Evidence map›Paper›PMID 24399998›Full record

ArticleFrontiers in microbiology2013

N-glycosylation in Haloferax volcanii: adjusting the sweetness.

Jerry Eichler, Adi Arbiv, Chen Cohen-Rosenzweig, Lina Kaminski, Lina Kandiba, Zvia Konrad

Abstract read
In one paragraph

Article in Frontiers in microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Journal of bacteriology · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Identifying Components of aFrontiers in microbiology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  12. Article
  13. Review
  14. Preface to the proceedings of Halophiles 2013.Frontiers in microbiology · 2015
    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

6 authors.

Jerry EichlerDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.
Adi ArbivDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.
Chen Cohen-RosenzweigDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.
Lina KaminskiDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.
Lina KandibaDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.
Zvia KonradDepartment of Life Sciences, Ben Gurion University of the Negev Beersheva, Israel.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target protein asparagine residues. Still, it is only in the last decade that pathways of N-glycosylation in Archaea have been delineated. In the haloarchaeon Haloferax volcanii, a series of Agl (archaeal glycosylation) proteins is responsible for the addition of an N-linked pentasaccharide to modified proteins, including the surface (S)-layer glycoprotein, the sole component of the surface layer surrounding the cell. The S-layer glycoprotein N-linked glycosylation profile changes, however, as a function of surrounding salinity. Upon growth at different salt concentrations, the S-layer glycoprotein is either decorated by the N-linked pentasaccharide introduced above or by both this pentasaccharide as well as a tetrasaccharide of distinct composition. Recent efforts have identified Agl5-Agl15 as components of a second Hfx. volcanii N-glycosylation pathway responsible for generating the tetrasaccharide attached to S-layer glycoprotein when growth occurs in 1.75 M but not 3.4 M NaCl-containing medium.

Indexed as

ArchaeaHaloferax volcaniiN-glycosylationpost-translational modificationprotein glycosylationS-layer glycoprotein

Identifiers

PMID24399998
PMCPMC3871713

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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.