Stephanie See

Stephanie See, Kampmann lab

[email protected]
Graduate student, Chemistry and Chemical Biology



  • PhD candidate in the program for Chemistry and Chemical Biology at UCSF (San Francisco, CA)
  • B.A. in Biological Chemistry from Wellesley College (Wellesley, MA)


  • Mavor D, Barlow K, Thompson S, Barad BA, Bonny AR, Cario CL, Gaskins G, Liu Z, Deming L, Axen SD, Caceres E, Chen W, Cuesta A, Gate RE, Green EM, Hulce KR, Ji W, Kenner LR, Mensa B, Morinishi LS, Moss SM, Mravic M, Muir RK, Niekamp S, Nnadi CI, Palovcak E, Poss EM, Ross TD, Salcedo EC, See SK, Subramaniam M, Wong AW, Li J, Thorn KS, Conchúir SÓ, Roscoe BP, Chow ED, DeRisi JL, Kortemme T, Bolon DN, Fraser JS. Determination of ubiquitin fitness landscapes under different chemical stresses in a classroom setting. Elife. 2016 Apr 25;5. PMC4862753.
  • See SK, Hoogendoorn S, Chung AH, Ye F, Steinman JB, Sakata-Kato T, Miller RM, Cupido T, Zalyte R, Carter AP, Nachury MV, Kapoor TM, Chen JK. Cytoplasmic Dynein Antagonists with Improved Potency and Isoform Selectivity. ACS Chem Biol. 2016 Jan 15;11(1):53-60. PMC4715766.

Honors and Awards:

  • National Defense Science & Engineering Graduate Fellowship (NDSEG), 2016

Research experience:

  • Chen Laboratory, Stanford University (Stanford, CA) – Developed isoform specific small-molecule antagonists of cytoplasmic dyneins.
  • Chang Laboratory, Massachusetts Institute of Technology (Cambridge, MA) – Investigated the role of the post-translational modification poly(ADP-ribose) in the stress granule.
  • Gage Laboratory, The Salk Institute for Biological Studies (La Jolla, CA) – Investigated the effect of exercise and housing conditions on neurogenesis in adult mice.

Research interests:

Many neurodegenerative diseases possess striking molecular signatures, including the formation of protein aggregates in the brain that manifest as lesions or inclusion bodies commonly associated with the loss of brain mass and cognitive impairment. A growing body of work suggests that aggregating species across many of these diseases share a prion-like mode of transmission. In particular, I am exploring the prion-like propagation of alpha-synuclein, the intrinsically disordered protein that aggregates into insoluble fibrils in Parkinson’s patients. Although Parkinson’s disease impacts nearly 7 million people worldwide and is the second most common neurodegenerative disease, the molecular determinants involved in the cellular spread of alpha-synuclein are still poorly understood. Using a combination of genomics, bioinformatics, and biochemistry I hope to define mechanisms of alpha-synuclein transmission that may lead to new therapeutic avenues.