ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. 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 Effect of Tannin-Rich Witch Hazel on Growth of ProbioticAntibiotics (Basel, Switzerland) · 2022Article
- whISOBAXAntibiotics (Basel, Switzerland) · 2020Article
- Witch Hazel Significantly Improves the Efficacy of Commercially Available Teat Dips.Pathogens (Basel, Switzerland) · 2020Article
- Heme catabolism in the causative agent of anthrax.Molecular microbiology · 2019Article
- Growth phenotype analysis of heme synthetic enzymes in a halophilic archaeon, Haloferax volcanii.PloS one · 2017Article
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Authors and funding
2 authors.
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Abstract
The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. The structure of TRAP consists of a central eight-stranded β-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit.
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