Evidence map›Paper›PMID 37626077›Full record

ArticleNature communications2023

Visualizing single-molecule conformational transition and binding dynamics of intrinsically disordered proteins.

Wenzhe Liu, Limin Chen, Dongbao Yin, Zhiheng Yang, Jianfei Feng, Qi Sun, Luhua Lai, Xuefeng Guo

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. DNA-Guided Robust Single-Protein Electronic Readout.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  12. 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

8 authors.

Wenzhe Liu *Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China.
Limin Chen *Peking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, P. R. China.
Dongbao YinBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China.
Zhiheng YangBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China.
Jianfei FengBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China.ORCID http://orcid.org/0000-0002-5399-8973
Qi SunBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China. qsun2015@pku.edu.cn.ORCID http://orcid.org/0000-0002-8519-657X
Luhua LaiBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China. lhlai@pku.edu.cn.ORCID http://orcid.org/0000-0002-8343-7587
Xuefeng GuoBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, 292 Chengfu Road, Haidian District, 100871, Beijing, P. R. China. guoxf@pku.edu.cn.ORCID http://orcid.org/0000-0001-5723-8528

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes and hold promise as drug targets. However, the dynamic nature of IDPs remains poorly understood. Here, we construct a single-molecule electrical nanocircuit based on silicon nanowire field-effect transistors (SiNW-FETs) and functionalize it with an individual disordered c-Myc bHLH-LZ domain to enable label-free, in situ, and long-term measurements at the single-molecule level. We use the device to study c-Myc interaction with Max and/or small molecule inhibitors. We observe the self-folding/unfolding process of c-Myc and reveal its interaction mechanism with Max and inhibitors through ultrasensitive real-time monitoring. We capture a relatively stable encounter intermediate ensemble of c-Myc during its transition from the unbound state to the fully folded state. The c-Myc/Max and c-Myc/inhibitor dissociation constants derived are consistent with other ensemble experiments. These proof-of-concept results provide an understanding of the IDP-binding/folding mechanism and represent a promising nanotechnology for IDP conformation/interaction studies and drug discovery.

Indexed as

Drug Delivery SystemsBasic-Leucine Zipper Transcription FactorsIntrinsically Disordered ProteinsModels, MolecularProtein BindingProtein Structure, TertiaryProto-Oncogene Proteins c-mycBasic-Leucine Zipper Transcription FactorsIntrinsically Disordered ProteinsMyc associated factor XProto-Oncogene Proteins c-myc

Identifiers

PMID37626077
PMCPMC10457384

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Registered trials

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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.