Mark Chance
Case Western Reserve University, OH·Biochemistry
Cancer is driven by changes in proteins — which ones are present, how they are chemically modified, which partners they bind, and how drugs latch onto them. Measuring all of that requires mass spectrometry, an instrument family that weighs molecules precisely enough to identify proteins and their modifications from complex samples, plus the computational tools to interpret the results.
- Fields
Biochemistry
Biophysics
Medicine & Clinical Research
- Topics
proteomics
mass spectrometry
post-translational modifications
- Grants
- 1 known grant, through Mar 2030
What they work on
- Provide proteomic and small-molecule analysis to cancer investigators, including protein identification, post-translational modification characterization, quantitative proteomics, protein interactome mapping and metabolomics, across collaborative and high-throughput service modes.
- Extend RoKAI, software that infers kinase activity from phosphoproteomic data using context-specific kinase–substrate interactions, to reveal how signaling networks are rewired in cancer and in therapy resistance.
- Build single-cell proteomics capability with a target of 3,000 proteins detected per cell, and deploy new mass spectrometry systems reaching roughly three times current proteome coverage to feed systems-biology analyses.
- Apply trifluoromethylation footprinting, a chemical labeling method that marks solvent-exposed protein surfaces, to map protein dynamics and drug binding sites at single-residue resolution for structural biology projects.
More about the research
This project operates the Proteomics Shared Resource of the Case Comprehensive Cancer Center, with facilities and staff at two sites, providing protein and small-molecule analysis to cancer investigators while developing new measurement methods.
Why it matters
Cancer researchers rarely have the instruments or expertise to measure proteins, their chemical modifications and their binding partners on their own; a shared facility makes those measurements available and supplies tools such as kinase-activity inference software that help pinpoint the signaling changes behind tumor formation and resistance to therapy. Structural mass spectrometry methods that resolve drug binding sites at single-residue precision could help explain how candidate drugs engage their targets.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Alexey Nesvizhskii
University of Michigan, MI·Biochemistry
Improve interactome analysis by moving the REPRINT resource (SAINT scoring plus the CRAPome contaminant repository) to an MSFragger-based pipeline, expanding CRAPome, and refining scoring of protein–protein interactions from AP-MS data.
Anna Malovannaya
Baylor College of Medicine, TX·Biochemistry
Provide antibody-based protein profiling for cancer researchers using a custom reverse phase protein array (RPPA), which measures many specific proteins across many samples.
Arthur Salomon
University of California-San Francisco, CA·Biochemistry
Identify the binding partners of signaling proteins in T cell lines and primary mouse T cells, using TurboID, a labeling enzyme that tags nearby proteins in living cells, followed by mass spectrometry.
The school
Case Western Reserve University: 34 labs on PI Pages, $643M a year on research, 213 research doctorates a year.
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