Bachelor of Science, University of Notre Dame, Chemistry and Russian Languages & Literature (2013)
Doctor of Philosophy, Stanford University, CHEM-PHD (2019)
Michael Snyder, Postdoctoral Faculty Sponsor
Reverse-ChIP Techniques for Identifying Locus-Specific Proteomes: A Key Tool in Unlocking the Cancer Regulome.
2023; 12 (14)
A phenotypic hallmark of cancer is aberrant transcriptional regulation. Transcriptional regulation is controlled by a complicated array of molecular factors, including the presence of transcription factors, the deposition of histone post-translational modifications, and long-range DNA interactions. Determining the molecular identity and function of these various factors is necessary to understand specific aspects of cancer biology and reveal potential therapeutic targets. Regulation of the genome by specific factors is typically studied using chromatin immunoprecipitation followed by sequencing (ChIP-Seq) that identifies genome-wide binding interactions through the use of factor-specific antibodies. A long-standing goal in many laboratories has been the development of a 'reverse-ChIP' approach to identify unknown binding partners at loci of interest. A variety of strategies have been employed to enable the selective biochemical purification of sequence-defined chromatin regions, including single-copy loci, and the subsequent analytical detection of associated proteins. This review covers mass spectrometry techniques that enable quantitative proteomics before providing a survey of approaches toward the development of strategies for the purification of sequence-specific chromatin as a 'reverse-ChIP' technique. A fully realized reverse-ChIP technique holds great potential for identifying cancer-specific targets and the development of personalized therapeutic regimens.
View details for DOI 10.3390/cells12141860
View details for PubMedID 37508524
- Students and Postdocs are Needed on the Provost Search Committee The Stanford Daily. https://stanforddaily.com/2023/05/07/from-the-community-students-and-postdocs-are-needed-on-the-provost-search-committee/. 2023
- A Note on Academic Freedom and Institutional Orthodoxy The Stanford Daily. https://stanforddaily.com/2023/06/15/from-the-community-a-note-on-academic-freedom-and-institutional-orthodoxy/. 2023
- Shared Governance The Stanford Daily. https://stanforddaily.com/2023/06/07/from-the-community-shared-governance/. 2023
- A Primer on the Stanford Budget or: How I Learned to Stop Worrying and Love the Endowment The Stanford Daily. https://stanforddaily.com/2022/04/13/from-the-community-a-primer-on-the-stanford-budget/. 2022
- Student Activism, not Endowment Returns, Led to Recent Affordability Initiatives The Stanford Daily. https://stanforddaily.com/2022/02/02/from-the-community-student-activism-not-endowment-returns-led-to-recent-affordability-initiatives/. 2022
Differential effects of modified batrachotoxins on voltage-gated sodium channel fast and slow inactivation.
Cell chemical biology
Voltage-gated sodium channels (NaVs) are targets for a number of acute poisons. Many of these agents act as allosteric modulators of channel activity and serve as powerful chemical tools for understanding channel function. Herein, we detail studies with batrachotoxin (BTX), a potent steroidal amine, and three ester derivatives prepared through de novo synthesis against recombinant NaV subtypes (rNaV1.4 and hNaV1.5). Two of these compounds, BTX-B and BTX-cHx, are functionally equivalent to BTX, hyperpolarizing channel activation and blocking both fast and slow inactivation. BTX-yne-a C20-n-heptynoate ester-is a conspicuous outlier, eliminating fast but not slow inactivation. This property differentiates BTX-yne among other NaV modulators as a unique reagent that separates inactivation processes. These findings are supported by functional studies with bacterial NaVs (BacNaVs) that lack a fast inactivation gate. The availability of BTX-yne should advance future efforts aimed at understanding NaV gating mechanisms and designing allosteric regulators of NaV activity.
View details for DOI 10.1016/j.chembiol.2021.12.003
View details for PubMedID 34963066