Evidence map›Paper›PMID 2169613›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1990

Structural design and molecular evolution of a cytokine receptor superfamily.

J F Bazan

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 398 papers.

0numbers the graph read from it
0cells of the map it votes in
398citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

398 citing papers in PubMed.

  1. Biomarkers of Cardiovascular Stress: A Historical Review.Journal of cardiovascular development and disease · 2026
    Review
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  9. The JAK-STAT pathway: from structural biology to cytokine engineering.Signal transduction and targeted therapy · 2024
    Review
  10. Article
  11. Article
  12. Molecular Engineering of Interleukin-2 for Enhanced Therapeutic Activity in Autoimmune Diseases.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024
    Review
  13. Review
  14. Strategies to therapeutically modulate cytokine action.Nature reviews. Drug discovery · 2023
    Review
  15. Review
  16. Article
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  18. Article
  19. Review
  20. Article

338 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

J F BazanDepartment of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A family of cytokine receptors comprising molecules specific for a diverse group of hematopoietic factors and growth hormones has been principally defined by a striking homology of binding domains. This work proposes that the approximately 200-residue binding segment of the canonical cytokine receptor is composed of two discrete folding domains that share a significant sequence and structural resemblance. Analogous motifs are found in tandem approximately 100-amino acid domains in the extracellular segments of a receptor family formed by the interferon-alpha/beta and -gamma receptors and tissue factor, a membrane tether for a coagulation protease. Domains from the receptor supergroup reveal clear evolutionary links to fibronectin type III structures, approximately 90-amino acid modules that are typically found in cell surface molecules with adhesive functions. Predictive structural analysis of the shared receptor and fibronectin domains locates seven beta-strands in conserved regions of the chain; these strands are modeled to fold into antiparallel beta-sandwiches with a topology that is similar to immunoglobulin constant domains. These findings have strong implications for understanding the evolutionary emergence of an important class of regulatory molecules from primitive adhesive modules. In addition, the resulting double-barrel design of the receptors and the spatial clustering of conserved residues suggest a likely binding site for cytokine ligands.

Indexed as

Biological EvolutionMultigene FamilyAmino Acid SequenceAnimalsBiological FactorsCytokinesHumansMiceMolecular Sequence DataProtein ConformationReceptors, Cell SurfaceSequence Homology, Nucleic AcidBiological FactorsCytokinesReceptors, Cell Surface

Identifiers

PMID2169613
PMCPMC54656

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.