Evidence map›Paper›PMID 35256949›Full record

ArticleActa pharmaceutica Sinica. B2022

Histone deacetylase inhibitors inhibit cervical cancer growth through Parkin acetylation-mediated mitophagy.

Xin Sun, Yuhan Shu, Guiqin Ye, Caixia Wu, Mengting Xu, Ruilan Gao, Dongsheng Huang, Jianbin Zhang

Open access · diamondAbstract read
In one paragraph

Article in Acta pharmaceutica Sinica. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.5field-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

56 citing papers in PubMed, 76 citations in OpenAlex.

  1. Research progress on lysine acetylation (Review).International journal of molecular medicine · 2026
    Review
  2. The histone deacetylase family in health and disease.Signal transduction and targeted therapy · 2026
    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

8 authors at 4 institutions in 1 country.

Xin SunDepartment of Oncology, Cancer Center of Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou 310014, China.
Yuhan ShuCollege of Biomedical Engineering & Instrument Science, Zhejiang University, Hangzhou 310028, China.
Guiqin YeKey Laboratory of Tumor Molecular Diagnosis and Individualized Medicine of Zhejiang Province, Hangzhou Medical College, Hangzhou 310014, China.
Caixia WuClinical Research Institute, Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou 310014, China.
Mengting XuCollege of Biomedical Engineering & Instrument Science, Zhejiang University, Hangzhou 310028, China.
Ruilan GaoDepartment of Hematology, the First Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou 310006, China.
Dongsheng HuangKey Laboratory of Tumor Molecular Diagnosis and Individualized Medicine of Zhejiang Province, Hangzhou Medical College, Hangzhou 310014, China.
Jianbin ZhangClinical Research Institute, Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou 310014, China.
Zhejiang Provincial People's Hospital · CNHangzhou Medical College · CNZhejiang University · CNZhejiang Chinese Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkin, an E3 ubiquitin ligase, plays a role in maintaining mitochondrial homeostasis through targeting damaged mitochondria for mitophagy. Accumulating evidence suggests that the acetylation modification of the key mitophagy machinery influences mitophagy level, but the underlying mechanism is poorly understood. Here, our study demonstrated that inhibition of histone deacetylase (HDAC) by treatment of HDACis activates mitophagy through mediating Parkin acetylation, leading to inhibition of cervical cancer cell proliferation. Bioinformatics analysis shows that Parkin expression is inversely correlated with HDAC2 expression in human cervical cancer, indicating the low acetylation level of Parkin. Using mass spectrometry, Parkin is identified to interact with two upstream molecules, acetylase acetyl-CoA acetyltransferase 1 (ACAT1) and deacetylase HDAC2. Under treatment of suberoylanilide hydroxamic acid (SAHA), Parkin is acetylated at lysine residues 129, 220 and 349, located in different domains of Parkin protein. In

Indexed as

ACAT1ACAT1, acetyl-CoA acetyltransferase 1AcetylationCCK-8, cell counting kit-8Cervical cancerCOXⅣ, cytochrome c oxidase ⅣGAPDH, glyceraldehyde-3-phosphate dehydrogenaseHDAC2HDAC, histone deacetylaseHIF-1α, hypoxia inducible factor-1αHSP60, heat shock protein 60 kDaLC3, microtubule-associated proteins 1A/1B light chain 3MFN2, mitofusion 2MitophagyMS, mass spectrometryPARK2, ParkinParkinPINK1, PTEN induced putative kinase 1ROS, reactive oxygen speciesSAHA, suberoylanilide hydroxamic acidTIM23, translocase of the inner membrane 23TOMM20, translocase of outer mitochondrial membrane 20TSA, trichostatin ATumor suppressionUbiquitinationULK1, unc-51 like autophagy activating kinase 1VDAC1, voltage-dependent anion-selective channel protein 1

Identifiers

PMID35256949
PMCPMC8897022
OpenAlexW3186907381

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.