Evidence map›Paper›PMID 18310347›Full record

ArticleJournal of bacteriology2008

Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein.

Mehtap Abu-Qarn, Assunta Giordano, Francesca Battaglia, Andrej Trauner, Paul G Hitchen, Howard R Morris, Anne Dell, Jerry Eichler

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.3field-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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
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  4. Identifying Components of aFrontiers in microbiology · 2021
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Extreme sweetness: protein glycosylation in archaea.Nature reviews. Microbiology · 2013
    Review
  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

8 authors at 3 institutions in 3 countries.

Mehtap Abu-QarnDepartment of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel.
Assunta Giordano
Francesca Battaglia
Andrej Trauner
Paul G Hitchen
Howard R Morris
Anne Dell
Jerry Eichler
Imperial College London · GBBen-Gurion University of the Negev · ILIstituto di Chimica Biomolecolare · IT

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast to relatively advanced understanding of the eukaryal N glycosylation process and the information being amassed on the bacterial process, little is known of this posttranslational modification in Archaea. Toward remedying this situation, the present report continues ongoing efforts to identify components involved in the N glycosylation of the Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE, originally identified as a homologue of murine Dpm1, was shown to play a role in the addition of the 190-Da sugar subunit of the novel pentasaccharide decorating the S-layer glycoprotein. Topological analysis of an AglE-based chimeric reporter assigns AglE as an integral membrane protein, with its N terminus and putative active site facing the cytoplasm. These finding, therefore, contribute to the developing picture of the N glycosylation pathway in Archaea.

Indexed as

Amino Acid SequenceArchaeal ProteinsChromosome MappingGene DeletionGlycosylationHaloferax volcaniiMannosyltransferasesMembrane GlycoproteinsMolecular Sequence DataSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationArchaeal Proteinsdolichyl-phosphate beta-D-mannosyltransferaseMannosyltransferasesMembrane Glycoproteins

Identifiers

PMID18310347
PMCPMC2347396
OpenAlexW2099868030

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.