Evidence map›Paper›PMID 31138648›Full record

ArticleThe Journal of biological chemistry2019

The ceramide moiety of disialoganglioside (GD3) is essential for GD3 recognition by the sialic acid-binding lectin SIGLEC7 on the cell surface.

Noboru Hashimoto, Shizuka Ito, Akiko Tsuchida, Robiul H Bhuiyan, Tetsuya Okajima, Akihito Yamamoto, Keiko Furukawa, Yuhsuke Ohmi, Koichi Furukawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. JACS Au · 2026
    Article
  3. Article
  4. New Sialic Acid-Binding Site of SIGLEC-7.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Gangliosides as Siglec ligands.Glycoconjugate journal · 2023
    Review
  17. MYC-driven synthesis of Siglec ligands is a glycoimmune checkpoint.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  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

9 authors at 3 institutions in 1 country.

Noboru HashimotoDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan,; Department of Tissue Regeneration, Tokushima University Graduate School of Biomedical Sciences, 3-18-5, Kuramoto-cho, Tokushima 770-8504, Japan.
Shizuka ItoDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Akiko TsuchidaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Robiul H BhuiyanDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan,; Department of Biomedical Sciences, Chubu University College of Life and Health Sciences, 1200 Matsumoto, Kasugai, Aichi 487-8501, Japan, and.
Tetsuya OkajimaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
Akihito YamamotoDepartment of Tissue Regeneration, Tokushima University Graduate School of Biomedical Sciences, 3-18-5, Kuramoto-cho, Tokushima 770-8504, Japan.
Keiko FurukawaDepartment of Biomedical Sciences, Chubu University College of Life and Health Sciences, 1200 Matsumoto, Kasugai, Aichi 487-8501, Japan, and.
Yuhsuke OhmiDepartment of Biomedical Sciences, Chubu University College of Life and Health Sciences, 1200 Matsumoto, Kasugai, Aichi 487-8501, Japan, and.
Koichi FurukawaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan,; Department of Biomedical Sciences, Chubu University College of Life and Health Sciences, 1200 Matsumoto, Kasugai, Aichi 487-8501, Japan, and. Electronic address: koichi@isc.chubu.ac.jp.
Chubu University · JPNagoya University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To analyze the binding specificity of a sialic acid-recognizing lectin, sialic acid-binding Ig-like lectin 7 (SIGLEC7), to disialyl gangliosides (GD3s), here we established GD3-expressing cells by introducing GD3 synthase (

Indexed as

Antigens, Differentiation, MyelomonocyticCell Line, TumorCell MembraneCeramidesGangliosidesGlycosphingolipidsHumansLectinsLeukocytes, MononuclearN-Acetylneuraminic AcidProtein BindingSialyltransferasesSubstrate SpecificityAntigens, Differentiation, MyelomonocyticCeramidesGangliosidesGlycosphingolipidsLectinsN-Acetylneuraminic AcidsialogangliosidesSialyltransferasesSIGLEC7 protein, humancancer-associated carbohydrateceramidefatty acidgangliosideglycolipid structureglycosphingolipidhydroxylationimmunitymembranesilica acid-binding Ig-like lectin 7 (Siglec-7)

Identifiers

PMID31138648
PMCPMC6635455
OpenAlexW2947980543

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.