Evidence map›Paper›PMID 29335412›Full record

ArticleNature communications2018

Phosphorylation-induced conformation of β

Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, Shunsuke Imai, Kunio Nakata, Toshimi Mizukoshi, Takumi Ueda, Hideo Iwaï, Ichio Shimada

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 82 citations in OpenAlex.

  1. AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026
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  10. Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

9 authors at 4 institutions in 2 countries.

Yutaro ShiraishiGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.
Mei NatsumeGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.
Yutaka KofukuGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.
Shunsuke ImaiGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.
Kunio NakataInstitute for Innovation, Ajinomoto Co., Inc, Kawasaki, 210-8681, Japan.
Toshimi MizukoshiInstitute for Innovation, Ajinomoto Co., Inc, Kawasaki, 210-8681, Japan.
Takumi UedaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0001-9677-0912
Hideo IwaïResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, 00014, Helsinki, Finland.ORCID http://orcid.org/0000-0001-7376-5264
Ichio ShimadaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan. shimada@iw-nmr.f.u-tokyo.ac.jp.
The University of Tokyo · JPAjinomoto (Japan) · JPJapan Science and Technology Agency · JPUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminal region of G-protein-coupled receptors (GPCRs), stimulated by agonist binding, is phosphorylated by GPCR kinases, and the phosphorylated GPCRs bind to arrestin, leading to the cellular responses. To understand the mechanism underlying the formation of the phosphorylated GPCR-arrestin complex, we performed NMR analyses of the phosphorylated β

Indexed as

beta-Arrestin 1Cell MembraneHumansMagnetic Resonance SpectroscopyModels, MolecularPhosphorylationProtein BindingProtein ConformationProtein DomainsReceptors, Adrenergic, beta-2beta-Arrestin 1Receptors, Adrenergic, beta-2

Identifiers

PMID29335412
PMCPMC5768704
OpenAlexW2782557575

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.