Evidence map›Paper›PMID 11313904›Full record

ReviewOncogene2001

Protease activated receptors: theme and variations.

P J O'Brien, M Molino, M Kahn, L F Brass

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 218 citations in OpenAlex.

  1. 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
  2. Review
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  10. Using PAR4 Inhibition as an Anti-Thrombotic Approach: Why, How, and When?International journal of molecular sciences · 2019
    Review
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  12. Review
  13. Article
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  16. Article
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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

4 authors at 1 institution in 1 country.

P J O'BrienDepartment of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
M Molino
M Kahn
L F Brass
University of Pennsylvania · US

Funding

Subcellular Mechanisms pf Platelet ActivationP01HL040387 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI BENNETT, JOEL S. · 1988 to 2018
$35.5M
NHLBI NIH HHS HL40387
6 · The paper itself

Abstract

The four PAR family members are G protein coupled receptors that are normally activated by proteolytic exposure of an occult tethered ligand. Three of the family members are thrombin receptors. The fourth (PAR2) is not activated by thrombin, but can be activated by other proteases, including trypsin, tryptase and Factor Xa. This review focuses on recent information about the manner in which signaling through these receptors is initiated and terminated, including evidence for inter- as well as intramolecular modes of activation, and continuing efforts to identify additional, biologically-relevant proteases that can activate PAR family members.

Indexed as

Signal TransductionAmino Acid SequenceBinding SitesEndopeptidasesGTP-Binding ProteinsModels, BiologicalMolecular Sequence DataReceptor, PAR-2Receptors, ThrombinEndopeptidasesGTP-Binding ProteinsReceptor, PAR-2Receptors, Thrombin

Identifiers

PMID11313904
OpenAlexW2314664886

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.