Evidence map›Paper›PMID 29519914›Full record

ArticleScience (New York, N.Y.)2018

Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum.

Katharina Braunger, Stefan Pfeffer, Shiteshu Shrimal, Reid Gilmore, Otto Berninghausen, Elisabet C Mandon, Thomas Becker, Friedrich Förster, Roland Beckmann

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
15.1field-weighted citation impact, top 1% 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

139 citing papers in PubMed, 237 citations in OpenAlex.

  1. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  2. Review
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  7. Calsyntenin-3 suppresses inflammation via inhibition of TLR N-glycosylation and membrane localization.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
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  10. Studying Glycan-Dependent ERAD of Misfolded Glycoproteins in Plants.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  11. Article
  12. Article
  13. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  14. Article
  15. Review
  16. Article
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  19. Article
  20. Article

79 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 3 countries.

Katharina BraungerDepartment of Biochemistry, Gene Center and Center for Integrated Protein Science Munich, University of Munich, 81377 Munich, Germany.ORCID 0000-0002-9067-2155
Stefan PfefferDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. beckmann@genzentrum.lmu.de pfeffer@biochem.mpg.de f.g.forster@uu.nl.ORCID 0000-0001-5843-2795
Shiteshu ShrimalDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.ORCID 0000-0002-6776-5265
Reid GilmoreDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.ORCID 0000-0002-1656-4041
Otto BerninghausenDepartment of Biochemistry, Gene Center and Center for Integrated Protein Science Munich, University of Munich, 81377 Munich, Germany.ORCID 0000-0002-9255-0522
Elisabet C MandonDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.ORCID 0000-0001-9616-3469
Thomas BeckerDepartment of Biochemistry, Gene Center and Center for Integrated Protein Science Munich, University of Munich, 81377 Munich, Germany.ORCID 0000-0001-8458-2738
Friedrich FörsterCryo-Electron Microscopy, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, Netherlands. beckmann@genzentrum.lmu.de pfeffer@biochem.mpg.de f.g.forster@uu.nl.ORCID 0000-0002-6044-2746
Roland BeckmannDepartment of Biochemistry, Gene Center and Center for Integrated Protein Science Munich, University of Munich, 81377 Munich, Germany. beckmann@genzentrum.lmu.de pfeffer@biochem.mpg.de f.g.forster@uu.nl.ORCID 0000-0003-4291-3898
Center for Integrated Protein Science Munich · DEUniversity of Massachusetts Chan Medical School · USMax Planck Institute of Biochemistry · DEUniversity of Applied Sciences Utrecht · NL

Funding

PROTEIN TRANSLOCATION ACROSS THE ENDOPLASMIC RETICULUMR01GM035687 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1985 to 2019
$5.9M
European Research CouncilNIGMS NIH HHS R01 GM035687
6 · The paper itself

Abstract

Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo-electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum.

Indexed as

Models, MolecularCryoelectron MicroscopyEndoplasmic ReticulumGlycosylationHEK293 CellsHexosyltransferasesHumansMembrane ProteinsProtein ConformationProtein TransportRibosomesSEC Translocation Channelsdolichyl-diphosphooligosaccharide - protein glycotransferaseHexosyltransferasesMembrane ProteinsSEC Translocation ChannelsSTT3A protein, human

Identifiers

PMID29519914
PMCPMC6319373
OpenAlexW2792177065

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.