Evidence map›Paper›PMID 31892516›Full record

ArticleThe Journal of biological chemistry2020

Molecular basis for activation and biased signaling at the thrombin-activated GPCR proteinase activated receptor-4 (PAR4).

Pierre E Thibeault, Jordan C LeSarge, D'Arcy Arends, Michaela Fernandes, Peter Chidiac, Peter B Stathopulos, Leonard G Luyt, Rithwik Ramachandran

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Species Differences in Platelet Protease-Activated Receptors.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Protease-activated receptors: An illustrated review.Research and practice in thrombosis and haemostasis · 2021
    Review
  16. Review
  17. Article
  18. 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 at 1 institution in 1 country.

Pierre E ThibeaultDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario N6A5C1, Canada.
Jordan C LeSargeDepartment of Chemistry, University of Western Ontario, London, Ontario N6A5C1, Canada.
D'Arcy ArendsDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario N6A5C1, Canada.
Michaela FernandesDepartment of Chemistry, University of Western Ontario, London, Ontario N6A5C1, Canada.
Peter ChidiacDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario N6A5C1, Canada.
Peter B StathopulosDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario N6A5C1, Canada.
Leonard G LuytDepartment of Chemistry, University of Western Ontario, London, Ontario N6A5C1, Canada; Department of Oncology, University of Western Ontario, London, Ontario N6A5C1, Canada; London Regional Cancer Program, Lawson Health Research Institute, London, Ontario N6C2R5, Canada.
Rithwik RamachandranDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario N6A5C1, Canada. Electronic address: rramach@uwo.ca.
Western University · CA

Funding

CIHR 376560
6 · The paper itself

Abstract

Proteinase-activated receptor (PAR)-4 is a member of the proteolytically-activated PAR family of G-protein-coupled receptors (GPCR) that represents an important target in the development of anti-platelet therapeutics. PARs are activated by proteolytic cleavage of their receptor N terminus by enzymes such as thrombin, trypsin, and cathepsin-G. This reveals the receptor-activating motif, termed the tethered ligand that binds intramolecularly to the receptor and triggers signaling. However, PARs are also activated by exogenous application of synthetic peptides derived from the tethered-ligand sequence. To better understand the molecular basis for PAR4-dependent signaling, we examined PAR4-signaling responses to a peptide library derived from the canonical PAR4-agonist peptide, AYPGKF-NH

Indexed as

Signal TransductionAlanineAmino Acid Substitutionbeta-ArrestinsCalciumCalcium SignalingGTP-Binding Protein alpha Subunits, Gq-G11HEK293 CellsHumansIsomerismMAP Kinase Signaling SystemMethylationMolecular Docking SimulationMutant ProteinsMutationPeptidesAlaninebeta-ArrestinsCalciumGTP-Binding Protein alpha Subunits, Gq-G11Mutant ProteinsPeptidesprotease-activated receptor 4Receptors, ThrombinThrombinarrestinbiased signalingbioluminescencebioluminescence resonance energy transfer (BRET)dockingG-proteinG-protein–coupled receptor (GPCR)mitogen-activated protein kinase (MAPK)peptideplateletprotease-activated receptor-4 (PAR4)

Identifiers

PMID31892516
PMCPMC7039573
OpenAlexW2997037077

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.