@article{ETD,
      school = {Ph.D.},
      author = {Lee, Yerim},
      url = {http://digitalcollections.ohsu.edu/record/7715},
      title = {Probing the spatiotemporal dynamics of Ras GTPases on the  cell membrane with high-throughput single-molecule  microscopy},
      publisher = {Marylhurst University: Oregon Health and Science  University},
      abstract = {Rat sarcoma viral oncogene homolog (Ras) proteins are  important signaling molecules ubiquitously expressed in  eukaryotes and are key regulators of normal proliferation  and differentiation. The Ras family is a group of small  GTPases that reside on the membrane and are involved in  multiple cell signaling cascades.They transmit growth  signals from cell surface receptors, such as tyrosine  kinase receptors, by switching between GTP or GDP bound  states. Ras is inactive when GDP bound, but stimulation by  upstream factors results in the exchange of GDP for GTP  with the aid of guanine exchange factors (GEFs). GTP bound  Ras is able to bind and recruit downstream electors to the  membrane. Although Ras is able to hydrolyze GTP to GDP, the  endogenous reaction is slow and is catalyzed by  GTPase-activating proteins (GAPs). A third of all human  cancers have a constitutively active Ras mutation, making  Ras one of the most frequently mutated oncogenes. Oncogenic  Ras mutations are single base substitutions that stabilize  GTP-bound state which results in constitutive activation of  Ras and its target proteins, leading to several hallmarks  of cancer.},
      number = {ETD},
      doi = {https://doi.org/10.6083/3t945r47j},
      recid = {7715},
      address = {2019},
}