Evidence map›Paper›PMID 32103179›Full record

ArticleNature2020

Structure and mechanism of the ER-based glucosyltransferase ALG6.

Joël S Bloch, Giorgio Pesciullesi, Jérémy Boilevin, Kamil Nosol, Rossitza N Irobalieva, Tamis Darbre, Markus Aebi, Anthony A Kossiakoff, Jean-Louis Reymond, Kaspar P Locher

Open access · greenAbstract read
In one paragraph

Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.7field-weighted citation impact, top 4% 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, 85 citations in OpenAlex.

  1. Article
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  6. Article
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  9. Article
  10. Article
  11. Article
  12. Review
  13. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
  14. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  15. Article
  16. Article
  17. Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

10 authors at 3 institutions in 2 countries.

Joël S BlochInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Giorgio PesciullesiDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Jérémy BoilevinDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Kamil NosolInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Rossitza N IrobalievaInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Tamis DarbreDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Markus AebiInstitute of Microbiology, ETH Zürich, Zürich, Switzerland.
Anthony A KossiakoffDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.
Jean-Louis ReymondDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Kaspar P LocherInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland. locher@mol.biol.ethz.ch.
ETH Zurich · CHUniversity of Bern · CHUniversity of Chicago · US

Funding

Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
NIGMS NIH HHS R01 GM117372NIH HHS GM117372
6 · The paper itself

Abstract

In eukaryotic protein N-glycosylation, a series of glycosyltransferases catalyse the biosynthesis of a dolichylpyrophosphate-linked oligosaccharide before its transfer onto acceptor proteins

Indexed as

Cryoelectron MicroscopyBiocatalysisCatalytic DomainConserved SequenceDolichol Monophosphate MannoseDolichol PhosphatesEndoplasmic ReticulumGlucoseGlycosyltransferasesIn Vitro TechniquesLipidsMembrane ProteinsModels, MolecularMutationPolyisoprenyl Phosphate MonosaccharidesProtein BindingALG6 protein, S cerevisiaedolichol-D-glucosylmonophosphatedolichol monophosphateDolichol Monophosphate MannoseDolichol PhosphatesGlucoseGlycosyltransferasesLipidsMembrane ProteinsPolyisoprenyl Phosphate MonosaccharidesSaccharomyces cerevisiae Proteins

Identifiers

PMID32103179
PMCPMC8712213
OpenAlexW3008857498

What OpenQuestion holds

Textmetadata
LicenceTDM
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.