Evidence map›Paper›PMID 36101744›Full record

ReviewGenetics research2022

Multiple Roles of SIRT2 in Regulating Physiological and Pathological Signal Transduction.

Changhui Zhu, Xue Dong, Xiwei Wang, Yingying Zheng, Juanjuan Qiu, Yanling Peng, Jiajun Xu, Zhengbin Chai, Chunyan Liu

Open access · goldAbstract readReview
In one paragraph

Review in Genetics research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
7.0field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
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  17. Sirtuins Contribute to the Migraine-Stroke Connection.International journal of molecular sciences · 2025
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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

9 authors at 4 institutions in 1 country.

Changhui ZhuDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Weifang Medical University, Weifang 261053, Shandong, China.
Xue DongDepartment of Education, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan 250014, China.ORCID 0000-0002-8204-2268
Xiwei WangDepartment of Anesthesiology, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan 250014, China.ORCID 0000-0002-7904-131X
Yingying ZhengMedical Research Center, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan 250014, China.ORCID 0000-0003-3764-040X
Juanjuan QiuShandong First Medical University & Shandong Academy of Medical Sciences, Jinan 250014, China.ORCID 0000-0002-9752-4307
Yanling PengShandong First Medical University & Shandong Academy of Medical Sciences, Jinan 250014, China.ORCID 0000-0002-6754-4403
Jiajun XuShandong First Medical University & Shandong Academy of Medical Sciences, Jinan 250014, China.ORCID 0000-0002-6539-742X
Zhengbin ChaiDepartment of Clinical Laboratory Medicine, Shandong Public Health Clinical Center, Shandong University, Jinan 250102, China.ORCID 0000-0001-5392-6040
Chunyan LiuMedical Research Center, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan 250014, China.ORCID 0000-0002-0249-0379
Shandong Provincial QianFoShan Hospital · CNShandong First Medical University · CNShandong University of Traditional Chinese Medicine · CNWeifang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sirtuin 2 (SIRT2), as a member of the sirtuin family, has representative features of evolutionarily highly conserved nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase activity. In addition, SIRT2, as the only sirtuin protein colocalized with tubulin in the cytoplasm, has its own functions and characteristics. In recent years, studies have increasingly shown that SIRT2 can participate in the regulation of gene expression and regulate signal transduction in the metabolic pathway mainly through its post-translational modification of target genes; thus, SIRT2 has become a key centre in the metabolic pathway and participates in the pathological process of metabolic disorder-related diseases. In this paper, it is discussed that SIRT2 can regulate all aspects of gene expression, including epigenetic modification, replication, transcription and translation, and post-translational modification, which enables SIRT2 to participate in energy metabolism in life activities, and it is clarified that SIRT2 is involved in metabolic process-specific signal transduction mechanisms. Therefore, SIRT2 can be involved in metabolic disorder-related inflammation and oxidative stress, thereby triggering the occurrence of metabolic disorder-related diseases, such as neurodegenerative diseases, tumours, diabetes, and cardiovascular diseases. Currently, although the role of SIRT2 in some diseases is still controversial, given the multiple roles of SIRT2 in regulating physiological and pathological signal transduction, SIRT2 has become a key target for disease treatment. It is believed that with increasing research, the clinical application of SIRT2 will be promoted.

Indexed as

Neurodegenerative DiseasesSirtuin 2HumansOxidative StressProtein Processing, Post-TranslationalSignal TransductionSIRT2 protein, humanSirtuin 2

Identifiers

PMID36101744
PMCPMC9444453
OpenAlexW4293733572

What OpenQuestion holds

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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.