Evidence map›Paper›PMID 23624439›Full record

ArticleNature chemical biology2013

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.

Angelyn Larkin, Michelle M Chang, Garrett E Whitworth, Barbara Imperiali

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact, top 96% 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

28 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Identifying Components of aFrontiers in microbiology · 2021
    Article
  7. Review
  8. Article
  9. In Search for the Membrane Regulators of Archaea.International journal of molecular sciences · 2019
    Review
  10. Disrupted Synthesis of a Di-Journal of bacteriology · 2019
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  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

4 authors at 1 institution in 1 country.

Angelyn LarkinDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Michelle M Chang
Garrett E Whitworth
Barbara Imperiali
Massachusetts Institute of Technology · US

Funding

SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
SPECIFICITY IN CO POST TRANSLATION MODIFICATIONR29GM039334 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI IMPERIALI, BARBARA · 1988 to 1992
–
NIGMS NIH HHS GM039334NIGMS NIH HHS R01 GM039334
6 · The paper itself

Abstract

Asparagine-linked glycosylation is a complex protein modification conserved among all three domains of life. Herein we report the in vitro analysis of N-linked glycosylation from the methanogenic archaeon Methanococcus voltae. Using a suite of synthetic and semisynthetic substrates, we show that AglK initiates N-linked glycosylation in M. voltae through the formation of α-linked dolichyl monophosphate N-acetylglucosamine, which contrasts with the polyprenyl diphosphate intermediates that feature in both eukaryotes and bacteria. Notably, AglK has high sequence homology to dolichyl phosphate β-glucosyltransferases, including Alg5 in eukaryotes, suggesting a common evolutionary origin. The combined action of the first two enzymes, AglK and AglC, afforded an α-linked dolichyl monophosphate glycan that serves as a competent substrate for the archaeal oligosaccharyl transferase AglB. These studies provide what is to our knowledge the first biochemical evidence revealing that, despite the apparent similarity of the overall pathways, there are actually two general strategies to achieve N-linked glycoproteins across the domains of life.

Indexed as

Gene Expression RegulationArchaeal ProteinsEscherichia coliEvolution, MolecularGlucosyltransferasesGlycopeptidesGlycoproteinsGlycosylationLipidsMagnetic Resonance SpectroscopyMass SpectrometryMethanococcusPlasmidsPolysaccharidesArchaeal ProteinsGlucosyltransferasesGlycopeptidesGlycoproteinsLipidsPolysaccharides

Identifiers

PMID23624439
PMCPMC3661703
OpenAlexW1567676619

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.