Evidence map›Paper›PMID 27558752›Full record

ArticleThe New phytologist2016

Endoplasmic reticulum-associated N-glycan degradation of cold-upregulated glycoproteins in response to chilling stress in Arabidopsis.

Jun Ma, Dinghe Wang, Jessica She, Jianming Li, Jian-Kang Zhu, Yi-Min She

Abstract read
In one paragraph

Article in The New phytologist, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Plants (Basel, Switzerland) · 2022
    Review
  7. Article
  8. Article
  9. Physiological and Biochemical Traits of Two MajorFrontiers in plant science · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. NaGenomics, proteomics & bioinformatics · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Molecular & cellular proteomics : MCP · 2018
    Article
  18. Article
  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

6 authors.

Jun MaShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.
Dinghe WangShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.
Jessica SheShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.
Jianming LiShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.
Jian-Kang ZhuShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.
Yi-Min SheShanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai, 201602, China.

Funding

CALCIUM SIGNALING--INTRACELL ION HOMEOSTASIS REGULATIONR01GM059138 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI ZHU, JIAN-KANG · 1999 to 2015
$4.4M
NIGMS NIH HHS R01 GM059138
6 · The paper itself

Abstract

N-glycosylation has a great impact on glycoprotein structure, conformation, stability, solubility, immunogenicity and enzyme activity. Structural characterization of N-glycoproteome has been challenging but can provide insights into the extent of protein folding and surface topology. We describe a highly sensitive proteomics method for large-scale identification and quantification of glycoproteins in Arabidopsis through (15) N-metabolic labeling, selective enrichment of glycopeptides, data-dependent MS/MS analysis and automated database searching. In-house databases of Arabidopsis glycoproteins and glycopeptides containing Asn-X-Ser/Thr/Cys motifs were constructed by reducing 20% and 90% of the public database size, respectively, to enable a rapid analysis of large datasets for comprehensive identification and quantification of glycoproteins and heterogeneous N-glycans in a complex mixture. Proteome-wide analysis identified c. 100 stress-related N-glycoproteins, of which the endoplasmic reticulum (ER) resident proteins were examined to be up-regulated. Quantitative measurements provided a molecular signature specific to glycoproteins for determining the degree of plant stress at low temperature. Structural N-glycoproteomics following time-course cold treatments revealed the stress-responsive degradation of high-mannose type N-glycans in ER in response to chilling stress, which may aid in elucidating the cellular mechanisms of protein relocation, transport, trafficking, misfolding and degradation under stress conditions.

Indexed as

FreezingProteolysisStress, PhysiologicalUp-RegulationAmino Acid SequenceArabidopsisArabidopsis ProteinsCold TemperatureEndoplasmic ReticulumGlycopeptidesGlycoproteinsHigh-Throughput Screening AssaysPolysaccharidesReproducibility of ResultsArabidopsis ProteinsGlycopeptidesGlycoproteinsPolysaccharidesArabidopsischilling stressendoplasmic reticulum (ER)glycoproteomicsliquid chromatography-tandem mass spectrometry

Identifiers

PMID27558752
PMCPMC5513495

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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.