Author

David Nicolas Giuseppe Huebert

University of TorontoORCID 0009-0001-9841-0213Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 1 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Organism:plant (other)· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

diego fernando quito-avilaiD· 1 shared Humberto DebatiD· 1 shared Justin J. KingiD· 1 shared Mani LarijaniiD· 1 shared Nicolás BejermaniD· 1 shared Robert A. Alvarez‐QuintoiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

6 top collaborators · 7 mutual co-author links

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1 shared paperMicrobiology

diego fernando quito-avilaORCID

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2 papers

Recent·Most cited

MicrobiologyVirusesPeer-reviewedOct 8, 2026

Data mining sheds light on a novel family of plant-associated negative-sense RNA viruses linked to lispiviruses

Nicolás Bejerman, David Nicolas Giuseppe Huebert, Robert A. Alvarez‐Quinto…·Humberto Debat

The paper identifies a new family of plant-associated negative-sense RNA viruses using transcriptomic data and structural analysis, expanding known diversity by ~40-fold.

DOI 10.3390/v18101113

plant (other)bulk RNA-seq

𝕏 PostBluesky

BiochemistrybioRxivPreprintSep 29, 2025

AID/APOBEC3 Dynamic Catalytic Pockets and AID-α7 Regulation Mechanisms

David Nicolas Giuseppe Huebert, Justin J. King, Mani Larijani

The paper uses molecular dynamics to analyze catalytic pocket dynamics of AID/APOBEC3 enzymes, finding that A3G-CD2 is predominantly open while most AID/APOBECs are closed or indeterminate, with specific residues influencing pocket states and catalytic activity.

DOI 10.1101/2025.09.29.679391

biophysical modelingprotein folding & dynamics

𝕏 PostBluesky