ArticleNucleic acids research2002
Purification and characterization of transcription factor IIIA from Acanthamoeba castellanii.
Article in Nucleic acids research, 2002. 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Identification of EhTIF-IA: The putative E. histolytica orthologue of the human ribosomal RNA transcription initiation factor-IA.Journal of biosciences · 2016Article
- Identification and characterization of transcription factor IIIA and ribosomal protein L5 from Arabidopsis thaliana.Nucleic acids research · 2003Article
- Acanthamoeba spp. as agents of disease in humans.Clinical microbiology reviews · 2003Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
TFIIIA is required to activate RNA polymerase III transcription from 5S RNA genes. Although all known TFIIIA homologs harbor nine zinc fingers that mediate DNA binding, very limited sequence homology is found among these proteins, which reflects unique properties of some TFIIIA homologs. For example, the Acanthamoeba castellanii homolog directly regulates 5S RNA transcription. We have purified and characterized A.castellanii TFIIIA (AcTFIIIA) as a step toward obtaining a clearer understanding of these differences and of the regulatory process. AcTFIIIA is 59 kDa, significantly larger than all other TFIIIA homologs isolated to date. Nevertheless, it exhibits a DNase I footprint very similar to those produced by the smaller vertebrate TFIIIA homologs, but distinct from the smaller footprint of the 51 kDa TFIIIA from Saccharomyces cerevisiae. Similar footprinting is not reflected in greater sequence similarity between the A.castellanii and vertebrate promoters.
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Registered trials
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