Evidence map›Paper›PMID 30113093›Full record

ArticleProtein science : a publication of the Protein Society2018

Elaborating a coiled-coil-assembled octahedral protein cage with additional protein domains.

Ajitha S Cristie-David, Philipp Koldewey, Ben A Meinen, James C A Bardwell, E Neil G Marsh

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. Protein Assembly by Design.Chemical reviews · 2021
    Review
  3. Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021
    Review
  4. Review
  5. Metal-dependent assembly of a protein nano-cage.Protein science : a publication of the Protein Society · 2019
    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

5 authors.

Ajitha S Cristie-DavidDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109.
Philipp KoldeweyDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, 48109.
Ben A MeinenDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, 48109.
James C A BardwellDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, 48109.
E Neil G MarshDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109.ORCID 0000-0003-1713-1683

Funding

Army Research Office W911NF-16-1-0147
6 · The paper itself

Abstract

De novo design of protein nano-cages has potential applications in medicine, synthetic biology, and materials science. We recently developed a modular, symmetry-based strategy for protein assembly in which short, coiled-coil sequences mediate the assembly of a protein building block into a cage. The geometry of the cage is specified by the combination of rotational symmetries associated with the coiled-coil and protein building block. We have used this approach to design well-defined octahedral and tetrahedral cages. Here, we show that the cages can be further elaborated and functionalized by the addition of another protein domain to the free end of the coiled-coil: in this case by fusing maltose-binding protein to an octahedral protein cage to produce a structure with a designed molecular weight of ~1.8 MDa. Importantly, the addition of the maltose binding protein domain dramatically improved the efficiency of assembly, resulting in ~ 60-fold greater yield of purified protein compared to the original cage design. This study shows the potential of using small, coiled-coil motifs as off-the-shelf components to design MDa-sized protein cages to which additional structural or functional elements can be added in a modular manner.

Indexed as

Protein DomainsProtein MultimerizationAmino AcidsAmino Acid SequenceCross-Linking ReagentsEscherichia coliMaltose-Binding ProteinsModels, MolecularMolecular WeightProtein FoldingAmino AcidsCross-Linking ReagentsMaltose-Binding Proteinscoiled coilscomputational modelingprotein designprotein nano-cages

Identifiers

PMID30113093
PMCPMC6201728

What OpenQuestion holds

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Registered trials

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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.