ReviewSub-cellular biochemistry2022
Structure and Assembly of the Bacterial Flagellum.
Review in Sub-cellular biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- The structure of the Vibrio alginolyticus flagellar filament suggests molecular mechanism for the rotation of sheathed flagella.Nature communications · 2026Article
- Complexity and psychopathology: from mechanistic science to a physical understanding of the mental conditions based on chaos and complexity.Frontiers in psychiatry · 2026Article
- Article
- The Small Molecule Inhibitor of the Type III Secretion System Fluorothiazinone Affects Flagellum Surface Presentation and Restricts Motility in Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2025Article
- The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.Nature communications · 2025Article
- Curvature Generation and Engineering Principles fromACS nano · 2025Article
- How Does the Archaellum Work?Biomolecules · 2025Review
- Multiple Chaperone DnaK-FliC Flagellin Interactions are Required for Pseudomonas aeruginosa Flagellum Assembly and Indicate a New Function for DnaK.Microbial biotechnology · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Structure and Assembly of theInternational journal of molecular sciences · 2023Article
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial flagellum is a large macromolecular assembly that acts as propeller, providing motility through the rotation of a long extracellular filament. It is composed of over 20 different proteins, many of them highly oligomeric. Accordingly, it has attracted a huge amount of interest amongst researchers and the wider public alike. Nonetheless, most of its molecular details had long remained elusive.This however has changed recently, with the emergence of cryo-EM to determine the structure of protein assemblies at near-atomic resolution. Within a few years, the atomic details of most of the flagellar components have been elucidated, revealing not only its overall architecture but also the molecular details of its rotation mechanism. However, many questions remained unaddressed, notably on the complexity of the assembly of such an intricate machinery.In this chapter, we review the current state of our understanding of the bacterial flagellum structure, focusing on the recent development from cryo-EM. We also highlight the various elements that still remain to be fully characterized. Finally, we summarize the existing model for flagellum assembly and discuss some of the outstanding questions that are still pending in our understanding of the diversity of assembly pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.