Overview:
Our laboratory uses mass spectrometry-based proteomics to investigate cellular processes related to protein homeostasis. We study the mechanisms of cellular protein folding, degradation and repair from a global perspective. We also investigate how these processes are affected by disease and aging. Current research areas include:
- development of proteomic methodologies for analysis of protein folding and degradation
- uncovering the mechanism of selectivity in macroautophagy
- determining the cellular basis of toxicity of prion aggregates
- understanding the relationship between protein turnover and aging
Recent Publications:
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The effect of protein folding stability on methionine oxidation
J Biol Chem. (2022)
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Cross-species comparison of proteome turnover kinetics
Mol. Cel. Proteomics (2018)
Mol. Cel. Proteomics (2021)
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Protein degradation in prion infected cells
Sci. Rep. (2020)
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Quantitative analysis of in vivo methionine oxidation of the human proteome
J. Proteome Res. (2020)
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Global analysis of methionine oxidation provides a census of folding stabilities for the human proteome
Proc. Nat. Acad. Sci. (2019)
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Proteome-wide modulation of degradation dynamics in response to growth arrest
Proc. Nat. Acad. Sci. (2017)
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Global analysis of protein dynamics by mass spectrometry
Mol. Cel. Proteomics (2016)
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Substrate selectivity in basal macroautophagy
Cell Reports (2016)
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Conformational adaptation of prion strains
Cold Spring Harb Perspect Med. (2016)
