Gibbs, E. B., et al., (2017).
Phosphorylation Induces Sequence-Specific Conformational Switches in the
RNA Polymerase II C-Terminal Domain.
accepted Nature Communications.

Yan, W., et. al., (2017).
Structural Snapshots of an Engineered Cystathionine-gamma-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.

Mayfield, J. E., et al., (2016).
Mapping the phosphorylation pattern of Drosophila RNA polymerase II carboxyl-terminal domain using ultraviolet photodissociation mass spectrometry.
ACS Chem Biol.

Cramer, S., et al., (2016).
Systemic depletion of serum L-Cyst(e)ine with an engineered human enzyme induces production of reactive oxygen species and suppresses tumor growth in mice.
Nature Medicine

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The transcription process in eukaryotic cells is controlled by the C-terminal domain of RNA polymerase II through its post-translational modification states. However enzymes that recognize the same phosphorylation site in CTD can lead to different transcriptional outcomes. To address the central question that how gene-specific regulation was achieved by CTD regulatory enzymes, we investigate the structure function mechanism of CTD phosphatases. Specifically, a protein regulation prolyl isomerization state of the CTD proline residues can affect the transcription by controlling the availability of the substrate pools for the phosphatases. We also develop chemical compounds as tools to understand the proline isomerization state specificity of CTD binding enzymes and chemical probes to promote neuron regeneration.

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