Evidence map›Paper›PMID 16046623›Full record

ArticleProtein science : a publication of the Protein Society2005

Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.

Tomi T Airenne, Yvonne Nymalm, Heidi Kidron, David J Smith, Marjo Pihlavisto, Marko Salmi, Sirpa Jalkanen, Mark S Johnson, Tiina A Salminen

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. The role of VAP-1 in cardiovascular disease: a review.Frontiers in cardiovascular medicine · 2025
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Copper active sites in biology.Chemical reviews · 2014
    Review
  9. Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Vascular adhesion protein 1 in the eye.Journal of ophthalmology · 2013
    Article
  17. Article
  18. The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  19. Article
  20. Article
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

9 authors at 3 institutions in 1 country.

Tomi T AirenneDepartment of Biochemistry and Pharmacy, Abo Akademi University, FIN-20520 Turku, Finland.
Yvonne Nymalm
Heidi Kidron
David J Smith
Marjo Pihlavisto
Marko Salmi
Sirpa Jalkanen
Mark S Johnson
Tiina A Salminen
Åbo Akademi University · FITurku Centre for Biotechnology · FIUniversity of Turku · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The expression of human vascular adhesion protein-1 (hVAP-1) is induced at sites of inflammation where extravasation of lymphocytes from blood to the peripheral tissue occurs. We have solved the X-ray structure of hVAP-1, a human copper amine oxidase (CAO), which is distinguished from other CAOs in being membrane-bound. The dimer structure reveals some intriguing features that may have fundamental roles in the adhesive and enzymatic functions of hVAP-1, especially regarding the role of hVAP-1 in inflammation, lymphocyte attachment, and signaling. Firstly, Leu469 at the substrate channel may play a key role in controlling the substrate entry; depending on its conformation, it either blocks or gives access to the active site. Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites. Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization. Thirdly, the existence of a solvent-exposed RGD motif at the entrance to each active site in hVAP-1 suggests that it may have a functional role.

Indexed as

Models, MolecularAmine Oxidase (Copper-Containing)Amino Acid SequenceBinding SitesCell Adhesion MoleculesCrystallography, X-RayDimerizationGlycosylationHumansMolecular Sequence DataProtein Structure, TertiaryAmine Oxidase (Copper-Containing)AOC3 protein, humanCell Adhesion Molecules

Identifiers

PMID16046623
PMCPMC2279308
OpenAlexW2146738740

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.