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Christina M. Woo

Researcher at Harvard University

Publications -  32
Citations -  618

Christina M. Woo is an academic researcher from Harvard University. The author has contributed to research in topics: Small molecule & Glycosylation. The author has an hindex of 10, co-authored 29 publications receiving 275 citations.

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Labeling Preferences of Diazirines with Protein Biomolecules

TL;DR: Alkyl diazirines are an especially effective chemistry for surveying the membrane proteome and will facilitate design and interpretation of biomolecular labeling experiments with diazIRines, according to a systematic evaluation of the labeling preferences.
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Engineering a Proximity-Directed O-GlcNAc Transferase for Selective Protein O-GlcNAcylation in Cells.

TL;DR: These first proximity-directed OGT constructs provide a flexible strategy for targeting additional proteins and a template for further engineering of OGT and the O-GlcNAc proteome in the future.
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Small Molecule Interactome Mapping by Photoaffinity Labeling Reveals Binding Site Hotspots for the NSAIDs.

TL;DR: Using SIM-PAL, the NSAID interactome consisting of over 1000 significantly enriched proteins was identified and nearly 200 conjugated peptides representing direct binding sites of the photo-NSAIDs with proteins from Jurkat and K562 cells were characterized.
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Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis.

Rebeca Kawahara, +56 more
- 01 Nov 2021 - 
TL;DR: In this article, a community study, comprising both developers and users of glycoproteomics software, evaluates solutions for system-wide glycopeptide analysis and concludes that diverse software packages for comprehensive glyopeptides data analysis exist, points to several high-performance search strategies and specifies key variables that will guide future software developments and assist informatics decision-making in glycoproteinomics.
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Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.

TL;DR: These findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite, and inform efforts to engineer substrates to explore biological functions.