and high-density lipoprotein cholesterol at baseline and follow-up visits 1 and 3-7.Incident nontraumatic fractures 1) 2 or more years after baseline, in relation to a single baseline level of lipids; and 2) 2-5 years later, in relation to time-varying lipid levels. Cox proportional hazards modelings estimated hazard ratios and 95% confidence interval (CI).Among the lipids, TG levels changed the most, with median levels increased by 16% during follow-up. An increase of 50 mg/dl in baseline TG level was associated with a 1.1-fold increased hazards of fracture (adjusted hazard ratio, 1.11; 95% CI, 1.04-1.18). Women with baseline TG higher than 300 mg/dl had an adjusted 2.5-fold greater hazards for fractures (95% CI, 1.13-5.44) than women with baseline TG lower than 150 mg/dl. Time-varying analyses showed a comparable TG level-fracture risk relationship. Associations between total cholesterol, low-density lipoprotein cholesterol, or high-density lipoprotein cholesterol levels and fractures were not observed.Midlife women with high fasting plasma TG had an increased risk of incident nontraumatic fracture. Secondary Abstract: Midlife women with fasting plasma triglyceride (TG) of at least 300 mg/dl had 2.5-fold greater hazards of fracture in 2 years later and onward, compared to those with TG below 150 mg/dl, in a multiethnic cohort. Time-varying analyses revealed comparable results.

    View details for DOI 10.1210/jc.2016-1366

    View details for PubMedCentralID PMC5010577

  • Inflammatory Protein Expression in Human Subglottic Stenosis Tissue Mirrors That in a Murine Model ANNALS OF OTOLOGY RHINOLOGY AND LARYNGOLOGY Haft, S., Lee, J. Y., Ghosh, A., Philiponis, G., Malaisrie, N., Leahy, K. P., Singhal, S., Cohen, N. A., Mirza, N. 2014; 123 (1): 65-70


    We undertook to describe the genetic and protein composition of subglottic stenosis (SGS) by measuring an array of protein expression and messenger RNA levels within human SGS tissue. We also sought to compare this human array to cytokine expression from a murine model of SGS in order to confirm the effective translational nature of our animal model.Human granulation tissue from 10 patients with early symptomatic SGS was compared to control bronchus. The expression levels of 24 different cytokines were measured by a Luminex protein assay and real-time polymerase chain reaction.The protein expression in human SGS mirrors that seen in murine SGS. Transforming growth factor β1, interleukin 1β, and matrix metalloproteinase 9 were markedly elevated in both human and mouse SGS tissues. The protein array showed a statistically significant elevation in the proinflammatory cytokines tumor necrosis factor α, interleukin 1, granulocyte macrophage colony-stimulating factor, and interferon γ.This is the first study, to our knowledge, to measure an array of protein expression within human SGS tissue. The expression profile suggests that symptomatic tracheal granulation tissue is mostly within the early inflammatory phase of wound healing and has only begun fibrotic and angiogenic remodeling. This study validates our murine model of SGS, and also helps to define the exact pathways of tissue injury, in the hope of leading to new treatments for this difficult condition.

    View details for DOI 10.1177/0003489414521146

    View details for Web of Science ID 000330823300010

    View details for PubMedID 24574426

  • Sphenoid sinus anatomy and suprasellar extension of pituitary tumors Clinical article JOURNAL OF NEUROSURGERY Ramakrishnan, V. R., Suh, J. D., Lee, J. Y., O'Malley, B. W., Grady, M. S., Palmer, J. N. 2013; 119 (3): 669-674
  • Nasal Congestion, Postnasal Drip, and Aural Fullness Sinonasal schwannoma JAMA OTOLARYNGOLOGY-HEAD & NECK SURGERY Lin, K. F., Lee, J. Y., Kennedy, D. W. 2013; 139 (8): 849-850
  • Pulse Steroid Therapy Inhibits Murine Subglottic Granulation 115th AAO-HNSF Annual Meeting and OTO EXPO Ghosh, A., Philiponis, G., Lee, J. Y., Leahy, K. P., Singhal, S., Cohen, N. A., Mirza, N. SAGE PUBLICATIONS LTD. 2013: 284–90


    Using a functional model of airway granulation tissue in subglottic stenosis, we investigated changes in inflammatory markers within granulation tissue in response to intraperitoneal dexamethasone injections. Changes in inflammatory markers will allow us to identify potential targets for immunological therapy.Institutional Animal Care and Use Committee-approved animal study.Philadelphia Veterans Administration Medical Center animal research facility.Laryngotracheal complexes of donor mice underwent direct airway injury and were transplanted into subcutaneous tissue of 19 recipient mice in 2 groups: steroid treated and untreated, with sample sizes of 10 and 9, respectively. The steroid-treated arm received intraperitoneal injection of dexamethasone for 3 weeks. Laryngotracheal complexes were then harvested, and granulation formation was measured. The messenger RNA (mRNA) expression of transforming growth factor (TGF)-β(1) and interleukin (IL)-1 was quantified.At 3 weeks posttransplantation, there were statistically significant differences in observable granulation formation as well as mRNA expression of TGF-β(1) and IL-1β in all groups within the steroid treated arm as compared with the untreated arm.Systemic steroids have been used to prevent formation of granulation tissue and subglottic stenosis. However, the study of the immunologic markers and the corresponding changes with steroid treatment has not been well studied in animal models. Using a previously described novel murine model, we begin to delineate inflammatory markers that can be applied for potential therapeutic targets.

