ArticleBiochemistry2022
Interdomain Linkers Regulate Histidine Kinase Activity by Controlling Subunit Interactions.
Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Chemotaxis kinase CheA is regulated by modulating interdomain interactions.Biophysical journal · 2026Article
- Electrically silent mutants unravel the mechanism of binding-gating coupling in Cys-loop receptors.Science advances · 2024Article
- Structural Evolution of Bacterial Polyphosphate Degradation Enzyme for Phosphorus Cycling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial chemoreceptors regulate the cytosolic multidomain histidine kinase CheA through largely unknown mechanisms. Residue substitutions in the peptide linkers that connect the P4 kinase domain to the P3 dimerization and P5 regulatory domain affect CheA basal activity and activation. To understand the role that these linkers play in CheA activity, the P3-to-P4 linker (L3) and P4-to-P5 linker (L4) were extended and altered in variants of
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Registered trials
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