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Article

Novel insights into the mechanism of well-ordered assembly of bacterial flagellar proteins in Salmonella.

Scientific reports - 29 Jan 2018

Inoue Yumi, Morimoto Yusuke V, Namba Keiichi, Minamino Tohru

Abstract excerpt

The FliI ATPase of the flagellar type III protein export apparatus forms the FliH2FliI complex along with its regulator FliH. The FliH2FliI complex is postulated to bring export substrates from the cytoplasm to the docking platform made of FlhA and FlhB although not essential for flagellar protein export. Here, to clarify the role of the FliH2FliI complex in flagellar assembly, we analysed the effect of FliH and...

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Source

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Identifiers

PMID: 29379125
DOI: 10.1038/s41598-018-20209-3
PMCID: PMC5789064

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Novel insights into the mechanism of well-ordered assembly of bacterial flagellar proteins in Salmonella.PMID 29379125Read ↗

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Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.Semantic proximity Read ↗

Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus.Semantic proximity Read ↗

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