Evidence map›Paper›PMID 31216068›Full record

ReviewElectrophoresis2019

MS-based strategies for identification of protein SUMOylation modification.

Zenghua Sheng, Xixi Wang, Yanni Ma, Dan Zhang, Yanfang Yang, Peng Zhang, Hongxia Zhu, Ningzhi Xu, Shufang Liang

Open access · hybridAbstract readReview
In one paragraph

Review in Electrophoresis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. A Landscape Analysis of Human SUMOylation.Molecular & cellular proteomics : MCP · 2026
    Article
  4. Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Identification ofInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Protein Sumoylation Is Crucial for Phagocytosis inInternational journal of molecular sciences · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
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

9 authors at 2 institutions in 1 country.

Zenghua ShengState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Xixi WangState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Yanni MaState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Dan ZhangState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Yanfang YangState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Peng ZhangDepartment of Urinary Surgery, West China Hospital, Sichuan University, Chengdu, Sichuan, P. R. China.
Hongxia ZhuLaboratory of Cell and Molecular Biology & State Key Laboratory of Molecular Oncology, Cancer Institute & Cancer Hospital, Chinese Academy of Medical Sciences, Beijing, P. R. China.
Ningzhi XuState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.
Shufang LiangState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu, P. R. China.ORCID 0000-0003-1000-7508
Sichuan University · CNChinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

The Role of Brain Stress Systems in the Prefrontal Cortex in Compulsive DrinkingR01AA020608 · NIAAA · SCRIPPS RESEARCH INSTITUTE, THE · PI GEORGE, OLIVIER · 2011 to 2015
$1.8M
Chengdu Science &Technology Program 2017-GH02-00062-HZHealth Commission of Sichuan Province 17ZD045National 863 High Tech Foundation 2014AA020608National Natural Science Foundation of China 31470810National Natural Sciences Foundation of China 31470810NIAAA NIH HHS R01 AA020608
6 · The paper itself

Abstract

Protein SUMOylation modification conjugated with small ubiquitin-like modifiers (SUMOs) is one kind of PTMs, which exerts comprehensive roles in cellular functions, including gene expression regulation, DNA repair, intracellular transport, stress responses, and tumorigenesis. With the development of the peptide enrichment approaches and MS technology, more than 6000 SUMOylated proteins and about 40 000 SUMO acceptor sites have been identified. In this review, we summarize several popular approaches that have been developed for the identification of SUMOylated proteins in human cells, and further compare their technical advantages and disadvantages. And we also introduce identification approaches of target proteins which are co-modified by both SUMOylation and ubiquitylation. We highlight the emerging trends in the SUMOylation field as well. Especially, the advent of the clustered regularly interspaced short palindromic repeats/ Cas9 technique will facilitate the development of MS for SUMOylation identification.

Indexed as

Mass SpectrometryPeptidesSmall Ubiquitin-Related Modifier ProteinsSumoylationCells, CulturedCRISPR-Cas SystemsGene EditingHumansModels, MolecularRecombinant Fusion ProteinsUbiquitinationPeptidesRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsMSPeptide enrichmentSmall ubiquitin-like modifiers (SUMOs)SUMOylationUbiquitylation

Identifiers

PMID31216068
PMCPMC6899701
OpenAlexW2950722044

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.