Evidence map›Paper›PMID 26331548›Full record

ArticleNature2015

Computational design of co-assembling protein-DNA nanowires.

Yun Mou, Jiun-Yann Yu, Timothy M Wannier, Chin-Lin Guo, Stephen L Mayo

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Modulation of Proteinoid Electrical Spiking Activity with Magnetic Nanoparticles.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  3. Programming crystallization kinetics of self-assembled DNA crystals with 5-methylcytosine modification.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. A Colorimetric/Fluorescent Dual-Mode Aptasensor forFoods (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Article
  8. Assessing and enhancing foldability in designed proteins.Protein science : a publication of the Protein Society · 2022
    Article
  9. Article
  10. Review
  11. Protein Assembly by Design.Chemical reviews · 2021
    Review
  12. Redefining Protein Interfaces within Protein Single Crystals with DNA.Journal of the American Chemical Society · 2021
    Article
  13. Strategies to Build Hybrid Protein-DNA Nanostructures.Nanomaterials (Basel, Switzerland) · 2021
    Review
  14. Supramolecular Architectures of Nucleic Acid/Peptide Hybrids.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Nanowired Bioelectric Interfaces.Chemical reviews · 2019
    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

5 authors at 1 institution in 1 country.

Yun MouDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Jiun-Yann YuDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Timothy M WannierDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Chin-Lin GuoDivision of Engineering and Applied Science, California Institute of Technology, Pasadena, California 91125, USA.
Stephen L MayoDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
California Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular self-assemblies are of great interest to nanotechnologists because of their functional versatility and their biocompatibility. Over the past decade, sophisticated single-component nanostructures composed exclusively of nucleic acids, peptides and proteins have been reported, and these nanostructures have been used in a wide range of applications, from drug delivery to molecular computing. Despite these successes, the development of hybrid co-assemblies of nucleic acids and proteins has remained elusive. Here we use computational protein design to create a protein-DNA co-assembling nanomaterial whose assembly is driven via non-covalent interactions. To achieve this, a homodimerization interface is engineered onto the Drosophila Engrailed homeodomain (ENH), allowing the dimerized protein complex to bind to two double-stranded DNA (dsDNA) molecules. By varying the arrangement of protein-binding sites on the dsDNA, an irregular bulk nanoparticle or a nanowire with single-molecule width can be spontaneously formed by mixing the protein and dsDNA building blocks. We characterize the protein-DNA nanowire using fluorescence microscopy, atomic force microscopy and X-ray crystallography, confirming that the nanowire is formed via the proposed mechanism. This work lays the foundation for the development of new classes of protein-DNA hybrid materials. Further applications can be explored by incorporating DNA origami, DNA aptamers and/or peptide epitopes into the protein-DNA framework presented here.

Indexed as

Computer SimulationDrug DesignBinding SitesCrystallizationCrystallography, X-RayDNADrosophila ProteinsHomeodomain ProteinsMicroscopy, Atomic ForceMicroscopy, FluorescenceModels, MolecularNanotechnologyNanowiresProtein MultimerizationTranscription FactorsDNADrosophila ProteinsEn protein, DrosophilaHomeodomain ProteinsTranscription Factors

Identifiers

PMID26331548
OpenAlexW1800483474

What OpenQuestion holds

Textmetadata
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.