Author

D. M. Duong

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Assay:proteomics· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:experimental assay· 1

Frequent Co-Authors

N. T. Seyfried· 3 shared E. B. Dammer· 2 shared I. Bishof· 2 shared A. I. Levey· 1 shared J. J. Lah· 1 shared J. N. Peoples· 1 shared J. Q. Kwong· 1 shared K. R. Hardin· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

N. T. Seyfried

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Author profile →

3 papers

Recent·Most cited

Mitochondrial energy dysfunction induces remodeling of the cardiac mitochondrial protein acylome

J. N. Peoples, N. Ghazal, D. M. Duong, K. R. Hardin, N. T. Seyfried, V. Faundez, J. Q. Kwong

This study shows that mitochondrial energy dysfunction in the heart causes acylome remodeling, including increased acetylation and malonylation of mitochondrial proteins, with functional consequences for IDH2 and SIRT5.

bioRxiv · Jan 31, 2021Cell Biology

Middle-down proteomics reveals dense sites of methylation and phosphorylation in arginine-rich RNA-binding proteins

S. R. Kundinger, I. Bishof, E. B. Dammer, D. M. Duong, N. T. Seyfried

The paper uses middle-down proteomics to identify dense methylation and phosphorylation sites in arginine-rich RNA-binding proteins, revealing their potential functional opposition.

bioRxiv · Sep 19, 2019Biochemistry

RNA-binding proteins with mixed charge domains self-assemble and aggregate in Alzheimer’s Disease

I. Bishof, E. B. Dammer, D. M. Duong, M. Gearing, J. J. Lah, A. I. Levey, N. T. Seyfried

This study identifies mixed charge domains in RNA-binding proteins that self-assemble and aggregate in Alzheimer’s Disease, linking them to Tau co-aggregation and nuclear RNA granule formation.

bioRxiv · Jan 4, 2018Biochemistry