ArticleScience advances2025
Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogen
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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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Who cites it
5 citing papers in PubMed.
- The Tol-Pal System Promotes Pseudoiodinine Production by Enhancing Bacterial Growth inMicroorganisms · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Cryo-EM SPR structures of Salmonella typhimurium ArnC; the key enzyme in lipid-A modification conferring polymyxin resistance.Protein science : a publication of the Protein Society · 2025Article
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10 authors.
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Abstract
Gram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold cell envelope integrity, an indispensable aspect for both division and survival. The IM TolQ-TolR complex is the essential part of the Tol-Pal system, serving as a conduit for PMF energy transfer to the outer membrane. Here we present cryo-electron microscopy reconstructions of
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