Evidence map›Paper›PMID 33139936›Full record

ArticleNature nanotechnology2021

A DNA-nanoassembly-based approach to map membrane protein nanoenvironments.

Elena Ambrosetti, Giulio Bernardinelli, Ian Hoffecker, Leonard Hartmanis, Georges Kiriako, Ario de Marco, Rickard Sandberg, Björn Högberg, Ana I Teixeira

Abstract read
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In one paragraph

Article in Nature nanotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 13% 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, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Interactions of the DNA Nanostructure with Silane-Based Self-Assembled Monolayers.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  4. Production of Antibody Fragments Suitable for 1:1, Site-Specific Labeling.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Proximity-activated DNA scanning encoded sequencing for massive access to membrane proteins nanoscale organization.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Applications of DNA-Functionalized Proteins.International journal of molecular sciences · 2021
    Review
  17. Review
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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 2 countries.

Elena AmbrosettiDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Giulio BernardinelliDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-3394-7976
Ian HoffeckerDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Leonard HartmanisDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Georges KiriakoDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-6117-6286
Ario de MarcoLaboratory for Environmental and Life Sciences, University of Nova Gorica, Nova Gorica, Slovenia.
Rickard SandbergDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-6473-1740
Björn HögbergDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-2715-7887
Ana I TeixeiraDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. ana.teixeira@ki.se.ORCID http://orcid.org/0000-0001-8169-8815
Karolinska Institutet · SEUniversity of Nova Gorica · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most proteins at the plasma membrane are not uniformly distributed but localize to dynamic domains of nanoscale dimensions. To investigate their functional relevance, there is a need for methods that enable comprehensive analysis of the compositions and spatial organizations of membrane protein nanodomains in cell populations. Here we describe the development of a non-microscopy-based method for ensemble analysis of membrane protein nanodomains. The method, termed nanoscale deciphering of membrane protein nanodomains (NanoDeep), is based on the use of DNA nanoassemblies to translate membrane protein organization information into a DNA sequencing readout. Using NanoDeep, we characterized the nanoenvironments of Her2, a membrane receptor of critical relevance in cancer. Importantly, we were able to modulate by design the inventory of proteins analysed by NanoDeep. NanoDeep has the potential to provide new insights into the roles of the composition and spatial organization of protein nanoenvironments in the regulation of membrane protein function.

Indexed as

BiochemistryCell Line, TumorDNADNA, Single-StrandedErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFemaleHigh-Throughput Nucleotide SequencingHumansMembrane ProteinsNanotechnologyOligonucleotidesProtein DomainsReceptor, ErbB-3Recombinant Fusion ProteinsReproducibility of ResultsDNADNA, Single-StrandedEGFR protein, humanERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesERBB3 protein, humanErbB ReceptorsMembrane ProteinsOligonucleotidesReceptor, ErbB-3Recombinant Fusion Proteins

Identifiers

PMID33139936
OpenAlexW3097963065

What OpenQuestion holds

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Read underepoch 390

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.