Evidence map›Paper›PMID 29490249›Full record

ArticleBiophysical journal2018

Lipid-Protein Interplay in Dimerization of Juxtamembrane Domains of Epidermal Growth Factor Receptor.

Ryo Maeda, Takeshi Sato, Kenji Okamoto, Masataka Yanagawa, Yasushi Sako

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

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  9. Thermodynamic analysis of the GASBiophysical journal · 2023
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  10. Article
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  12. Review
  13. Review
  14. Review
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  19. Review
  20. Review
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

5 authors at 2 institutions in 1 country.

Ryo MaedaCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, Japan.
Takeshi SatoKyoto Pharmaceutical University, 5, Misasagi-cho, Yamashina-ku, Kyoto-shi, Kyoto, Japan; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, Japan.
Kenji OkamotoCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, Japan.
Masataka YanagawaCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, Japan.
Yasushi SakoCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, Japan. Electronic address: sako@riken.jp.
RIKEN Advanced Science Institute · JPKyoto Pharmaceutical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane (TM) helix and juxtamembrane (JM) domains (TM-JM) bridge the extracellular and intracellular domains of single-pass membrane proteins, including epidermal growth factor receptor (EGFR). TM-JM dimerization plays a crucial role in regulation of EGFR kinase activity at the cytoplasmic side. Although the interaction of JM with membrane lipids is thought to be important to turn on EGF signaling, and phosphorylation of Thr654 on JM leads to desensitization, the underlying kinetic mechanisms remain unclear. In particular, how Thr654 phosphorylation regulates EGFR activity is largely unknown. Here, combining single-pair FRET imaging and nanodisc techniques, we showed that phosphatidylinositol 4,5-bis phosphate (PIP

Indexed as

Bayes TheoremBinding SitesCell MembraneDimerizationErbB ReceptorsHumansMembrane LipidsModels, MolecularPhosphatidylinositolsPhosphorylationProtein BindingProtein DomainsSignal TransductionThreonineEGFR protein, humanErbB ReceptorsMembrane LipidsPhosphatidylinositolsThreonine

Identifiers

PMID29490249
PMCPMC5984969
OpenAlexW2766352488

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.