Evidence map›Paper›PMID 25948169›Full record

ArticleGlycoconjugate journal2015

Each GPI-anchored protein species forms a specific lipid raft depending on its GPI attachment signal.

Arisa Miyagawa-Yamaguchi, Norihiro Kotani, Koichi Honke

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Distinct nanoscale membrane organizations of mucins andbioRxiv : the preprint server for biology · 2026
    Article
  3. Elucidation of Ganglioside Microdomains Using Proximity Labeling.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Review
  5. Review
  6. Major Surface Antigens in ZoonoticPathogens (Basel, Switzerland) · 2022
    Review
  7. Article
  8. Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Glycosylphosphatidylinositol-Anchored Proteins inFrontiers in plant science · 2019
    Review
  13. Review
  14. Proximity-dependent labeling methods for proteomic profiling in living cells.Wiley interdisciplinary reviews. Developmental biology · 2017
    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

3 authors at 2 institutions in 1 country.

Arisa Miyagawa-YamaguchiCenter for Innovate and Translational Medicine, Kochi University Medical School, Nankoku, Kochi, 783-8505, Japan.
Norihiro KotaniDepartment of Biochemistry, Saitama Medical University, Iruma-gun, Saitama, 350-0495, Japan.
Koichi HonkeCenter for Innovate and Translational Medicine, Kochi University Medical School, Nankoku, Kochi, 783-8505, Japan. khonke@kochi-u.ac.jp.
Kōchi University · JPSaitama Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported a method, termed enzyme-mediated activation of radical sources (EMARS) for analysis of co-clustered molecules with horseradish peroxidase (HRP) fusion proteins expressed in living cells. This method is featured by radical formation of labeling reagents by HRP. In the current study, we have employed another labeling reagent, fluorescein-conjugated tyramide (FT) instead of the original arylazide compounds. Although hydrogen peroxide is required for the activation of FT, the labeling efficiency by HRP and the nonspecific reactions by endogenous enzyme(s) have been dramatically improved compared with the original fluorescein arylazide. This revised EMARS method has enabled visualization of co-clustered molecules in the endoplasmic reticulum and Golgi membranes with confocal microscopy. By using this method, we have found that GPI-anchored proteins, decay accelerating factor (DAF) and Thy-1 are exclusively co-clustered with HRP-DAFGPI and HRP-Thy1GPI, in which GPI attachment signals of DAF and Thy-1 have been connected to HRP, respectively. Furthermore, the N-glycosylation types of DAF and Thy-1 have been found to correspond to those of HRP-DAFGPI and HRP-Thy1GPI, respectively. These results indicate that each GPI-anchored protein species forms a specific lipid raft depending on its GPI attachment signal, and that the EMARS method can segregate individual lipid rafts.

Indexed as

AnimalsCD55 AntigensCell LineCell MembraneEndoplasmic ReticulumFluoresceinGlycosylationGolgi ApparatusHorseradish PeroxidaseMembrane MicrodomainsMembrane ProteinsCD55 AntigensFluoresceinHorseradish PeroxidaseMembrane ProteinsEMARSFluorescein tyramideHRPN-glycosylationVisualization of co-clustering molecules

Identifiers

PMID25948169
OpenAlexW315500892

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.