Evidence map›Paper›PMID 25972078›Full record

ArticleNature communications2015

Green fluorescent protein nanopolygons as monodisperse supramolecular assemblies of functional proteins with defined valency.

Young Eun Kim, Yu-na Kim, Jung A Kim, Ho Min Kim, Yongwon Jung

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024
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  6. Development of molecular sensors based on fluorescent proteins for polarized macrophages identification.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024
    Article
  7. Article
  8. Review
  9. Engineering highly stable variants of Corynactis californica green fluorescent proteins.Protein science : a publication of the Protein Society · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Aptamer-Array-Guided Protein Assembly Enhances Synthetic mRNA Switch Performance.Angewandte Chemie (International ed. in English) · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Protein Assembly by Design.Chemical reviews · 2021
    Review
  18. Article
  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

5 authors at 1 institution in 1 country.

Young Eun KimDepartment of Chemistry, KAIST, 291 Daehak-ro, Yuseong-gu, Daejeon 305-701, Korea.
Yu-na KimDepartment of Chemistry, KAIST, 291 Daehak-ro, Yuseong-gu, Daejeon 305-701, Korea.
Jung A KimGraduate School of Nanoscience and Technology, KAIST, Daejeon 305-701 Korea.
Ho Min KimGraduate School of Medical Science and Engineering, KAIST, Daejeon 305-701, Korea.
Yongwon JungDepartment of Chemistry, KAIST, 291 Daehak-ro, Yuseong-gu, Daejeon 305-701, Korea.
Korea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Supramolecular protein assemblies offer novel nanoscale architectures with molecular precision and unparalleled functional diversity. A key challenge, however, is to create precise nano-assemblies of functional proteins with both defined structures and a controlled number of protein-building blocks. Here we report a series of supramolecular green fluorescent protein oligomers that are assembled in precise polygonal geometries and prepared in a monodisperse population. Green fluorescent protein is engineered to be self-assembled in cells into oligomeric assemblies that are natively separated in a single-protein resolution by surface charge manipulation, affording monodisperse protein (nano)polygons from dimer to decamer. Several functional proteins are multivalently displayed on the oligomers with controlled orientations. Spatial arrangements of protein oligomers and displayed functional proteins are directly visualized by a transmission electron microscope. By employing our functional protein assemblies, we provide experimental insight into multivalent protein-protein interactions and tools to manipulate receptor clustering on live cell surfaces.

Identifiers

PMID25972078
PMCPMC4479010
OpenAlexW2262781415

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.