Evidence map›Paper›PMID 28270545›Full record

ArticleThe Biochemical journal2017

Manganese-induced turnover of TMEM165.

Sven Potelle, Eudoxie Dulary, Leslie Climer, Sandrine Duvet, Willy Morelle, Dorothée Vicogne, Elodie Lebredonchel, Marine Houdou, Corentin Spriet, Marie-Ange Krzewinski-Recchi and 8 more

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.7field-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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. SLC10A7 regulates O-GalNAc glycosylation and CaCellular and molecular life sciences : CMLS · 2025
    Article
  4. Putative role of TMEM165 in congenital cardiomyopathies.Frontiers in molecular neuroscience · 2025
    Review
  5. Article
  6. Review
  7. Insights into the regulation of cellular MnBiochimica et biophysica acta. Molecular basis of disease · 2023
    Article
  8. Review
  9. Article
  10. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Iron and manganese transport in mammalian systems.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  18. Article
  19. Review
  20. Article
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

18 authors at 6 institutions in 3 countries.

Sven PotelleCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Eudoxie DularyCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Leslie ClimerDepartment of Physiology and Biophysics, College of Medicine, University of Arkansas for Medical Sciences, Biomed 261-2, Slot 505, 200 South Cedar St., Little Rock, AR 72205, U.S.A.
Sandrine DuvetCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Willy MorelleCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Dorothée VicogneCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Elodie LebredonchelCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Marine HoudouCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Corentin SprietCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Marie-Ange Krzewinski-RecchiCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Romain PeanneCenter for Human Genetics, KU Leuven, Leuven, Belgium.
André KleinCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Geoffroy de BettigniesCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure").
Pierre MorsommeInstitut des Sciences de la Vie, Université catholique de Louvain, Louvain-la-Neuve B-1348, Belgium.
Gert MatthijsCenter for Human Genetics, KU Leuven, Leuven, Belgium.
Thorsten MarquardtKlinik und Poliklinik für Kinder- und Jugendmedizin, Universitätsklinikum Münster, Albert-Schweitzer-Campus 1, Gebäude A 1, Münster 48149, Germany.
Vladimir LupashinDepartment of Physiology and Biophysics, College of Medicine, University of Arkansas for Medical Sciences, Biomed 261-2, Slot 505, 200 South Cedar St., Little Rock, AR 72205, U.S.A.
François FoulquierCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille F-59000, France and the LIA GLYCOLAB4CDG France/ Belgium (International Associated Laboratory "Laboratory for the Research on Congenital Disorders of Glycosylation - from cellular mechanisms to cure") francois.foulquier@univ-lille1.fr.
Université de Lille · FRUnité de Glycobiologie Structurale et Fonctionnelle · FRCentre National de la Recherche Scientifique · FRKU Leuven · BEUCLouvain · BEUniversity Hospital Münster · DE

Funding

Characterization of mammalian COG complex-interacting intra-Golgi trafficking macR01GM083144 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VLADIMIR V LUPASHIN · 2008 to 2026
$6.5M
Super-Res Holographic Microscopy to Advance Research on Golgi Apparatus FunctionU54GM105814 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI BROOKER, GARY, LUPASHIN, VLADIMIR V · 2013 to 2017
$2.1M
NIGMS NIH HHS R01 GM083144NIGMS NIH HHS U54 GM105814
6 · The paper itself

Abstract

TMEM165 deficiencies lead to one of the congenital disorders of glycosylation (CDG), a group of inherited diseases where the glycosylation process is altered. We recently demonstrated that the Golgi glycosylation defect due to TMEM165 deficiency resulted from a Golgi manganese homeostasis defect and that Mn

Indexed as

Amino Acid MotifsAmino Acid SequenceAntiportersBlotting, WesternCalcium-Transporting ATPasesCation Transport ProteinsDose-Response Relationship, DrugGene Knockdown TechniquesGlutamatesGlycosylationGolgi ApparatusHEK293 CellsHeLa CellsHumansLysosomesManganeseAntiportersATP2C1 protein, humanCalcium-Transporting ATPasesCation Transport ProteinsGlutamatesManganeseMembrane ProteinsTMEM165 protein, humancongenital disorders of glycosylationglycosylationGolgi apparatusmanganeseTMEM165

Identifiers

PMID28270545
PMCPMC5595065
OpenAlexW2594241987

What OpenQuestion holds

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Registered trials

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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.