Evidence map›Paper›PMID 29331584›Full record

ReviewCellular signalling2018

Protein neddylation and its alterations in human cancers for targeted therapy.

Lisha Zhou, Wenjuan Zhang, Yi Sun, Lijun Jia

Abstract readReview
In one paragraph

Review in Cellular signalling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

145 citing papers in PubMed, 219 citations in OpenAlex.

  1. Trial
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  8. UBE2M deficiency in alveolar macrophages promotes emphysema through HIF-2α/MMP12 axis.Chinese medical journal pulmonary and critical care medicine · 2026
    Article
  9. Article
  10. Discovery of SKP2-Recruiting PROTACs for Target Protein Degradation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  11. Review
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85 more citing papers are in PubMed but not listed here.

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

4 authors at 4 institutions in 3 countries.

Lisha ZhouCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai 200032, China.
Wenjuan ZhangCancer Institute, Fudan University Shanghai Cancer Center; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai 200032, China. Electronic address: 13211230018@fudan.edu.cn.
Yi SunInstitute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 30029, China; Division of Radiation and Cancer Biology, Department of Radiation Oncology, University of Michigan, 1301 Catherine Street, Ann Arbor, MI 48109, USA. Electronic address: yisun@zju.edu.cn.
Lijun JiaCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai 200032, China. Electronic address: ljjia@shutcm.edu.cn.
Fudan University Shanghai Cancer Center · CNLonghua Hospital Shanghai University of Traditional Chinese Medicine · CNShanghai University of Traditional Chinese Medicine · CNUniversity of Michigan–Ann Arbor · US

Funding

The role of FBXW2 as a novel lung tumor suppressor that cross-talks with oncogenic beta-TrCP and SKP2R01CA156744 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORGAN, MEREDITH A · 2011 to 2020
$3.4M
Role of SAG/RBX2 E3 Ubiquitin Ligase in Skin CarcinogenesisR01CA171277 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2013 to 2017
$1.6M
NCI NIH HHS R01 CA156744NCI NIH HHS R01 CA171277
6 · The paper itself

Abstract

Neddylation, a post-translational modification that conjugates an ubiquitin-like protein NEDD8 to substrate proteins, is an important biochemical process that regulates protein function. The best-characterized substrates of neddylation are the cullin subunits of Cullin-RING ligases (CRLs), which, as the largest family of E3 ubiquitin ligases, control many important biological processes, including tumorigenesis, through promoting ubiquitylation and subsequent degradation of a variety of key regulatory proteins. Recently, increasing pieces of experimental evidence strongly indicate that the process of protein neddylation modification is elevated in multiple human cancers, providing sound rationale for its targeting as an attractive anticancer therapeutic strategy. Indeed, neddylation inactivation by MLN4924 (also known as pevonedistat), a small molecule inhibitor of E1 NEDD8-activating enzyme currently in phase I/II clinical trials, exerts significant anticancer effects by inducing cell cycle arrest, apoptosis, senescence and autophagy in a cell-type and context dependent manner. Here, we summarize the latest progresses in the field with a major focus on preclinical studies in validation of neddylation modification as a promising anticancer target.

Indexed as

Molecular Targeted TherapyApoptosisAutophagyCell Cycle CheckpointsCellular SenescenceCyclopentanesHumansNeoplasmsProtein Processing, Post-TranslationalPyrimidinesUbiquitin-Activating EnzymesUbiquitin-Protein LigasesCULL-RING ligase, humanCyclopentanesNAE protein, humanpevonedistatPyrimidinesUbiquitin-Activating EnzymesUbiquitin-Protein LigasesApoptosisAutophagyCancer targetCell cycle arrestCullin RING ligaseMLN4924NeddylationSenescence

Identifiers

PMID29331584
PMCPMC5829022
OpenAlexW2784179760

What OpenQuestion holds

Textmetadata
LicenceTDM
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.