Evidence map›Paper›PMID 24990072›Full record

ArticleThrombosis and haemostasis2014

Thrombin-induced platelet activation via PAR4: pivotal role for exosite II.

N Boknäs, L Faxälv, D Sanchez Centellas, M Wallstedt, S Ramström, M Grenegård, T L Lindahl

Open access · bronzeAbstract read
In one paragraph

Article in Thrombosis and haemostasis, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. 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
  3. Article
  4. Observational
  5. Article
  6. Arteriosclerosis, thrombosis, and vascular biology · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

7 authors at 2 institutions in 1 country.

N Boknäs
L Faxälv
D Sanchez Centellas
M Wallstedt
S Ramström
M Grenegård
T L LindahlTomas Lindahl, Department of Clinical and Experimental Medicine, Linköping University, SE-51885 Linköping, Sweden, Tel.: +46 101033227, Fax: +46 101033240, E-mail: tomas.lindahl@liu.se.
Linköping University · SEÖrebro University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thrombin-induced platelet activation via PAR1 and PAR4 is an important event in haemostasis. Although the underlying mechanisms responsible for ensuring efficient PAR1 activation by thrombin have been extensively studied, the potential involvement of recognitions sites outside the active site of the protease in thrombin-induced PAR4 activation is largely unknown. In this study, we developed a new assay to assess the importance of exosite I and II for PAR4 activation with α - and γ-thrombin. Surprisingly, we found that exosite II is critical for activation of PAR4. We also show that this dependency on exosite II likely represents a new mechanism, as it is unaffected by blockage of the previously known interaction between thrombin and glycoprotein Ibα.

Indexed as

HemostasisAptamers, NucleotideBlood PlateletsCalcium SignalingCatalytic DomainCells, CulturedHeparinHumansPlatelet ActivationPlatelet Glycoprotein GPIb-IX ComplexProtein BindingReceptor, PAR-1Receptors, ThrombinThrombinAptamers, NucleotideHeparinPlatelet Glycoprotein GPIb-IX Complexprotease-activated receptor 4Receptor, PAR-1Receptors, ThrombinThrombin

Identifiers

PMID24990072
PMCPMC6374991
OpenAlexW2089277302

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.