Evidence map›Paper›PMID 32409993›Full record

ArticlePlant molecular biology2020

Multiple N-glycans cooperate in balancing misfolded BRI1 secretion and ER retention.

Tianshu Chen, Huchen Zhang, Guanting Niu, Shuo Zhang, Zhi Hong

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. In-Depth Analysis of theInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. 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

5 authors at 2 institutions in 1 country.

Tianshu ChenState Key Laboratory of Pharmaceutical Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing, 210046, Jiangsu, China.
Huchen ZhangState Key Laboratory of Pharmaceutical Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing, 210046, Jiangsu, China.
Guanting NiuState Key Laboratory of Pharmaceutical Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing, 210046, Jiangsu, China.
Shuo ZhangState Key Laboratory of Pharmaceutical Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing, 210046, Jiangsu, China.
Zhi HongState Key Laboratory of Pharmaceutical Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing, 210046, Jiangsu, China. zhihong@nju.edu.cn.ORCID http://orcid.org/0000-0002-6962-3981
China Pharmaceutical University · CNNanjing University · CN

Funding

National Natural Science Foundation of China No.31322008National Natural Science Foundation of China No.31870263
6 · The paper itself

Abstract

key messageN-glycans play a protective or monitoring role according to the folding state of associated protein or the distance from structural defects. Asparagine-linked (Asn/N-) glycosylation is one of the most prevalent and complex protein modifications and the associated N-glycans play crucial roles on protein folding and secretion. The studies have shown that many glycoproteins hold multiple N-glycans, yet little is known about the redundancy of N-glycans on a protein. In this study, we used BRI1 to decipher the roles of N-glycans on protein secretion and function. We found that all 14 potential N-glycosylation sites on BRI1 were occupied with oligosaccharides. The elimination of single N-glycan had no obvious effect on BRI1 secretion or function except N

Indexed as

AlkaloidsArabidopsisArabidopsis ProteinsEndoplasmic ReticulumGlycoproteinsGlycoside HydrolasesGlycosylationModels, MolecularOligosaccharidesPlants, Genetically ModifiedPolysaccharidesProtein ConformationProtein DomainsProtein KinasesProtein Processing, Post-TranslationalSeedlingsAlkaloidsArabidopsis ProteinsBRI1 protein, ArabidopsisGlycoproteinsGlycoside HydrolaseskifunensineOligosaccharidesPolysaccharidesProtein KinasesArabidopsis thalianaBRI1ERQCLRR-RLKsN-glycosylationProtein secretion

Identifiers

PMID32409993
OpenAlexW3024481773

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.