Author

Danielle J. Gelsinger

University of California San Diego

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

Biology Disciplines

Click to filter author papers

Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Approach:experimental assay· 1 Organism:human· 1 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

Alexander R. D. Jordon· 1 shared Amanda Mercedes JamiesoniD· 1 shared Anthony John O’DonoghueiD· 1 shared Craig P. EbersoniD· 1 shared Elany Barbosa da SilvaiD· 1 shared Jack G. HaggettiD· 1 shared Lawrence LiuiD· 1 shared Meredith J. CraneiD· 1 shared

Activity by Year

2025-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiochemistry

Alexander R. D. Jordon

Mutual co-authors in cluster

Author profile →

1 paper

Recent·Most cited

Aspartic proteases are abundant and active in acidified wound fluid

Elany Barbosa da Silva, Meredith J. Crane, Lawrence Liu, Danielle J. Gelsinger, Alexander R. D. Jordon, Phuong Le, Jack G. Haggett, Samuel A. Myers, Robin L. McKinney, Craig P. Eberson, Amanda Mercedes Jamieson, Anthony John O’Donoghue

This study identifies aspartic proteases as active enzymes in acidified wound fluid, showing their activity is optimal between pH 3.0 and 3.8 and persists for ten days post-injury.

Journal of Biological Chemistry · Sep 16, 2025Peer-reviewedBiochemistry