Evidence map›Paper›PMID 27249579›Full record

ArticleNature communications2016

Geometrical assembly of ultrastable protein templates for nanomaterials.

Dominic J Glover, Lars Giger, Steve S Kim, Rajesh R Naik, Douglas S Clark

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Modular repeat protein sculpting using rigid helical junctions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
  16. Protein-Mediated Biotemplating on the Nanoscale.Biomimetics (Basel, Switzerland) · 2017
    Review
  17. 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.

Dominic J GloverDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, USA.
Lars GigerDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, USA.
Steve S KimMaterials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Dayton, Ohio 45433, USA.
Rajesh R NaikMaterials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Dayton, Ohio 45433, USA.
Douglas S ClarkDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fabrication of nanoscale devices requires architectural templates on which to position functional molecules in complex arrangements. Protein scaffolds are particularly promising templates for nanomaterials due to inherent molecular recognition and self-assembly capabilities combined with genetically encoded functionalities. However, difficulties in engineering protein quaternary structure into stable and well-ordered shapes have hampered progress. Here we report the development of an ultrastable biomolecular construction kit for the assembly of filamentous proteins into geometrically defined templates of controllable size and symmetry. The strategy combines redesign of protein-protein interaction specificity with the creation of tunable connector proteins that govern the assembly and projection angles of the filaments. The functionality of these nanoarchitectures is illustrated by incorporation of nanoparticles at specific locations and orientations to create hybrid materials such as conductive nanowires. These new structural components facilitate the manufacturing of nanomaterials with diverse shapes and functional properties over a wide range of processing conditions.

Indexed as

Archaeal ProteinsCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsKineticsMetal NanoparticlesMethanocaldococcusMolecular ChaperonesMolecular Dynamics SimulationNanotechnologyNanowiresProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein Interaction Domains and MotifsArchaeal ProteinsMolecular ChaperonesprefoldinRecombinant Proteins

Identifiers

PMID27249579
PMCPMC4895442

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.