Evidence map›Paper›PMID 36890153›Full record

ArticleNature communications2023

Size limits the sensitivity of kinetic schemes.

Jeremy A Owen, Jordan M Horowitz

Abstract read
In one paragraph

Article in Nature communications, 2023. 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. Article
  6. Ecosystems as adaptive living circuits.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Stochastic thermodynamics for biological functions.Quantitative biology (Beijing, China) · 2025
    Review
  9. Article
  10. Article
  11. Flexibility and sensitivity in gene regulation out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. A local-global principle for nonequilibrium steady states.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. The Hill function is the universal Hopfield barrier for sharpness of input-output responses.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

2 authors.

Jeremy A OwenDepartment of Physics, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA. jo6038@princeton.edu.ORCID 0000-0002-9180-3794
Jordan M HorowitzDepartment of Biophysics, University of Michigan, Ann Arbor, MI, 48109, USA. jmhorow@umich.edu.ORCID 0000-0002-9139-0811

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Living things benefit from exquisite molecular sensitivity in many of their key processes, including DNA replication, transcription and translation, chemical sensing, and morphogenesis. At thermodynamic equilibrium, the basic biophysical mechanism for sensitivity is cooperative binding, for which it can be shown that the Hill coefficient, a sensitivity measure, cannot exceed the number of binding sites. Generalizing this fact, we find that for any kinetic scheme, at or away from thermodynamic equilibrium, a very simple structural quantity, the size of the support of a perturbation, always limits the effective Hill coefficient. We show how this bound sheds light on and unifies diverse sensitivity mechanisms, including kinetic proofreading and a nonequilibrium Monod-Wyman-Changeux (MWC) model proposed for the E. coli flagellar motor switch, representing in each case a simple, precise bridge between experimental observations and the models we write down. In pursuit of mechanisms that saturate the support bound, we find a nonequilibrium binding mechanism, nested hysteresis, with sensitivity exponential in the number of binding sites, with implications for our understanding of models of gene regulation and the function of biomolecular condensates.

Indexed as

Escherichia coliAllosteric RegulationBinding SitesKineticsThermodynamics

Identifiers

PMID36890153
PMCPMC9995461

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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.