ArticleImmunogenetics1996
Sequence and characterization of two HSP70 genes in the colonial protochordate Botryllus schlosseri.
Article in Immunogenetics, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed, 15 citations in OpenAlex.
- Botryllus schlosseri allorecognition: tackling the enigma.Developmental and comparative immunology · 2015Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes belonging to the heat shock protein 70 gene family have been cloned from the colonial protochordate Botryllus schlosseri. The two intronless genes (HSP70.1 and HSP70.2) exhibit 93.6% sequence identity within the predicted coding region, and 83.3% and 81.7% sequence identity in the 5' and 3' flanking regions, respectively. The predicted amino acid sequences are 95% identical and contain several signatures characteristic of cytoplasmic eukaryotic HSP70 genes (Gupta et al. 1994; Rensing and Maier 1994). Northern blotting and sequence analysis suggest that both genes are heat-inducible members of the HSP70 gene family. Given these characteristics, HSP70.1 and HSP70.2 appear to be good candidates for protochordate homologues of the major histocompatibility complex-linked HSP70 genes of human, mouse, and rat (Milner and Campbell 1990; Walter et al. 1994). Further experiments to determine whether there is functional evidence for such similarity are in progress.
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