Evidence map›Paper›PMID 34183817›Full record

ArticleNature chemistry2021

Chemical profiling of DNA G-quadruplex-interacting proteins in live cells.

Xiaoyun Zhang, Jochen Spiegel, Sergio Martínez Cuesta, Santosh Adhikari, Shankar Balasubramanian

Open access · hybridAbstract read
In one paragraph

Article in Nature chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
9.1field-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

101 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. KRSC advances · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. CTCF directly binds G-quadruplex structures to regulate genome topology and gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Investigating Potential 5' UTR G-Quadruplexes Within NRF2 mRNA.Current issues in molecular biology · 2026
    Article
  20. Article

41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Xiaoyun Zhang *Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-4132-3573
Jochen Spiegel *Cancer Research UK Cambridge Institute, Li Ka Shing Centre, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-7641-1066
Sergio Martínez CuestaDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-9806-2805
Santosh AdhikariDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-1501-2106
Shankar BalasubramanianDepartment of Chemistry, University of Cambridge, Cambridge, UK. sb10031@cam.ac.uk.ORCID http://orcid.org/0000-0002-0281-5815
University of Cambridge · GBAstraZeneca (United Kingdom) · GB

Funding

Cancer Research UK 18618Cancer Research UK 19836Cancer Research UK 29214Cancer Research UK C9545/A19836Cancer Research UK C9681/A29214Wellcome TrustWellcome Trust 209441/Z/17/Z
6 · The paper itself

Abstract

DNA-protein interactions regulate critical biological processes. Identifying proteins that bind to specific, functional genomic loci is essential to understand the underlying regulatory mechanisms on a molecular level. Here we describe a co-binding-mediated protein profiling (CMPP) strategy to investigate the interactome of DNA G-quadruplexes (G4s) in native chromatin. CMPP involves cell-permeable, functionalized G4-ligand probes that bind endogenous G4s and subsequently crosslink to co-binding G4-interacting proteins in situ. We first showed the robustness of CMPP by proximity labelling of a G4 binding protein in vitro. Employing this approach in live cells, we then identified hundreds of putative G4-interacting proteins from various functional classes. Next, we confirmed a high G4-binding affinity and selectivity for several newly discovered G4 interactors in vitro, and we validated direct G4 interactions for a functionally important candidate in cellular chromatin using an independent approach. Our studies provide a chemical strategy to map protein interactions of specific nucleic acid features in living cells.

Indexed as

G-QuadruplexesAlkynesAminoquinolinesCell Line, TumorCross-Linking ReagentsDiazomethaneDNADNA-Binding ProteinsHEK293 CellsHumansLigandsProof of Concept StudyProtein BindingUltraviolet RaysAlkynesAminoquinolinesCross-Linking ReagentsDiazomethaneDNADNA-Binding ProteinsLigands

Identifiers

PMID34183817
PMCPMC8245323
OpenAlexW3163289953

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.