Author

J. Bergeron

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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Biophysics· 3 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:bacteria (other)· 3 Assay:cryo-EM· 3 Research Focus:protein folding & dynamics· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

D. Mann· 2 shared J. Fan· 2 shared J. M. Kollman· 2 shared A. Beavil· 1 shared A. Burrell· 1 shared A. Muenks· 1 shared C. Kamischke· 1 shared C. Parry· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

D. Mann

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

A family of bacterial actin homologues forms a 3-stranded tubular structure

J. Bergeron, S. L. Lale-Farjat, H. M. Lewicka, C. Parry, J. M. Kollman

The paper identifies a family of bacterial actins forming a unique 3-stranded tubular structure via ATP binding, revealing new insights into bacterial cytoskeletal diversity.

bioRxiv · Nov 7, 2023 · PreprintBiophysics

Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome

S. L. Evans, M. Al-Hazeem, D. Mann, N. Smetacek, A. Beavil, Y. Sun, T. Chen, G. Dykes, L.-N. Liu, J. Bergeron

This study uses single-particle cryo-EM to determine the structure of a native α-carboxysome from a marine cyanobacterium, revealing its shell architecture and internal enzyme organization.

bioRxiv · Feb 18, 2022Biophysics

Oligomerization of the FliF domains suggests a coordinated assembly of the bacterial flagellum MS ring

G. Mariano, R. Faba-Rodriguez, S. Bui, W. Zhao, J. Ross, S. Tsokov, J. Bergeron

This study investigates the oligomerization of FliF domains in Salmonella typhimurium, revealing how RBM1, RBM2, and RBM3 contribute to the assembly of the MS ring through domain interactions.

bioRxiv · Sep 23, 2021Biophysics

Structure and lipid dynamics in the A. baumannii maintenance of lipid asymmetry (MLA) inner membrane complex

D. Mann, J. Fan, D. Farrell, K. Somboon, A. Muenks, S. Tzokov, S. Khalid, F. DiMaio, S. Miller, J. Bergeron

This study reports cryo-EM structures of the A. baumannii MLA complex in different states and proposes a molecular mechanism for lipid transport.

bioRxiv · May 30, 2020Biochemistry

The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane

C. Kamischke, J. Fan, J. Bergeron, H. D. Kulasekara, Z. D. Dalebroux, A. Burrell, J. M. Kollman, S. I. Miller

This study identifies the Mla system in Acinetobacter baumannii as essential for glycerophospholipid transport to the outer membrane and antibiotic resistance.

bioRxiv · Aug 4, 2018Microbiology