Evidence map›Paper›PMID 9096318›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Expression cloning and characterization of a cDNA encoding a novel membrane protein required for the formation of O-acetylated ganglioside: a putative acetyl-CoA transporter.

A Kanamori, J Nakayama, M N Fukuda, W B Stallcup, K Sasaki, M Fukuda, Y Hirabayashi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 10% 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, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.

  1. Frontiers in neuroscience · 2019
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. The dual role of SrbA from Paracoccidioides lutzii: a hypoxic regulator.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021
    Article
  15. Review
  16. Review
  17. Role of Sialyl-Cells · 2021
    Article
  18. Article
  19. Article
  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

7 authors at 3 institutions in 2 countries.

A KanamoriLaboratory for Cellular Glycobiology, The Institute of Physical and Chemical Research, Wako, Saitama, Japan.
J Nakayama
M N Fukuda
W B Stallcup
K Sasaki
M Fukuda
Y Hirabayashi
RIKEN · JPSanford Burnham Prebys Medical Discovery Institute · USDigital Research Alliance of Canada

Funding

THE A(1,3)FUCOSYLTRANSFERASE GENES AND SELECTIN LIGAND EXPRESSIONP01CA071932 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LOWE, JOHN B · 1996 to 2012
$15.5M
Polylactosamines in Development and CancerR01CA048737 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI FUKUDA, MINORU · 1989 to 2007
$3.1M
NCI NIH HHS CA 48737NCI NIH HHS P01 CA071932NCI NIH HHS P01 CA71932NCI NIH HHS R01 CA048737
6 · The paper itself

Abstract

By expression cloning using COS-1 cells stably transfected with GD3-synthase (COS-1/GD3+) as a recipient cell line, we have isolated a cDNA, termed AT-1, encoding a novel protein required for the formation of O-acetylated (Ac) gangliosides. The cDNA encodes a protein with multitransmembrane spanning domains with a leucine zipper motif. It consists of 549 amino acids and has a molecular mass of 60.9 kDa. Although both O-Ac-GD3 and O-Ac-GT3 were barely detectable in recipient cells or cells transfected with the vector alone, their amount increased significantly in transfectants containing AT-1. When semi-intact cells prepared by treatment with streptolysin O were incubated with [Ac-14C]-Ac-CoA, increased incorporation of radioactivity was found in those cells transfected with AT-1 when compared with the mock transfectants. Northern blot analysis showed two major transcripts of 3.3 and 4.3 kb in all tissues examined. Immunohistochemical study with an antibody specific to the AT-1 protein suggested that it is most probably expressed in the endoplasmic reticulum membrane. Based on these results, the protein encoded by AT-1 is suggested to be an Ac-CoA transporter that is involved in the process of O-acetylation.

Indexed as

Membrane Transport ProteinsAcetylationAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernCarrier ProteinsCloning, MolecularCOS CellsDNA, ComplementaryGangliosidesHeLa CellsHumansImmunohistochemistryMembrane ProteinsMolecular Sequence DataCarrier ProteinsDNA, ComplementaryGangliosidesMembrane ProteinsMembrane Transport ProteinsRNA, MessengerSLC33A1 protein, human

Identifiers

PMID9096318
PMCPMC20294
OpenAlexW2061522246

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.