ArticleJournal of bacteriology2004
Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- Article
- Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway.Journal of bacteriology · 2013Article
- The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers.Journal of bacteriology · 2011Article
- Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains.Journal of bacteriology · 2011Article
- Mapping the interactions between Escherichia coli TolQ transmembrane segments.The Journal of biological chemistry · 2011Article
- Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore.Journal of bacteriology · 2011Article
- Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB.Molecular microbiology · 2009Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.
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Registered trials
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