Evidence map›Paper›PMID 26452604›Full record

ArticleGlycoconjugate journal2015

The role of N-glycan modification of TNFR1 in inflammatory microglia activation.

Lijian Han, Dongmei Zhang, Tao Tao, Xiaolei Sun, Xiaojuan Liu, Guizhou Zhu, Zhiwei Xu, Liang Zhu, Yu Zhang, Wangrui Liu and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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  15. Review
  16. Palmitoylation is required for TNF-R1 signaling.Cell communication and signaling : CCS · 2019
    Article
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  19. Review
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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

12 authors.

Lijian HanDepartment of Neurology, Affiliated Hospital of Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Dongmei ZhangThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Tao TaoThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Xiaolei SunThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Xiaojuan LiuThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Guizhou ZhuThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Zhiwei XuThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Liang ZhuDepartment of Neurology, Affiliated Hospital of Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Yu ZhangDepartment of Neurology, Affiliated Hospital of Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Wangrui LiuThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China.
Kaifu KeDepartment of Neurology, Affiliated Hospital of Nantong University, Nantong, 226000, Jiangsu, People's Republic of China. kekaifu1@sina.com.
Aiguo ShenThe Jiangsu Province Key Laboratory for Inflammation and Molecular Drug Target, Nantong University, Nantong, 226000, Jiangsu, People's Republic of China. shag@ntu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulating evidences demonstrated that microglia activation and the autocrine loop of tumor necrosis factor-α (TNFα) greatly contribute to the pathogenesis of several CNS diseases. TNFα exerts its biological effects by interacting with two different receptors: TNF receptor 1 (TNFR1) and TNFR2. The classic proinflammatory activity of TNFα is mainly mediated by TNFR1. In the present study, we found that TNFR1 was modificated by N-glycosylation on Asn151 and Asn202 in microglia. The N-glycosylation of TNFR1 could facilitate its capability of binding to TNFα and further promote the formation of TNFα autocrine loop in microglia stimulated by TNFα, resulting in excessive microglia activation and CNS inflammation. All these processes were related to TNFR1-mediated NF-κB pathways. Elimination of N-glycosylation did not affect the subcellular transportation and cell surface localization of TNFR1, but suppressed ligand-binding affinity. These findings indicated that the N-glycosylation of TNFR1 played an important role during microglia activation in CNS inflammation. By this study, we aimed to provide some valuable experimental evidence for a better understanding of the significance of protein glycosylation in microglia inflammatory activation and CNS disease.

Indexed as

Protein Processing, Post-TranslationalAnimalsGlycosylationHEK293 CellsHumansMiceMicrogliaNF-kappa BProtein BindingProtein TransportReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alphaNF-kappa BReceptors, Tumor Necrosis Factor, Type ITnfrsf1a protein, mouseTumor Necrosis Factor-alphaMicroglia activationNF-κBN-glycosylationTNFR1TNFα

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Registered trials

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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.