Honors & Awards
EMBO Short Term Fellowship, European Molecular Biology Organization (November 2016)
'Hermanas in STEM' Proposal awarded funding, Diversity Improvement Funds (VPGE), Stanford University (2015)
Bio-X Graduate Fellowship, Stanford Bio-X, Stanford University (2014-2015)
ADVANCE Fellow, Stanford University (2013)
Professional Affiliations and Activities
Co-President, Stanford Hermanas in STEM (2015 - Present)
Biology Liaison, Vice Provost for Teaching and Learning (2014 - 2016)
International Student Advocate, BioAIMs (2015 - 2016)
Career Development Chair, BioAIMs (2014 - 2015)
Lucy O'Brien, Doctoral (Program)
Long-term live imaging of the Drosophila adult midgut reveals real-time dynamics of division, differentiation, and loss.
Organ renewal is governed by the dynamics of cell division, differentiation, and loss. To study these dynamics in real time, we present a platform for extended live imaging of the adult Drosophila midgut, a premier genetic model for stem cell-based organs. A window cut into a living animal allows the midgut to be imaged while intact and physiologically functioning. This approach prolongs imaging sessions to 12-16 hours and yields movies that document cell and tissue dynamics at vivid spatiotemporal resolution. Applying a pipeline for movie processing and analysis, we uncover new, intriguing cell behaviors: that mitotic stem cells dynamically re-orient, that daughter cells use slow kinetics of Notch activation to reach a fate-specifying threshold, and that enterocytes extrude via ratcheted constriction of a junctional ring. By enabling real-time study of midgut phenomena that were previously inaccessible, our platform opens a new realm for dynamic understanding of adult organ renewal.
View details for PubMedID 30427308
Role of Metal Ions on the Activity of Mycobacterium tuberculosis Pyrazinamidase
AMERICAN JOURNAL OF TROPICAL MEDICINE AND HYGIENE
2012; 87 (1): 153-161
Pyrazinamidase of Mycobacterium tuberculosis catalyzes the conversion of pyrazinamide to the active molecule pyrazinoic acid. Reduction of pyrazinamidase activity results in a level of pyrazinamide resistance. Previous studies have suggested that pyrazinamidase has a metal-binding site and that a divalent metal cofactor is required for activity. To determine the effect of divalent metals on the pyrazinamidase, the recombinant wild-type pyrazinamidase corresponding to the H37Rv pyrazinamide-susceptible reference strain was expressed in Escherichia coli with and without a carboxy terminal. His-tagged pyrazinamidase was inactivated by metal depletion and reactivated by titration with divalent metals. Although Co(2+), Mn(2+), and Zn(2+) restored pyrazinamidase activity, only Co(2+) enhanced the enzymatic activity to levels higher than the wild-type pyrazinamidase. Cu(2+), Fe(2+), Fe(3+), and Mg(2+) did not restore the activity under the conditions tested. Various recombinant mutated pyrazinamidases with appropriate folding but different enzymatic activities showed a differential pattern of recovered activity. X-ray fluorescence and atomic absorbance spectroscopy showed that recombinant wild-type pyrazinamidase expressed in E. coli most likely contained Zn. In conclusion, this study suggests that M. tuberculosis pyrazinamidase is a metalloenzyme that is able to coordinate several ions, but in vivo, it is more likely to coordinate Zn(2+). However, in vitro, the metal-depleted enzyme could be reactivated by several divalent metals with higher efficiency than Zn.
View details for DOI 10.4269/ajtmh.2012.10-0565
View details for Web of Science ID 000306153500026
View details for PubMedID 22764307
View details for PubMedCentralID PMC3391041