Evidence map›Paper›PMID 29255047›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Enzyme leaps fuel antichemotaxis.

Ah-Young Jee, Sandipan Dutta, Yoon-Kyoung Cho, Tsvi Tlusty, Steve Granick

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Artificial chemotaxis in micro/nanomotors.Nature communications · 2026
    Review
  3. Article
  4. Interactions Between Active Matters and Endogenous Fields.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  5. Collective Dynamics of Urease-Based Nanomotors in a Chemical Gradient.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  6. Article
  7. Mechanochemical active ratchet.Scientific reports · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Single-particle diffusional fingerprinting: A machine-learning framework for quantitative analysis of heterogeneous diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Review
  19. Review
  20. A thermodynamic perspective on enhanced enzyme diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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.

Ah-Young JeeCenter for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea.
Sandipan DuttaCenter for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea.
Yoon-Kyoung ChoCenter for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea.
Tsvi TlustyCenter for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea.ORCID 0000-0002-9662-3725
Steve GranickCenter for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea; sgranick@ibs.re.kr.ORCID 0000-0003-4775-2202

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is mounting evidence that enzyme diffusivity is enhanced when the enzyme is catalytically active. Here, using superresolution microscopy [stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS)], we show that active enzymes migrate spontaneously in the direction of lower substrate concentration ("antichemotaxis") by a process analogous to the run-and-tumble foraging strategy of swimming microorganisms and our theory quantifies the mechanism. The two enzymes studied, urease and acetylcholinesterase, display two families of transit times through subdiffraction-sized focus spots, a diffusive mode and a ballistic mode, and the latter transit time is close to the inverse rate of catalytic turnover. This biochemical information-processing algorithm may be useful to design synthetic self-propelled swimmers and nanoparticles relevant to active materials. Executed by molecules lacking the decision-making circuitry of microorganisms, antichemotaxis by this run-and-tumble process offers the biological function to homogenize product concentration, which could be significant in situations when the reactant concentration varies from spot to spot.

Indexed as

ElectrophorusAcetylcholinesteraseAnimalsFish ProteinsUreaseAcetylcholinesteraseFish ProteinsUreaseactive matterchemotaxisenzymeFCSfluorescence correlation spectroscopy

Identifiers

PMID29255047
PMCPMC5776828

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.