Evidence map›Paper›PMID 29484374›Full record

ReviewInternational journal of oncology2018

The post-translational modification, SUMOylation, and cancer (Review).

Zhi-Jian Han, Yan-Hu Feng, Bao-Hong Gu, Yu-Min Li, Hao Chen

Open access · hybridAbstract readReview
In one paragraph

Review in International journal of oncology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 249 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
249citing papers in PubMed, 1 pooled it
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

249 citing papers in PubMed, 1 synthesis or guideline pooled it, 328 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. A RAC1 SUMOylation switch governs breast cancer metastasis.Signal transduction and targeted therapy · 2026
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189 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

5 authors at 2 institutions in 1 country.

Zhi-Jian HanKey Laboratory of the Digestive System Tumors of Gansu Province, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.
Yan-Hu FengKey Laboratory of the Digestive System Tumors of Gansu Province, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.
Bao-Hong GuDepartment of General Surgery, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.
Yu-Min LiDepartment of General Surgery, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.
Hao ChenDepartment of General Surgery, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.
Lanzhou University Second Hospital · CNLanzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis. Four SUMO isoforms have been identified, which are SUMO1, SUMO2/3 and SUMO4. The small ubiquitin-like modifier (SUMO) pathway is conserved in all eukaryotes and plays pivotal roles in the regulation of gene expression, cellular signaling and the maintenance of genomic integrity. The SUMO catalytic cycle includes maturation, activation, conjugation, ligation and de-modification. The dysregulation of the SUMO system is associated with a number of diseases, particularly cancer. SUMOylation is widely involved in carcinogenesis, DNA damage response, cancer cell proliferation, metastasis and apoptosis. SUMO can be used as a potential therapeutic target for cancer. In this review, we briefly outline the basic concepts of the SUMO system and summarize the involvement of SUMO proteins in cancer cells in order to better understand the role of SUMO in human disease.

Indexed as

NeoplasmsAnimalsHumansProtein Processing, Post-TranslationalSmall Ubiquitin-Related Modifier ProteinsSumoylationSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID29484374
PMCPMC5843405
OpenAlexW2790018833

What OpenQuestion 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 OpenQuestion graph.