Author

D. Belnap

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1 Assay:DNA methylation· 1 Research Focus:gene regulatory network inference· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

A. D. Gloss· 1 shared A. Deutschbauer· 1 shared A. hawks· 1 shared A. M. Manuel· 1 shared A. Muszynski· 1 shared A. Peterson· 1 shared A. Sharma· 1 shared B. Preece· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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Curved chords = mutual co-authorship

1 shared paperMicrobiology

A. D. Gloss

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

A weaponized phage suppresses competitors in historical and modern metapopulations of pathogenic bacteria

N. Backman, S. M. Latorre, E. Symeonidi, A. Muszynski, E. Bleak, L. Eads, P. Martinez-Koury, S. Som, A. hawks, A. D. Gloss, D. Belnap, A. M. Manuel, A. Deutschbauer, J. Bergelson, P. Azadi, , T. Karasov

The paper identifies a tailocin, a phage-derived element, used by Pseudomonas spp. to suppress competitors in metapopulations, showing its persistence over 170 years.

bioRxiv · Apr 17, 2023 · PreprintMicrobiology

Minimal system for assembly of SARS-CoV-2 virus like particles

H. Swann, A. Sharma, B. Preece, A. Peterson, C. Eldredge, D. Belnap, M. Vershinin, S. Saffarian

The paper demonstrates the assembly of non-infectious SARS-CoV-2 virus-like particles using viral proteins S, M, and E in mammalian cells, showing their structural stability and potential for vaccine development.

Scientific Reports · Dec 14, 2020Peer-reviewedBiophysics

Membrane Proteins Significantly Restrict Exosome Mobility

M. Skliar, V. Chernyshev, D. Belnap, S. Hakami, I. Stijleman, R. Rachamadugu, P. Bernard

This study shows that surface proteins significantly reduce exosome mobility, making it a dynamic property influenced by the extracellular environment.

bioRxiv · Sep 30, 2017Biochemistry