Evidence map›Paper›PMID 38710693›Full record

ArticleNature communications2024

A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3

Weize Wang, Ling Liang, Zonglin Dai, Peng Zuo, Shang Yu, Yishuo Lu, Dian Ding, Hongyi Chen, Hui Shan, Yan Jin and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Integrating Senescence and Oxidative Stress in Cardiac Disease.International journal of molecular sciences · 2025
    Review
  8. Article
  9. Article
  10. TheGenes · 2025
    Article
  11. 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

12 authors.

Weize Wang *Institute of Precision Medicine, Peking University Shenzhen Hospital, Shenzhen, 518036, China.ORCID http://orcid.org/0000-0001-7258-0356
Ling Liang *Department of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China. liangling@bjmu.edu.cn.ORCID http://orcid.org/0000-0002-3115-2563
Zonglin Dai *Institute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China.ORCID http://orcid.org/0000-0002-4005-1297
Peng ZuoInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China.ORCID http://orcid.org/0000-0002-5631-9534
Shang YuDepartment of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China.
Yishuo LuPeking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.ORCID http://orcid.org/0000-0002-4557-0686
Dian DingInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China.ORCID http://orcid.org/0000-0003-1764-2256
Hongyi ChenPeking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.
Hui ShanInstitute of Precision Medicine, Peking University Shenzhen Hospital, Shenzhen, 518036, China.
Yan JinInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China.
Youdong MaoPeking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.ORCID http://orcid.org/0000-0001-9302-2257
Yuxin YinInstitute of Precision Medicine, Peking University Shenzhen Hospital, Shenzhen, 518036, China. yinyuxin@hsc.pku.edu.cn.ORCID http://orcid.org/0000-0003-4102-0043

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31800626National Natural Science Foundation of China (National Science Foundation of China) 32171224National Natural Science Foundation of China (National Science Foundation of China) 81874235National Natural Science Foundation of China (National Science Foundation of China) 82030081
6 · The paper itself

Abstract

The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assembly is required for its ligase activity remains elusive. Here, we report the cryo-EM structure of the dimeric CRL3

Indexed as

Amino Acid MotifsCryoelectron MicroscopyCullin ProteinsReceptors, Interleukin-17UbiquitinationUbiquitin-Protein LigasesConserved SequenceHEK293 CellsHumansModels, MolecularProtein BindingProtein MultimerizationCUL3 protein, humanCullin ProteinsIL17RB protein, humanReceptors, Interleukin-17Ubiquitin-Protein Ligases

Identifiers

PMID38710693
PMCPMC11074293

What Socratic 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 Socratic graph.