Evidence map›Paper›PMID 38340287›Full record

ArticleJournal of applied genetics2024

Peptidylprolyl isomerase D circular RNA sensitizes breast cancer to trastuzumab through remodeling HER2 N4-acetylcytidine modification.

Shengting Wang, Qian Li, Yufang Wang, Xiaoming Li, Xinghua Feng, Yuxuan Wei, Jiaman Wang, Xin Zhou

Abstract read
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Article in Journal of applied genetics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 7 citations in OpenAlex.

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  6. The mechanism of ncRNA in trastuzumab resistance in HER2-positive tumors.Medical oncology (Northwood, London, England) · 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

8 authors at 1 institution in 1 country.

Shengting WangClinical Medical Center, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China. stwang@peihua.edu.cn.
Qian LiClinical Medical Center, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Yufang WangClinical Medical Center, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Xiaoming LiClinical Medical Center, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Xinghua FengClinical Medical Center, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Yuxuan WeiDepartment of Stomatology Technology, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Jiaman WangDepartment of Stomatology Technology, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Xin ZhouDepartment of Stomatology Technology, Xi'an Peihua University, Xi'an, 710125, Shaanxi, China.
Xi'an Peihua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human epidermal growth factor receptor 2 (HER2) overexpression and activation are crucial for trastuzumab resistance in HER2-positive breast cancer; however, the potential regulatory mechanism of HER2 is still largely undetermined. In this study, a novel circular RNA derived from peptidylprolyl isomerase D (PPID) is identified as a negative regulator of trastuzumab resistance. Circ-PPID is highly stable and significantly downregulated in trastuzumab-resistant cells and tissues. Restoration of circ-PPID markedly enhances HER2-positive breast cell sensitivity to trastuzumab in vitro and in vivo. Circ-PPID directly binds to N-acetyltransferase 10 (NAT10) in the nucleus and blocks the interaction between NAT10 and HER2 mRNA, reducing N4-acetylcytidine (ac4C) modification on HER2 exon 25, leading to HER2 mRNA decay. Intriguingly, the subcellular localization of circ-PPID differs between trastuzumab-sensitive and -resistant cells. Circ-PPID in trastuzumab-resistant cells is located more in the cytoplasm, mainly due to the upregulation of Exportin 4 (XPO4), which results in the loss of spatial conditions for circ-PPID to bind to nuclear NAT10. Taken together, our data suggest that circ-PPID is a previously unappreciated ac4C-dependent HER2 epigenetic regulator, providing a promising therapeutic direction for overcoming trastuzumab resistance in clinical setting.

Indexed as

Breast NeoplasmsCytidineDrug Resistance, NeoplasmErb-b2 Receptor Tyrosine KinasesRNA, CircularTrastuzumabAnimalsCell Line, TumorFemaleGene Expression Regulation, NeoplasticHumansMiceN-Terminal AcetyltransferasesRNA StabilityCytidineERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesN-acetylcytidineNAT10 protein, humanN-Terminal AcetyltransferasesRNA, CircularTrastuzumabCircular RNAHER2-positive breast cancerN4-acetylcytidine modificationNuclear exportTrastuzumab resistance

Identifiers

PMID38340287
OpenAlexW4391719470

What OpenQuestion holds

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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.