ArticleGenetics1992
Size polymorphisms due to changes in the number of O-glycosylated tandem repeats in the Dictyostelium discoideum glycoprotein PsA.
Article in Genetics, 1992. 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, 22 citations in OpenAlex.
- The extracellular matrix of the Dictyostelium discoideum slug.Experientia · 1995Review
- Replacement of the phospholipid-anchor in the contact site A glycoprotein of D. discoideum by a transmembrane region does not impede cell adhesion but reduces residence time on the cell surface.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular weight polymorphism in the Dictyostelium discoideum cell surface glycoprotein PsA is due to incremental copies of an O-glycosylated tandem tetrapeptide repeat. Allelic variation at the pspA locus results in a PsA glycoprotein with three, four or five tandem copies of Pro-Thr-Val-Thr. The simplest explanation for the origin of this polymorphism is an unequal crossing over event in the ancestral gene containing four copies. Each Thr in the tandem repeat is substituted with carbohydrate, which is completely absent from PsA in strains carrying a glycosylation defective modB mutation. Glycosylated tandem repeats appear to be a common feature of cell surface glycoproteins which are characterized by short domains rich in Pro and Thr or Ser. It is probable that the glycosylated repeat domain acts as a "spacer" peptide that projects the globular domain above the glycocalyx.
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