Evidence map›Paper›PMID 31803901›Full record

ReviewBiochemical Society transactions2019

Better together: building protein oligomers naturally and by design.

Rebecca E A Gwyther, D Dafydd Jones, Harley L Worthy

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. BTBCell reports methods · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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.

Rebecca E A GwytherMolecular Biosciences, School of Biosciences, Cardiff University, Cardiff, U.K.
D Dafydd JonesMolecular Biosciences, School of Biosciences, Cardiff University, Cardiff, U.K.
Harley L WorthySchool of Biosciences, University of Exeter, Exeter, U.K.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein oligomers are more common in nature than monomers, with dimers being the most prevalent final structural state observed in known structures. From a biological perspective, this makes sense as it conserves vital molecular resources that may be wasted simply by generating larger single polypeptide units, and allows new features such as cooperativity to emerge. Taking inspiration from nature, protein designers and engineers are now building artificial oligomeric complexes using a variety of approaches to generate new and useful supramolecular protein structures. Oligomerisation is thus offering a new approach to sample structure and function space not accessible through simply tinkering with monomeric proteins.

Indexed as

Amino AcidsBiopolymersPolymerizationProtein ConformationProtein EngineeringProteinsAmino AcidsBiopolymersProteinsexpanded genetic codeoligomerizationprotein complexesprotein engineeringstructural biologysynthetic biology

Identifiers

PMID31803901
PMCPMC6925524

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.