Evidence map›Paper›PMID 28225593›Full record

ArticleACS nano2017

Programmed Self-Assembly of Hierarchical Nanostructures through Protein-Nanoparticle Coengineering.

Rubul Mout, Gulen Yesilbag Tonga, Li-Sheng Wang, Moumita Ray, Trinava Roy, Vincent M Rotello

Abstract read
In one paragraph

Article in ACS nano, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
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  11. Review
  12. Cytosolic Delivery of Functional ProteinsACS applied materials & interfaces · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Self-assembly as a key player for materials nanoarchitectonics.Science and technology of advanced materials · 2019
    Review
  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

6 authors.

Rubul MoutDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.ORCID 0000-0001-6125-5873
Gulen Yesilbag TongaDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.
Li-Sheng WangDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.
Moumita RayDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.
Trinava RoyDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.
Vincent M RotelloDepartment of Chemistry, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.ORCID 0000-0002-5184-5439

Funding

Recognition and Presentation of Alpha Helices using Nanoparticle ReceptorsR01GM077173 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ROTELLO, VINCENT M. · 2007 to 2018
$3.7M
NIGMS NIH HHS R01 GM077173
6 · The paper itself

Abstract

Hierarchical organization of macromolecules through self-assembly is a prominent feature in biological systems. Synthetic fabrication of such structures provides materials with emergent functions. Here, we report the fabrication of self-assembled superstructures through coengineering of recombinant proteins and nanoparticles. These structures feature a highly sophisticated level of multilayered hierarchical organization of the components: individual proteins and nanoparticles coassemble to form discrete assemblies that collapse to form granules, which then further self-organize to generate superstructures with sizes of hundreds of nanometers. The components within these superstructures are dynamic and spatially reorganize in response to environmental influences. The precise control over the molecular organization of building blocks imparted by this protein-nanoparticle coengineering strategy provides a method for creating hierarchical hybrid materials.

Indexed as

Protein EngineeringFluorescenceGreen Fluorescent ProteinsMacromolecular SubstancesNanostructuresParticle SizeRecombinant ProteinsSurface PropertiesGreen Fluorescent ProteinsMacromolecular SubstancesRecombinant Proteinsbiomimetic self-assemblygold nanoparticlehierarchical assemblymolecular organizationprotein engineering

Identifiers

PMID28225593
PMCPMC5848079

What OpenQuestion holds

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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.