Author

D. Burns

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

Biophysics· 2 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Organism:human· 1 Assay:imaging· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

D. A. Potoyan· 2 shared V. Venditti· 2 shared A. Singh· 1 shared B. Ogunlade· 1 shared D. E. McCoy· 1 shared E. Klopfer· 1 shared J. A. Dionne· 1 shared L. Herndon· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 18 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

2 shared papersBiophysics

D. A. Potoyan

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Heart cockle shells transmit sunlight to photosymbiotic algae using bundled fiber optic cables and condensing lenses

D. E. McCoy, D. Burns, E. Klopfer, L. Herndon, B. Ogunlade, J. A. Dionne, S. Johnsen

The paper demonstrates that heart cockles use biophotonic structures to transmit sunlight to their photosymbiotic algae while filtering harmful UV radiation.

Nature Communications · Nov 19, 2024Peer-reviewedEvolutionary Biology

Temperature-Sensitive Contact Modes Allosterically Gate TRPV3

D. Burns, V. Venditti, D. A. Potoyan

This study identifies temperature-sensitive residue-residue interactions in TRPV3 using simulations and machine learning, revealing how these contacts allosterically regulate channel gating.

bioRxiv · Jan 2, 2023Biophysics

Temperature Sensitive Contacts in Disordered Loops Tune Enzyme I Activity

D. Burns, A. Singh, V. Venditti, D. A. Potoyan

This study identifies temperature-sensitive contacts in disordered loops of Enzyme I homologs that tune catalytic activity across temperatures.

bioRxiv · Jun 18, 2022Biophysics