Evidence map›Paper›PMID 31868591›Full record

ArticleeLife2019

C-mannosylation supports folding and enhances stability of thrombospondin repeats.

Aleksandra Shcherbakova, Matthias Preller, Manuel H Taft, Jordi Pujols, Salvador Ventura, Birgit Tiemann, Falk Fr Buettner, Hans Bakker

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 81 citations in OpenAlex.

  1. From a single C-mannose to multiple C-mannosyltransferases.The Journal of biological chemistry · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. ProteinMolecules (Basel, Switzerland) · 2025
    Review
  7. Article
  8. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. RSC advances · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
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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

8 authors at 2 institutions in 2 countries.

Aleksandra ShcherbakovaInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0003-4175-547X
Matthias PrellerInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-7784-4012
Manuel H TaftInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0001-5853-8629
Jordi PujolsInstitut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Salvador VenturaInstitut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.ORCID 0000-0002-9652-6351
Birgit TiemannInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.
Falk Fr BuettnerInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-8468-1223
Hans BakkerInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-1364-9154
Medizinische Hochschule Hannover · DEUniversitat Autònoma de Barcelona · ES

Funding

Deutsche Forschungsgemeinschaft BA 4091/5-1Deutsche Forschungsgemeinschaft BU 2920/2-1Deutsche Forschungsgemeinschaft FOR2509 BA 4091/6-1
6 · The paper itself

Abstract

Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin receptor UNC-5. In absence of C-mannosylation, UNC-5 TSRs could only be obtained at low temperature and a significant proportion displayed incorrect intermolecular disulfide bridging, which was hardly observed when C-mannosylated. Glycosylated TSRs exhibited higher resistance to thermal and reductive denaturation processes, and the presence of C-mannoses promoted the oxidative folding of a reduced and denatured TSR in vitro. Molecular dynamics simulations supported the experimental studies and showed that C-mannoses can be involved in intramolecular hydrogen bonding and limit the flexibility of the TSR tryptophan-arginine ladder. We propose that in the endoplasmic reticulum folding process, C-mannoses orient the underlying tryptophan residues and facilitate the formation of the tryptophan-arginine ladder, thereby influencing the positioning of cysteines and disulfide bridging.

Indexed as

Protein FoldingAnimalsArginineCaenorhabditis elegansCaenorhabditis elegans ProteinsCysteineDisulfidesDrosophila melanogasterEndoplasmic ReticulumGlycosylationHydrogen BondingMannoseMembrane ProteinsMolecular Dynamics SimulationProtein ConformationReceptors, Cell SurfaceArginineCaenorhabditis elegans ProteinsCysteineDisulfidesDPY-19 protein, C elegansMannoseMembrane ProteinsReceptors, Cell SurfaceThrombospondinsTryptophanUNC-5 protein, C elegansbiochemistryC. eleganscell biologychemical biologyC-mannosylationD. melanogasterglycosylationprotein foldingprotein stabilitythrombospondin type 1 repeatstryptophan-arginine ladder

Identifiers

PMID31868591
PMCPMC6954052
OpenAlexW2995628811

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.