    View details for DOI 10.1177/0194599812466533

    View details for Web of Science ID 000318361700017

    View details for PubMedID 23172907

  • Bilateral silent sinus syndrome. Ear, nose, & throat journal Suh, J. D., Ramakrishnan, V., Lee, J. Y., Chiu, A. G. 2012; 91 (12): E19-21


    Silent sinus syndrome is a rare clinical entity associated with progressive enophthalmos, collapse of the maxillary sinus, and hypoglobus. We report a case of bilateral silent sinus syndrome in a 29-year-old man. Representative radiographic and intraoperative images are presented. The purpose of this article is to illustrate a new presentation of the disease and to review the current diagnostic and treatment modalities.

    View details for PubMedID 23288826

  • Localization in stereocilia, plasma membrane, and mitochondria suggests diverse roles for NMHC-IIa within cochlear hair cells BRAIN RESEARCH Lalwani, A. K., Atkin, G., Li, Y., Lee, J. Y., Hillman, D. E., Mhatre, A. N. 2008; 1197: 13-22


    NMHC-IIa, a nonmuscle myosin heavy chain isoform encoded by MYH9, is expressed in sensory hair cells and its dysfunction is associated with syndromic and nonsyndromic hearing loss. In this study, we investigate the ultrastructural distribution of NMHC-IIa within murine hair cells to elucidate its potential role in hair cell function. Using previously characterized anti-mouse NMHC-IIa antibody detected with immunogold labelling, NMHC-IIa was observed in the stereocilia, in the cytosol along the plasma membrane, and within mitochondria. Within stereocilia, presence of NMHC-IIa is observed throughout its length along the actin core, from the center to the periphery and at its base in the cuticular plate, suggesting a potential role in structural support. Within the sensory hair cells, NMHC-IIa was distributed throughout the cytoplasm and along the plasma membrane. A novel finding of this study is the localization of NMHC-IIa within the mitochondria, with the majority of the label along its inner membrane folds. The presence of NMHC-IIa within heterogeneous areas of the hair cell suggests that it may play different functional roles in these distinct regions. Thus, mutant NMHC-IIa may cause hearing loss by affecting hair cell dysfunction through structural and or functional disruption of its stereocilia, plasma membrane, and/or mitochondria.

    View details for DOI 10.1016/j.brainres.2007.12.058

    View details for Web of Science ID 000254070900002

    View details for PubMedID 18241845

  • The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro JOURNAL OF BIOLOGICAL CHEMISTRY Fraser, C. S., Lee, J. Y., Mayeur, G. L., Bushell, M., Doudna, J. A., Hershey, J. W. 2004; 279 (10): 8946-8956


    Eukaryotic initiation factor 3 (eIF3) is a 12-subunit protein complex that plays a central role in binding of initiator methionyl-tRNA and mRNA to the 40 S ribosomal subunit to form the 40 S initiation complex. The molecular mechanisms by which eIF3 exerts these functions are poorly understood. To learn more about the structure and function of eIF3 we have expressed and purified individual human eIF3 subunits or complexes of eIF3 subunits using baculovirus-infected Sf9 cells. The results indicate that the subunits of human eIF3 that have homologs in Saccharomyces cerevisiae form subcomplexes that reflect the subunit interactions seen in the yeast eIF3 core complex. In addition, we have used an in vitro 40 S ribosomal subunit binding assay to investigate subunit requirements for efficient association of the eIF3 subcomplexes to the 40 S ribosomal subunit. eIF3j alone binds to the 40 S ribosomal subunit, and its presence is required for stable 40 S binding of an eIF3bgi subcomplex. Furthermore, purified eIF3 lacking eIF3j binds 40 S ribosomal subunits weakly, but binds tightly when eIF3j is added. Cleavage of a 16-residue C-terminal peptide from eIF3j by caspase-3 significantly reduces the affinity of eIF3j for the 40 S ribosomal subunit, and the cleaved form provides substantially less stabilization of purified eIF3-40S complexes. These results indicate that eIF3j, and especially its C terminus, play an important role in the recruitment of eIF3 to the 40 S ribosomal subunit.

    View details for DOI 10.1074/jbc.M312745200

    View details for Web of Science ID 000189265900053

    View details for PubMedID 14688252

Latest information on COVID-19