Evidence map›Paper›PMID 10318897›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.

Y J Sun, C C Chou, W S Chen, R T Wu, M Meng, C D Hsiao

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 111 citations in OpenAlex.

  1. Duplicate entries in the Protein Data Bank: how to detect and handle them.Acta crystallographica. Section D, Structural biology · 2025
    Article
  2. Article
  3. Targeting Energy Metabolism in Cancer Treatment.International journal of molecular sciences · 2022
    Review
  4. The Metabolite Saccharopine Impairs Neuronal Development by Inhibiting the Neurotrophic Function of Glucose-6-Phosphate Isomerase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  5. Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  13. Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  14. Article
  15. Review
  16. Review
  17. Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  18. Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007
    Article
  19. Tumor metabolism: new opportunities for cancer therapy.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2006
    Review
  20. Review
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

6 authors at 1 institution in 1 country.

Y J SunInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, Republic of China.
C C Chou
W S Chen
R T Wu
M Meng
C D Hsiao
Institute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alpha/beta structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCrystallography, X-RayEpidermal Growth FactorGeobacillus stearothermophilusGlucose-6-Phosphate IsomeraseMiceModels, MolecularMolecular Sequence DataProtein Structure, SecondaryRatsRats, Sprague-DawleySequence AlignmentStatic ElectricityTumor Cells, CulturedEpidermal Growth FactorGlucose-6-Phosphate Isomerase

Identifiers

PMID10318897
PMCPMC21873
OpenAlexW2123411433

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.