Bio

Bio


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 west coast at Stanford to head the division of General Otololarygnology.
Dr. Lee's clinical interests includes primary sinusitis, neck masses, chronic tonsillitis, sleep apnea surgery, chronic ear disorders amongst others. Her research focus is in improving and developing education for the next generation of otolaryngologists.

Clinical Focus


  • Otolaryngology

Academic Appointments


Professional Education


  • Residency:University of Pennsylvania Hospital (2013) PA
  • Internship:University of Pennsylvania Hospital (2009) PA
  • Medical Education:Albert Einstein College of Medicine (2008) NY

Publications

Journal Articles


  • 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 OTOLARYNGOLOGY-HEAD AND NECK SURGERY Ghosh, A., Philiponis, G., Lee, J. Y., Leahy, K. P., Singhal, S., Cohen, N. A., Mirza, N. 2013; 148 (2): 284-290

    Abstract

    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

    Abstract

    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

    Abstract

    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

    Abstract

    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

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