Evidence map›Paper›PMID 15733055›Full record

ArticleThe Biochemical journal2005

Sphingosine 1-phosphate analogue recognition and selectivity at S1P4 within the endothelial differentiation gene family of receptors.

Yuichi Inagaki, Trucchi T Pham, Yuko Fujiwara, Takayuki Kohno, Daniel A Osborne, Yasuyuki Igarashi, Gabor Tigyi, Abby L Parrill

Abstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Lysophospholipid interactions with protein targets.Biochimica et biophysica acta · 2008
    Review
  15. Article
  16. Molecular recognition in the sphingosine 1-phosphate receptor family.Journal of molecular graphics & modelling · 2008
    Article
  17. Article
  18. 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

8 authors.

Yuichi InagakiDepartment of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Trucchi T Pham
Yuko Fujiwara
Takayuki Kohno
Daniel A Osborne
Yasuyuki Igarashi
Gabor Tigyi
Abby L Parrill

Funding

Ligand Recognition by Phospholipid Growth Factor ReceptorsR01CA092160 · NCI · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI TIGYI, GABOR J · 2001 to 2022
$5.9M
NCI NIH HHS 1 R01 CA92160-01NCI NIH HHS R01 CA092160
6 · The paper itself

Abstract

Synergistic computational and experimental studies provided previously unforeseen details concerning the structural basis of S1P (sphingosine 1-phosphate) recognition by the S1P4 G-protein-coupled receptor. Similarly to reports on the S1P1 receptor, cationic and anionic residues in the third transmembrane domain (R3.28 and E3.29 at positions 124 and 125) form ion pairs with the phosphate and ammonium of S1P, and alanine mutations at these positions abolished specific S1P binding, S1P-induced receptor activation and cell migration. Unlike findings on the S1P1 receptor, no cationic residue in the seventh transmembrane domain interacts with the phosphate. Additionally, two previously undiscovered interactions with the S1P polar headgroup have been identified. Trp186 at position 4.64 in the fourth transmembrane domain interacts by a cation-pi interaction with the ammonium group of S1P. Lys204 at position 5.38 forms an ion pair with the S1P. The S1P4 and S1P1 receptors show differences in binding-pocket shape and electrostatic distributions that correlate with the published structure-activity relationships. In particular, the binding pocket of mS1P4 (mouse S1P4) has recognition sites for the anionic phosphate and cationic ammonium groups that are equidistant from the end of the non-polar tail. In contrast, the binding pocket of hS1P1 (human S1P4) places the ammonium recognition site 2 A (1 A=0.1 nm) closer to the end of the non-polar tail than the phosphate recognition site.

Indexed as

Multigene FamilyAmino Acid SequenceAnimalsBinding SitesCell LineCell MembraneCell MovementCricetinaeEndothelial CellsHumansLigandsLysophospholipidsMiceMolecular StructureMutationReceptors, Lysosphingolipiddihydrosphingosine 1-phosphateLigandsLysophospholipidsphytosphingosine-1-phosphateReceptors, LysosphingolipidSphingosinesphingosine 1-phosphate

Identifiers

PMID15733055
PMCPMC1184551

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.