Honors & Awards

  • Gates Millennium Scholarship, Bill & Melinda Gates Foundation / UNCF (2008)
  • Graduate Research Fellowship, National Science Foundation (NSF) (2012)
  • Gilliam Fellowships for Advanced Study, Howard Hughes Medical Institute (2015)

Professional Affiliations and Activities

  • Member, Stanford Human Subjects Institutional Review Board (2015 - Present)
  • President, Stanford Biosciences Student Association (2016 - 2017)
  • CGAP Graduate Student Representative, Stanford Biosciences Committee on Graduate Admissions and Policy (2014 - 2017)

Education & Certifications

  • B.S., Massachusetts Institute of Technology, Biology & Brain and Cognitive Sciences (2012)

Stanford Advisors

Current Research and Scholarly Interests

Basic understanding of the mechanisms underlying autophagy, chaperones, and protein quality control in the nervous system as a route to more effective therapies for neurodegenerative diseases (Alzheimer's, Frontotemporal Dementia, Huntington's, etc.).

All Publications

  • SIRT1 collaborates with ATM and HDAC1 to maintain genomic stability in neurons NATURE NEUROSCIENCE Dobbin, M. M., Madabhushi, R., Pan, L., Chen, Y., Kim, D., Gao, J., Ahanonu, B., Pao, P., Qiu, Y., Zhao, Y., Tsai, L. 2013; 16 (8): 1008-U54


    Defects in DNA repair have been linked to cognitive decline with age and neurodegenerative disease, yet the mechanisms that protect neurons from genotoxic stress remain largely obscure. We sought to characterize the roles of the NAD(+)-dependent deacetylase SIRT1 in the neuronal response to DNA double-strand breaks (DSBs). We found that SIRT1 was rapidly recruited to DSBs in postmitotic neurons, where it showed a synergistic relationship with ataxia telangiectasia mutated (ATM). SIRT1 recruitment to breaks was ATM dependent; however, SIRT1 also stimulated ATM autophosphorylation and activity and stabilized ATM at DSB sites. After DSB induction, SIRT1 also bound the neuroprotective class I histone deacetylase HDAC1. We found that SIRT1 deacetylated HDAC1 and stimulated its enzymatic activity, which was necessary for DSB repair through the nonhomologous end-joining pathway. HDAC1 mutations that mimic a constitutively acetylated state rendered neurons more susceptible to DNA damage, whereas pharmacological SIRT1 activators that promoted HDAC1 deacetylation also reduced DNA damage in two mouse models of neurodegeneration. We propose that SIRT1 is an apical transducer of the DSB response and that SIRT1 activation offers an important therapeutic avenue in neurodegeneration.

    View details for DOI 10.1038/nn.3460

    View details for Web of Science ID 000322323000010

    View details for PubMedID 23852118

    View details for PubMedCentralID PMC4758134

  • On the Technology Prospects and Investment Opportunities for Scalable Neuroscience arXiv Dean, T., Ahanonu, B., et al 2013; 1307 (7302)