Evidence map›Paper›PMID 37564410›Full record

ArticleChemical science2023

A highly sensitive nanochannel device for the detection of SUMO1 peptides.

Yue Qin, Xiaoyu Zhang, Yanling Song, Bowen Zhong, Lu Liu, Dongdong Wang, Yahui Zhang, Wenqi Lu, Xinjia Zhao, Zhiqi Jia and 3 more

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Biosensing With Nanofluidics.Exploration (Beijing, China) · 2026
    Review
  3. Review
  4. Review
  5. SENP1 inhibits aerobic glycolysis in AβCell biology and toxicology · 2025
    Article
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

13 authors at 2 institutions in 1 country.

Yue QinCollege of Pharmaceutical and Biological Engineering, Shenyang University of Chemical Technology No. 11 Street, Economic and Technological Development Zone Shenyang 110142 P. R. China.
Xiaoyu ZhangCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0001-9428-0813
Yanling SongCollege of Pharmaceutical and Biological Engineering, Shenyang University of Chemical Technology No. 11 Street, Economic and Technological Development Zone Shenyang 110142 P. R. China.
Bowen ZhongCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.
Lu LiuCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.
Dongdong WangCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.
Yahui ZhangCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0003-1509-0670
Wenqi LuCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.
Xinjia ZhaoCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0001-5101-7273
Zhiqi JiaCollege of Pharmaceutical and Biological Engineering, Shenyang University of Chemical Technology No. 11 Street, Economic and Technological Development Zone Shenyang 110142 P. R. China.
Minmin LiCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0003-0596-5445
Lihua ZhangCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0003-2543-1547
Guangyan QingCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 P. R. China qinggy@dicp.ac.cn lihuazhang@dicp.ac.cn.ORCID https://orcid.org/0000-0002-4888-9318
Dalian Institute of Chemical Physics · CNShenyang University of Chemical Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation is an important and highly dynamic post-translational modification (PTM) process of protein, and its disequilibrium may cause various diseases, such as cancers and neurodegenerative disorders. SUMO proteins must be accurately detected to understand disease states and develop effective drugs. Reliable antibodies against SUMO2/3 are commercially available; however, efficient detectors are yet to be developed for SUMO1, which has only 50% homology with SUMO2 and SUMO3. Here, using phage display technology, we identified two cyclic peptide (CP) sequences that could specifically bind to the terminal dodecapeptide sequence of SUMO1. Then we combined the CPs and polyethylene terephthalate conical nanochannel films to fabricate a nanochannel device highly sensitive towards the SUMO1 terminal peptide and protein; sensitivity was achieved by ensuring marked variations in both transmembrane ionic current and Faraday current. The satisfactory SUMO1-sensing ability of this device makes it a promising tool for the time-point monitoring of the SENP1 enzyme-catalyzed de-SUMOylation reaction and cellular imaging. This study not only solves the challenge of SUMO1 precise recognition that could promote SUMO1 proteomics analysis, but also demonstrates the good potential of the nanochannel device in monitoring of enzymes and discovery of effective drugs.

Identifiers

PMID37564410
PMCPMC10411628
OpenAlexW4384274057

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.