Evidence map›Paper›PMID 24212570›Full record

ArticleApplied and environmental microbiology2014

Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.

Chen Cohen-Rosenzweig, Ziqiang Guan, Boaz Shaanan, Jerry Eichler

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Identification of a novelThe Journal of biological chemistry · 2020
    Article
  8. Review
  9. Frontiers in microbiology · 2019
    Article
  10. Article
  11. Article
  12. 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
  13. Article
  14. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

4 authors at 2 institutions in 2 countries.

Chen Cohen-RosenzweigDepartment of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel.
Ziqiang Guan
Boaz Shaanan
Jerry Eichler
Ben-Gurion University of the Negev · ILDuke Medical Center · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
NIGMS NIH HHS GM-069338NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Across evolution, N-glycosylation involves oligosaccharyltransferases that transfer lipid-linked glycans to selected Asn residues of target proteins. While these enzymes catalyze similar reactions in each domain, differences exist in terms of the chemical composition, length and degree of phosphorylation of the lipid glycan carrier, the sugar linking the glycan to the lipid carrier, and the composition and structure of the transferred glycan. To gain insight into how oligosaccharyltransferases cope with such substrate diversity, the present study analyzed the archaeal oligosaccharyltransferase AglB from four haloarchaeal species. Accordingly, it was shown that despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei could readily replace their counterpart from Haloferax volcanii when introduced into Hfx. volcanii cells deleted of aglB. As the four enzymes show significant sequence and apparently structural homology, it appears that the functional similarity of the four AglB proteins reflects the relaxed substrate specificity of these enzymes. Such demonstration of AglB substrate promiscuity is important not only for better understanding of N-glycosylation in Archaea and elsewhere but also for efforts aimed at transforming Hfx. volcanii into a glycoengineering platform.

Indexed as

Amino Acid SequenceArchaeal ProteinsDolicholsGlycosylationHaloarcula marismortuiHalobacterium salinarumHaloferax volcaniiHexosyltransferasesMembrane ProteinsModels, MolecularMolecular Sequence DataPolysaccharidesProtein ConformationSubstrate SpecificityArchaeal ProteinsDolicholsdolichyl-diphosphooligosaccharide - protein glycotransferaseHexosyltransferasesMembrane ProteinsPolysaccharides

Identifiers

PMID24212570
PMCPMC3911113
OpenAlexW2145543303

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.