ArticleThe Biochemical journal1995
Expression and DNA binding of the human 52 kDa Ro/SSA autoantigen.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- SS-56, a novel cellular target of autoantibody responses in Sjögren syndrome and systemic lupus erythematosus.The Journal of clinical investigation · 2001Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 52 kDa Ro/SSA protein is an intracellular autoantigen that is frequently recognized by antibodies in sera of patients with systemic lupus erythematosus or Sjogren's syndrome. While the function of this molecule is not known, zinc finger and leucine zipper motifs have been identified in its predicted amino acid sequence which suggest that it may interact with nucleic acids. To test this hypothesis, the human gene which encodes this protein was cloned in a baculovirus and expressed in Spodoptera frugipoda cells. Extracts from these infected insect cells were used as a source of protein for this study. The protein is similar in size and antigenicity to that expressed in human cells. This protein binds to DNA at physiological temperature and is eluted with high concentrations of sodium chloride. Striking similarities were found between the sequence in, and adjacent to, the nucleic acid-binding motifs of 52 kDa Ro/SSA and a growing family of zinc finger proteins which have been shown to bind to DNA or regulate gene expression. The findings presented here place this protein structurally and functionally in this family and demonstrate a biochemical assay which can be used to study its function.
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Registered trials
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