Author

Harris D. Bernstein

National Institutes of HealthORCID 0000-0002-4941-3741Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

Aidan B. GrosasiD· 1 shared Alanah Grace EisenhuthiD· 1 shared Alastair G. StewartiD· 1 shared Anthony Simon DoniD· 1 shared Catherine ZhangiD· 1 shared Constance B. BaileyiD· 1 shared Denisse L. LeytoniD· 1 shared Ghaeath S. K. Abbas· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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1 shared paperBiochemistry

Aidan B. GrosasORCID

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2 papers

Recent·Most cited

Mechanism of phospholipid transport to the bacterial outer membrane by TAM.

Alanah Grace Eisenhuth, Lachlan S. R. Adamson, Catherine Zhang, Ghaeath S. K. Abbas, Rachel A. North, Denisse L. Leyton, Harris D. Bernstein, Simon H. J. Brown, Alastair G. Stewart, Constance B. Bailey, Anthony Simon Don, Aidan B. Grosas, Matthew Thomas Doyle

This study identifies TAM as a bacterial phospholipid transport system, revealing its structure and mechanism for lipid delivery to the outer membrane.

bioRxiv · Mar 24, 2026 · PreprintBiochemistry

The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro

Xu Wang, Sarah B. Nyenhuis, Harris D. Bernstein

This study shows that the TAM complex catalyzes the assembly of bacterial outer membrane proteins in vitro, similar to the BAM complex, and identifies the necessity of TamA and TamB for its activity.

Nature Communications · Aug 23, 2024Peer-reviewedMicrobiology