Evidence map›Paper›PMID 36690633›Full record

ReviewCell death discovery2023

NEDD8-conjugating enzyme E2s: critical targets for cancer therapy.

Lisha Zhou, Xiongzhi Lin, Jin Zhu, Luyi Zhang, Siyuan Chen, Hui Yang, Lijun Jia, Baofu Chen

Open access · goldAbstract readReview
In one paragraph

Review in Cell death discovery, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 26 citations in OpenAlex.

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  16. Neddylation modification stabilizes LC3B by antagonizing its ubiquitin-mediated degradation and promoting autophagy in skin.Proceedings of the National Academy of Sciences of the United States of America · 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 5 institutions in 1 country.

Lisha Zhou *Taizhou Central Hospital (Taizhou University Hospital), Taizhou University, Taizhou, Zhejiang, China. lishazhou@tzc.edu.cn.ORCID http://orcid.org/0000-0001-7038-4984
Xiongzhi Lin *Graduate School of Medicine, Hebei North University, Zhangjiakou, Hebei, China.
Jin Zhu *Department of Surgical Oncology, Jiangxi Cancer Hospital, Nanchang, Jiangxi, China.
Luyi ZhangTaizhou Central Hospital (Taizhou University Hospital), Taizhou University, Taizhou, Zhejiang, China.
Siyuan ChenTaizhou Central Hospital (Taizhou University Hospital), Taizhou University, Taizhou, Zhejiang, China.
Hui YangDepartment of Neurosurgery, Huashan Hospital, Fudan University, Shanghai, China. hui_yang@fudan.edu.cn.ORCID http://orcid.org/0000-0002-2865-5311
Lijun JiaCancer Institute of Traditional Chinese Medicine, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China. ljjia@shutcm.edu.cn.ORCID http://orcid.org/0000-0001-9902-8246
Baofu ChenTaizhou Central Hospital (Taizhou University Hospital), Taizhou University, Taizhou, Zhejiang, China. chenbf@tzc.edu.cn.ORCID http://orcid.org/0000-0002-9185-8103
Taizhou Central Hospital · CNFudan University · CNHebei North University · CNJiangxi Provincial Cancer Hospital · CNShanghai University of Traditional Chinese Medicine · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 81820108022National Natural Science Foundation of China (National Science Foundation of China) 81871870, 82073069National Natural Science Foundation of China (National Science Foundation of China) 82073166, 82273203Natural Science Foundation of Zhejiang Province (Zhejiang Provincial Natural Science Foundation) LY21H160008
6 · The paper itself

Abstract

NEDD8-conjugating enzymes, E2s, include the well-studied ubiquitin-conjugating enzyme E2 M (UBE2M) and the poorly characterized ubiquitin-conjugating enzyme E2 F (UBE2F). UBE2M and UBE2F have distinct and prominent roles in catalyzing the neddylation of Cullin or non-Cullin substrates. These enzymes are overexpressed in various malignancies, conferring a worse overall survival. Targeting UBE2M to influence tumor growth by either modulating several biological responses of tumor cells (such as DNA-damage response, apoptosis, or senescence) or regulating the anti-tumor immunity holds strong therapeutic potential. Multiple inhibitors that target the interaction between UBE2M and defective cullin neddylation protein 1 (DCN1), a co-E3 for neddylation, exhibit promising anti-tumor effects. By contrast, the potential benefits of targeting UBE2F are still to be explored. It is currently reported to inhibit apoptosis and then induce cell growth; hence, targeting UBE2F serves as an effective chemo-/radiosensitizing strategy by triggering apoptosis. This review highlights the most recent advances in the roles of UBE2M and UBE2F in tumor progression, indicating these E2s as two promising anti-tumor targets.

Identifiers

PMID36690633
PMCPMC9871045
OpenAlexW4317746830

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.