Evidence map›Paper›PMID 39242774›Full record

ArticleEMBO reports2024

Molecular mechanism of β-arrestin-2 pre-activation by phosphatidylinositol 4,5-bisphosphate.

Kiae Kim, Ka Young Chung

Abstract read
In one paragraph

Article in EMBO reports, 2024. 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
–field-weighted citation impact
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.

  1. Review
  2. Intrinsic conformational equilibria position arrestin-2 for activation.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Intrinsic conformational equilibria position arrestin-2 for activation.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  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

2 authors.

Kiae KimSchool of Pharmacy, Sungkyunkwan University, 2066 Seobu-ro, Jangan-gu, Suwon, 16419, Republic of Korea.ORCID 0000-0002-1212-4372
Ka Young ChungSchool of Pharmacy, Sungkyunkwan University, 2066 Seobu-ro, Jangan-gu, Suwon, 16419, Republic of Korea. kychung2@skku.edu.ORCID 0000-0001-9038-9571

Funding

Ministry of Oceans and Fisheries (MOF) 2021633Ministry of Science and ICT, South Korea (MSIT) NRF-2019R1A5A2027340Ministry of Science and ICT, South Korea (MSIT) NRF-2021R1A2C3003518
6 · The paper itself

Abstract

Phosphorylated residues of G protein-coupled receptors bind to the N-domain of arrestin, resulting in the release of its C-terminus. This induces further allosteric conformational changes, such as polar core disruption, alteration of interdomain loops, and domain rotation, which transform arrestins into the receptor-activated state. It is widely accepted that arrestin activation occurs by conformational changes propagated from the N- to the C-domain. However, recent studies have revealed that binding of phosphatidylinositol 4,5-bisphosphate (PIP

Indexed as

beta-Arrestin 2Phosphatidylinositol 4,5-DiphosphateProtein BindingAnimalsHumansHydrogen Deuterium Exchange-Mass SpectrometryModels, MolecularPhosphorylationProtein ConformationProtein DomainsReceptors, Vasopressinbeta-Arrestin 2Phosphatidylinositol 4,5-DiphosphateReceptors, VasopressinArrestinHDX-MSPhosphatidylinositol 4,5-bisphosphateStructure

Identifiers

PMID39242774
PMCPMC11467438

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.