Evidence map›Paper›PMID 30789994›Full record

ArticleDiabetologia2019

Cytoplasmic ends of tetraspanin 7 harbour epitopes recognised by autoantibodies in type 1 diabetes.

Anne Eugster, Gloria Kraus, Vicky Lidzba, Denise Müller, Manja Jolink, Anette-G Ziegler, Ezio Bonifacio

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Diabetologia, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Review
  3. Anti-Islet Autoantibodies in Type 1 Diabetes.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Review
  6. Autoimmunity to tetraspanin-7 in type 1 diabetes.Medical microbiology and immunology · 2020
    Review
  7. Birth and coming of age of islet autoantibodies.Clinical and experimental immunology · 2019
    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 4 institutions in 1 country.

Anne EugsterDFG-Centre for Regenerative Therapies Dresden, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Fetscherstrasse 105, 01307, Dresden, Germany.
Gloria KrausDFG-Centre for Regenerative Therapies Dresden, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Fetscherstrasse 105, 01307, Dresden, Germany.
Vicky LidzbaDFG-Centre for Regenerative Therapies Dresden, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Fetscherstrasse 105, 01307, Dresden, Germany.
Denise MüllerDFG-Centre for Regenerative Therapies Dresden, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Fetscherstrasse 105, 01307, Dresden, Germany.
Manja JolinkInstitute of Diabetes Research, Helmholtz Zentrum München, Munich, Germany.
Anette-G ZieglerInstitute of Diabetes Research, Helmholtz Zentrum München, Munich, Germany.
Ezio BonifacioDFG-Centre for Regenerative Therapies Dresden, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Fetscherstrasse 105, 01307, Dresden, Germany. ezio.bonifacio@tu-dresden.de.
University Hospital Carl Gustav Carus · DETU Dresden · DEKlinikum rechts der Isar · DEMünchen Klinik · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aims/hypothesisThe beta cell protein tetraspanin 7 is a target of autoantibodies in individuals with type 1 diabetes. The aim of this study was to identify autoantibody epitope-containing regions and key residues for autoantibody binding.

methodsAutoantibody epitope regions were identified by immunoprecipitation of luciferase-tagged single or multiple tetraspanin 7 domains using tetraspanin 7 antibody-positive sera. Subsequently, amino acids (AAs) relevant for autoantibody binding were identified by single AA mutations.

resultsIn tetraspanin 7 antibody-positive sera, antibody binding was most frequent to tetraspanin 7 proteins that contained the NH CONCLUSIONS/

interpretationWe hypothesise that conformation and, potentially, modification of protein terminal ends of tetraspanin 7 may be important for autoantibody binding in type 1 diabetes.

Indexed as

AdolescentAutoantibodiesAutoantigensChildDiabetes Mellitus, Type 1DNA Mutational AnalysisEpitopesFemaleHumansInsulin-Secreting CellsLuciferasesMaleMutationNerve Tissue ProteinsPhosphorylationProtein BindingAutoantibodiesAutoantigensEpitopesLuciferasesNerve Tissue ProteinsTetraspaninsTSPAN7 protein, humanAutoantibodiesEpitopesGlima 38Tetraspanin 7Type 1 diabetes mellitus

Identifiers

PMID30789994
OpenAlexW2916841368

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.