Daniel Nelson

University of Maryland; ExoLytics; Nelson Lab

My research interests include studying bacterial pathogenesis and bacteriophage-host interactions, although the largest part of my current research is centered on proteins that are part of the bacteriophage lytic system. These proteins, known as lysins or endolysins, have the ability to rapidly bind to and degrade the cell wall of a host species. As such, they represent an alternative approach to conventional antibiotics. My laboratory focuses on structure/function and engineering studies for several of the more active endolysins. Based on this collected knowledge, my group is now generating endolysins with more desirable attributes, such as higher activity, an expanded host range, or a more favorable thermostability profile. It is anticipated these bioengineering approaches will result in development of the next generation endolysins with enhanced properties.

Source-reported research

Research context

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  • 2026-08-05: coauthored “Directed evolution of the bacteriophage endolysin PlyC reveals a charge-mediated mechanism of thermal stabilization”. [2] [3] [4] [5]
Sources and review
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  2. api.crossref.org Observed . Explicit source name or declared given/family rendering; exact author slot
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Reviewed by ai:codex-identities-ce68394c9be2. Consolidated final review. Concise dated publication-history context cites the exact supported author/work evidence; no current-project, current-employment, individual-contribution or unobserved result claims. Older work is dated and does not count as a recent-paper selection.

Source-selected papers

AI-assisted source report. It may be incomplete or mistaken and may not reflect current work. Reviewed .

Sources and review
  1. phage.directory Observed . Native directory ID and submitted public anchors in the frozen roster
  2. api.crossref.org Observed . Explicit source name or declared given/family rendering; exact author slot
  3. api.crossref.org Observed . Primary exact DOI author-block ORCID
  4. api.crossref.org Observed . Decoded own work title
  5. api.crossref.org Observed . Own DOI
  6. doi.org Observed . Canonical exact-DOI native paper ID

Reviewed by ai:codex-identities-ce68394c9be2. Consolidated final review of exact own DOI, actual author slot/identifier or independently accepted work affiliation, phage relevance and source date. Native IDs resolve the same DOI; candidate namesakes and alternate editions remain explicit holds. No global identity or employment/contribution inference.