Evidence map›Paper›PMID 25033911›Full record

ArticleNature communications2014

Self-assembly and modular functionalization of three-dimensional crystals from oppositely charged proteins.

Ville Liljeström, Joona Mikkilä, Mauri A Kostiainen

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
14.5field-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

39 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  5. Article
  6. Protein Cage Directed Assembly of Binary Nanoparticle Superlattices.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Colloidal superionic conductors.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Morphology control in crystalline nanoparticle-polymer aggregates.Annals of the New York Academy of Sciences · 2021
    Article
  16. Protein Assembly by Design.Chemical reviews · 2021
    Review
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Ville Liljeström1] Biohybrid Materials Group, Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland [2] Molecular Materials Group, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Joona Mikkilä1] Biohybrid Materials Group, Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland [2] Molecular Materials Group, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Mauri A KostiainenBiohybrid Materials Group, Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland.
Aalto University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multicomponent crystals and nanoparticle superlattices are a powerful approach to integrate different materials into ordered nanostructures. Well-developed, especially DNA-based, methods for their preparation exist, yet most techniques concentrate on molecular and synthetic nanoparticle systems in non-biocompatible environment. Here we describe the self-assembly and characterization of binary solids that consist of crystalline arrays of native biomacromolecules. We electrostatically assembled cowpea chlorotic mottle virus particles and avidin proteins into heterogeneous crystals, where the virus particles adopt a non-close-packed body-centred cubic arrangement held together by avidin. Importantly, the whole preparation process takes place at room temperature in a mild aqueous medium allowing the processing of delicate biological building blocks into ordered structures with lattice constants in the nanometre range. Furthermore, the use of avidin-biotin interaction allows highly selective pre- or post-functionalization of the protein crystals in a modular way with different types of functional units, such as fluorescent dyes, enzymes and plasmonic nanoparticles.

Indexed as

AvidinBiotinBromovirusCrystallizationDendrimersFluorescent DyesGoldMicroscopy, Electron, TransmissionNanostructuresProteinsScattering, Small AngleSpectrophotometry, UltravioletStatic ElectricityAvidinBiotinDendrimersFluorescent DyesGoldProteins

Identifiers

PMID25033911
PMCPMC4109007
OpenAlexW2004739063

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.