Evidence map›Paper›PMID 26824063›Full record

ArticleScience advances2015

Engineering a nanopore with co-chaperonin function.

Ching-Wen Ho, Veerle Van Meervelt, Keng-Chang Tsai, Pieter-Jan De Temmerman, Jan Mast, Giovanni Maglia

Abstract read
In one paragraph

Article in Science advances, 2015. 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
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Real-Time and Label-Free Measurement of Deubiquitinase Activity with a MspA Nanopore.Chembiochem : a European journal of chemical biology · 2021
    Article
  10. Review
  11. Article
  12. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Single-molecule nanopore enzymology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  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.

Ching-Wen HoDepartment of Chemistry, University of Leuven, Leuven 3001, Belgium.
Veerle Van MeerveltDepartment of Chemistry, University of Leuven, Leuven 3001, Belgium.
Keng-Chang TsaiNational Research Institute of Chinese Medicine, Ministry of Health and Welfare, Taipei 11221, Taiwan.
Pieter-Jan De TemmermanElectron Microscopy Unit, Veterinary and Agrochemical Research Centre (CODA-CERVA), Brussels 1180, Belgium.ORCID 0000-0001-5170-9376
Jan MastElectron Microscopy Unit, Veterinary and Agrochemical Research Centre (CODA-CERVA), Brussels 1180, Belgium.ORCID 0000-0002-4879-3367
Giovanni MagliaGroningen Biotechnology Institute, University of Groningen, Groningen 9747AG, Netherlands.

Funding

European Research Council 260884
6 · The paper itself

Abstract

The emergence of an enzymatic function can reveal functional insights and allows the engineering of biological systems with enhanced properties. We engineered an alpha hemolysin nanopore to function as GroES, a protein that, in complex with GroEL, forms a two-stroke protein-folding nanomachine. The transmembrane co-chaperonin was prepared by recombination of GroES functional elements with the nanopore, suggesting that emergent functions in molecular machines can be added bottom-up by incorporating modular elements into preexisting protein scaffolds. The binding of a single-ring version of GroEL to individual GroES nanopores prompted large changes to the unitary nanopore current, most likely reflecting the allosteric transitions of the chaperonin apical domains. One of the GroEL-induced current levels showed fast fluctuations (<1 ms), a characteristic that might be instrumental for efficient substrate encapsulation or folding. In the presence of unfolded proteins, the pattern of current transitions changed, suggesting a possible mechanism in which the free energy of adenosine triphosphate binding and hydrolysis is expended only when substrate proteins are occupied.

Indexed as

GroELGroESloop graftingnanomachineProtein foldingsingle-molecule

Identifiers

PMID26824063
PMCPMC4730846

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.