Evidence map›Paper›PMID 27573243›Full record

ArticleThe Journal of biological chemistry2016

Bacterial N-Glycosylation Efficiency Is Dependent on the Structural Context of Target Sequons.

Julie Michelle Silverman, Barbara Imperiali

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Acceptors stability modulates the efficiency of post-translational protein N-glycosylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Proteomics Reveals Multiple Phenotypes Associated withMolecular & cellular proteomics : MCP · 2019
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Gut microbes
    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

2 authors at 1 institution in 1 country.

Julie Michelle SilvermanFrom the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Barbara ImperialiFrom the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 imper@mit.edu.
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
Molecular determinants of N-linked glycosylation in Campylobacter jejuniF32AI109857 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SILVERMAN, JULIE MICHELLE · 2014 to 2017
$156k
NIAID NIH HHS F32 AI109857NIGMS NIH HHS R01 GM039334
6 · The paper itself

Abstract

Site selectivity of protein N-linked glycosylation is dependent on many factors, including accessibility of the modification site, amino acid composition of the glycosylation consensus sequence, and cellular localization of target proteins. Previous studies have shown that the bacterial oligosaccharyltransferase, PglB, of Campylobacter jejuni favors acceptor proteins with consensus sequences ((D/E)X

Indexed as

Bacterial Secretion SystemsCampylobacter jejuniEscherichia coliEscherichia coli ProteinsGlycosylationHexosyltransferasesLipoproteinsMembrane ProteinsMembrane Transport ProteinsPeriplasmAcrA protein, E coliBacterial Secretion Systemsdolichyl-diphosphooligosaccharide - protein glycotransferaseEscherichia coli ProteinsHexosyltransferasesLipoproteinsMembrane ProteinsMembrane Transport ProteinsN-linked glycosylationoligosaccharyltransferaseprotein foldingprotein translocationsubstrate specificity

Identifiers

PMID27573243
PMCPMC5063983
OpenAlexW2511075865

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.