Evidence map›Paper›PMID 23839273›Full record

ArticleNature communications2013

Protein analysis by time-resolved measurements with an electro-switchable DNA chip.

Andreas Langer, Paul A Hampel, Wolfgang Kaiser, Jelena Knezevic, Thomas Welte, Valentina Villa, Makiko Maruyama, Matej Svejda, Simone Jähner, Frank Fischer and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

49 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Review
  3. DNA-Binding Properties of Iridium(III) Complexes Encompassing Design, Function and Biophysical Assessments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Rationally Designed DNA-Based Scaffolds and Switching Probes for Protein Sensing.Advances in biochemical engineering/biotechnology · 2024
    Review
  13. Article
  14. Review
  15. The Impact ofInternational journal of molecular sciences · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021
    Review
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 at 2 institutions in 1 country.

Andreas LangerChemistry Department and Walter Schottky Institute, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Paul A Hampel
Wolfgang Kaiser
Jelena Knezevic
Thomas Welte
Valentina Villa
Makiko Maruyama
Matej Svejda
Simone Jähner
Frank Fischer
Ralf Strasser
Ulrich Rant
Schott (Germany) · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Measurements in stationary or mobile phases are fundamental principles in protein analysis. Although the immobilization of molecules on solid supports allows for the parallel analysis of interactions, properties like size or shape are usually inferred from the molecular mobility under the influence of external forces. However, as these principles are mutually exclusive, a comprehensive characterization of proteins usually involves a multi-step workflow. Here we show how these measurement modalities can be reconciled by tethering proteins to a surface via dynamically actuated nanolevers. Short DNA strands, which are switched by alternating electric fields, are employed as capture probes to bind target proteins. By swaying the proteins over nanometre amplitudes and comparing their motional dynamics to a theoretical model, the protein diameter can be quantified with Angström accuracy. Alterations in the tertiary protein structure (folding) and conformational changes are readily detected, and even post-translational modifications are revealed by time-resolved molecular dynamics measurements.

Indexed as

Bacterial ProteinsChorionic GonadotropinDNAElectricityFungal ProteinsHumansImmunoglobulin GKineticsMolecular Dynamics SimulationOligonucleotide Array Sequence AnalysisProtein FoldingProtein Processing, Post-TranslationalProtein Structure, TertiaryTime FactorsBacterial ProteinsChorionic GonadotropinDNAFungal ProteinsImmunoglobulin G

Identifiers

PMID23839273
PMCPMC3719012
OpenAlexW1977702947

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.