ArticleFEBS open bio2012
Formation of MgF3 (-)-dependent complexes between an AAA(+) ATPase and σ(54.).
Article in FEBS open bio, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 7 citations in OpenAlex.
- Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases.Biomolecules · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Mutations in RNA Polymerase Bridge Helix and Switch Regions Affect Active-Site Networks and Transcript-Assisted Hydrolysis.Journal of molecular biology · 2015Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The widely distributed bacterial σ(54)-dependent transcription regulates pathogenicity and numerous adaptive responses in diverse bacteria. Formation of the σ(54)-dependent open promoter complex is a multi-step process driven by AAA(+) ATPases. Non-hydrolysable nucleotide analogues are particularly suitable for studying such complexity by capturing various intermediate states along the energy coupling pathway. Here we report a novel ATP analogue, ADP-MgF3 (-), which traps an AAA(+) ATPase with its target σ(54). The MgF3 (-)-dependent complex is highly homogeneous and functional assays suggest it may represent an early transcription intermediate state valuable for structural studies.
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Registered trials
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