Evidence map›Paper›PMID 32310828›Full record

ArticleAging2020

SIRT1 regulates O-GlcNAcylation of tau through OGT.

Shu Lu, Xiaomin Yin, Jia Wang, Qun Gu, Qin Huang, Nana Jin, Dandan Chu, Ziqi Xu, Fei Liu, Wei Qian

Open access · greenAbstract read
In one paragraph

Article in Aging, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. The sirtuin family in health and disease.Signal transduction and targeted therapy · 2022
    Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Frontiers in genetics · 2020
    Review
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

10 authors at 2 institutions in 2 countries.

Shu LuDepartment of Intensive Care Unit, The Affiliated Hospital of Nantong University, Nantong, Jiangsu, P. R. China.
Xiaomin YinDepartment of Biochemistry and Molecular Biology, Medical School, Nantong, Jiangsu, P. R. China.
Jia WangJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Qun GuJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Qin HuangJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Nana JinJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Dandan ChuJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Ziqi XuDepartment of Biochemistry and Molecular Biology, Medical School, Nantong, Jiangsu, P. R. China.
Fei LiuJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, P. R. China.
Wei QianDepartment of Biochemistry and Molecular Biology, Medical School, Nantong, Jiangsu, P. R. China.
Nantong University · CNAffiliated Hospital of Nantong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau is modified with O-GlcNAcylation extensively in human brain. The O-GlcNAcylation levels of tau are decreased in Alzheimer's disease (AD) brain. Sirtuin type 1 (SIRT1) is an enzyme that deacetylates proteins including transcriptional factors and associates with neurodegenerative diseases, such as AD. Aberrant SIRT1 expression levels in AD brain is in parallel with the accumulation of tau. cAMP response element binding protein (CREB), a cellular transcription factor, plays a critical role in learning and memory. In this present study, we found SIRT1 deacetylates CREB and inhibits phosphorylation of CREB at Ser133. The inactivated CREB suppresses OGT expression and therefore decreases the O-GlcNAcylation of tau and thus increases the phosphorylation of tau at specific sites. These findings suggest that SIRT1 may be a potential therapeutic target for treating tauopathies.

Indexed as

AcetylglucosamineAnimalsChlorocebus aethiopsCOS CellsCyclic AMP Response Element-Binding ProteinGlycosylationHEK293 CellsHumansN-AcetylglucosaminyltransferasesPhosphorylationRatsRats, Sprague-DawleySirtuin 1tau ProteinsAcetylglucosamineCyclic AMP Response Element-Binding ProteinN-AcetylglucosaminyltransferasesO-GlcNAc transferaseSIRT1 protein, humanSirtuin 1tau ProteinsAlzheimer’s diseaseO-GlcNAcylation of tauOGTphosphorylation of tauSIRT1

Identifiers

PMID32310828
PMCPMC7202539
OpenAlexW3016438533

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.