Evidence map›Paper›PMID 21438117›Full record

ReviewIUBMB life2011

Regulation of protease-activated receptor signaling by post-translational modifications.

Neil Grimsey, Antonio G Soto, JoAnn Trejo

Open access · bronzeAbstract readReview
In one paragraph

Review in IUBMB life, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. UsingFrontiers in cell and developmental biology · 2021
    Review
  2. Edema Induced by aInternational journal of molecular sciences · 2018
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. New insights into modulation of thrombin formation.Current atherosclerosis reports · 2013
    Review
  8. Review
  9. 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

3 authors at 1 institution in 1 country.

Neil GrimseyDepartment of Pharmacology, School of Medicine, University of California, San Diego, CA 92093-0636, USA.
Antonio G Soto
JoAnn Trejo
University of California, San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Regulation of Protease-activated Receptor-1 SignalingR01HL073328 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TREJO, JOANN · 2004 to 2012
$3.6M
Mechanisms Regulating GPCR TraffickingR01GM090689 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TREJO, JOANN · 2010 to 2018
$2.9M
NHLBI NIH HHS HL073328NHLBI NIH HHS R01 HL073328NIGMS NIH HHS GM090689NIGMS NIH HHS R01 GM090689NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

Protease-activated receptors (PARs) are a unique family of G-protein-coupled receptors (GPCRs) that are irreversibly activated following proteolytic cleavage of their extracellular N-terminus. PARs play critical functions in hemostasis, thrombosis, inflammation, embryonic development, and cancer progression. Because of the irreversible proteolytic nature of PAR activation, signaling by the receptors is tightly regulated. Three distinct processes including desensitization, internalization, and lysosomal degradation, regulate the temporal and spatial aspects of activated PAR signaling. Post-translational modifications play a critical role in regulating each of these processes and here we review the nature of PAR post-translational modifications and their importance in signal regulation. The PARs are activated by numerous proteases, and some can elicit distinct cellular responses, how this biased agonism is determined is unknown. Further study of the function of post-translational modifications of the PARs will lead to a greater understanding of the physiological regulation of baised agonism and how PAR signaling is precisely controlled in different cellular contexts.

Indexed as

Protein Processing, Post-TranslationalModels, BiologicalProtein IsoformsReceptors, Proteinase-ActivatedSignal TransductionProtein IsoformsReceptors, Proteinase-Activated

Identifiers

PMID21438117
PMCPMC3121918
OpenAlexW2069561320

What OpenQuestion holds

Textmetadata
LicenceTDM
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.