Evidence map›Paper›PMID 9618465›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Cloning and characterization of human protease-activated receptor 4.

W F Xu, H Andersen, T E Whitmore, S R Presnell, D P Yee, A Ching, T Gilbert, E W Davie, D C Foster

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 222 papers.

0numbers the graph read from it
0cells of the map it votes in
222citing papers in PubMed
27.8field-weighted citation impact, top 1% 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

222 citing papers in PubMed, 814 citations in OpenAlex.

  1. Review
  2. Article
  3. The Structural Analogy of MASP-2 with Thrombin and MASP-1 Reveals Strong Binding with PAR4.Anti-inflammatory & anti-allergy agents in medicinal chemistry · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Endothelial protease-activated receptor 4: impotent or important?Frontiers in cardiovascular medicine · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. PAR2: The Cornerstone of Pancreatic Diseases.Physiological research · 2022
    Review
  19. Article
  20. Diversification of PAR signaling through receptor crosstalk.Cellular & molecular biology letters · 2022
    Review

162 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

9 authors at 1 institution in 1 country.

W F XuDepartment of Biochemistry, University of Washington, Box 357350, Seattle, WA 98195-7350, USA.
H Andersen
T E Whitmore
S R Presnell
D P Yee
A Ching
T Gilbert
E W Davie
D C Foster
University of Washington · US

Funding

THE STRUCTURE/FUNCTION RELATIONSHIPS OF HUMAN FACTOR VIIIR01HL016919 · NHLBI · UNIVERSITY OF WASHINGTON · PI DAVIE, EARL W · 1985 to 2006
$4.5M
NHLBI NIH HHS HL16919NHLBI NIH HHS R01 HL016919
6 · The paper itself

Abstract

Protease-activated receptors 1-3 (PAR1, PAR2, and PAR3) are members of a unique G protein-coupled receptor family. They are characterized by a tethered peptide ligand at the extracellular amino terminus that is generated by minor proteolysis. A partial cDNA sequence of a fourth member of this family (PAR4) was identified in an expressed sequence tag database, and the full-length cDNA clone has been isolated from a lymphoma Daudi cell cDNA library. The ORF codes for a seven transmembrane domain protein of 385 amino acids with 33% amino acid sequence identity with PAR1, PAR2, and PAR3. A putative protease cleavage site (Arg-47/Gly-48) was identified within the extracellular amino terminus. COS cells transiently transfected with PAR4 resulted in the formation of intracellular inositol triphosphate when treated with either thrombin or trypsin. A PAR4 mutant in which the Arg-47 was replaced with Ala did not respond to thrombin or trypsin. A hexapeptide (GYPGQV) representing the newly exposed tethered ligand from the amino terminus of PAR4 after proteolysis by thrombin activated COS cells transfected with either wild-type or the mutant PAR4. Northern blot showed that PAR4 mRNA was expressed in a number of human tissues, with high levels being present in lung, pancreas, thyroid, testis, and small intestine. By fluorescence in situ hybridization, the human PAR4 gene was mapped to chromosome 19p12.

Indexed as

Amino Acid SequenceBase SequenceCloning, MolecularHumansInositol 1,4,5-TrisphosphateMolecular Sequence DataMutationReceptors, Cell SurfaceReceptors, ThrombinSequence AnalysisTransfectionInositol 1,4,5-Trisphosphateprotease-activated receptor 4Receptors, Cell SurfaceReceptors, Thrombin

Identifiers

PMID9618465
PMCPMC22580
OpenAlexW1964499190

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.