Evidence map›Paper›PMID 22212680›Full record

ReviewNature reviews. Drug discovery2012

Targeting proteinase-activated receptors: therapeutic potential and challenges.

Rithwik Ramachandran, Farshid Noorbakhsh, Kathryn Defea, Morley D Hollenberg

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed, 1 pooled it
19.4field-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

159 citing papers in PubMed, 1 synthesis or guideline pooled it, 306 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. 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
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99 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

4 authors at 3 institutions in 3 countries.

Rithwik RamachandranDepartment of Physiology and Pharmacology, Faculty of Medicine, University of Calgary, Alberta T2N 4N1, Canada. rramacha@ucalgary.ca
Farshid Noorbakhsh
Kathryn Defea
Morley D Hollenberg
University of Calgary · CATehran University of Medical Sciences · IRUniversity of California, Riverside · US

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Proteinase-activated receptors (PARs), a family of four seven-transmembrane G protein-coupled receptors, act as targets for signalling by various proteolytic enzymes. PARs are characterized by a unique activation mechanism involving the proteolytic unmasking of a tethered ligand that stimulates the receptor. Given the emerging roles of these receptors in cancer as well as in disorders of the cardiovascular, musculoskeletal, gastrointestinal, respiratory and central nervous system, PARs have become attractive targets for the development of novel therapeutics. In this Review we summarize the mechanisms by which PARs modulate cell function and the roles they can have in physiology and diseases. Furthermore, we provide an overview of possible strategies for developing PAR antagonists.

Indexed as

AnimalsDrug Delivery SystemsGuanidinesHumansNeoplasmsOligopeptidesPharmaceutical PreparationsReceptors, Proteinase-ActivatedGuanidinesN-cinnamoyl-4-fluorophenylalanyl-4-guanidinophenylalanyl-leucyl-arginyl-argininamideOligopeptidesPharmaceutical PreparationsReceptors, Proteinase-Activated

Identifiers

PMID22212680
OpenAlexW2085176272

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.