Evidence map›Paper›PMID 8643551›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor.

H W Sun, J Bernhagen, R Bucala, E Lolis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
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

129 citing papers in PubMed, 330 citations in OpenAlex.

  1. Trial
  2. Article
  3. Crystal structure of Plasmodium vivax macrophage migration inhibitory factor.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

69 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

4 authors at 1 institution in 1 country.

H W SunDepartment of Pharmacology, Yale University, New Haven, CT 06510, USA.
J Bernhagen
R Bucala
E Lolis
Yale University · US

Funding

MIF AND PARASITIC DISEASESR01AI035931 · NIAID · PICOWER INSTITUTE FOR MEDICAL RESEARCH · PI BUCALA, RICHARD J · 1994 to 1997
–
NIAID NIH HHS AI35931PHS HHS PDB/1MIF
6 · The paper itself

Abstract

Macrophage migration inhibitory factor (MIF) was the first cytokine to be described, but for 30 years its role in the immune response remained enigmatic. In recent studies, MIF has been found to be a novel pituitary hormone and the first protein identified to be released from immune cells on glucocorticoid stimulation. Once secreted, MIF counterregulates the immunosuppressive effects of steroids and thus acts as a critical component of the immune system to control both local and systemic immune responses. We report herein the x-ray crystal structure of human MIF to 2.6 angstrom resolution. The protein is a trimer of identical subunits. Each monomer contains two antiparallel alpha-helices that pack against a four-stranded beta-sheet. The monomer has an additional two beta-strands that interact with the beta-sheets of adjacent subunits to form the interface between monomers. The three beta-sheets are arranged to form a barrel containing a solvent-accessible channel that runs through the center of the protein along a molecular 3-fold axis. Electrostatic potential maps reveal that the channel has a positive potential, suggesting that it binds negatively charged molecules. The elucidated structure for MIF is unique among cytokines or hormonal mediators, and suggests that this counterregulator of glucocorticoid action participates in novel ligand-receptor interactions.

Indexed as

Protein Structure, SecondaryAmino Acid SequenceComputer GraphicsCrystallography, X-RayEscherichia coliHumansMacromolecular SubstancesMacrophage Migration-Inhibitory FactorsModels, MolecularModels, StructuralMolecular Sequence DataRecombinant ProteinsMacromolecular SubstancesMacrophage Migration-Inhibitory FactorsRecombinant Proteins

Identifiers

PMID8643551
PMCPMC39220
OpenAlexW2026192283

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.