Evidence map›Paper›PMID 23009860›Full record

ArticleBiophysical journal2012

Protein logic: a statistical mechanical study of signal integration at the single-molecule level.

Wiet de Ronde, Pieter Rein ten Wolde, Andrew Mugler

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Design principles of the cytotoxic CD8Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Trainable computation in molecular networks.bioRxiv : the preprint server for biology · 2025
    Article
  3. Design principles of the cytotoxic CD8bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Time-Tailoring van der Waals Heterostructures for Human Memory System Programming.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Article
  11. Combinatorial Control through Allostery.The journal of physical chemistry. B · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. 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.

Wiet de RondeFoundation for Fundamental Research on Matter (FOM) Institute AMOLF, Amsterdam, The Netherlands. deronde@amolf.nl
Pieter Rein ten Wolde
Andrew Mugler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Information processing and decision-making is based upon logic operations, which in cellular networks has been well characterized at the level of transcription. In recent years, however, both experimentalists and theorists have begun to appreciate that cellular decision-making can also be performed at the level of a single protein, giving rise to the notion of protein logic. Here we systematically explore protein logic using a well-known statistical mechanical model. As an example system, we focus on receptors that bind either one or two ligands, and their associated dimers. Notably, we find that a single heterodimer can realize any of the 16 possible logic gates, including the XOR gate, by variation of biochemical parameters. We then introduce what to our knowledge is a novel idea: that a set of receptors with fixed parameters can encode functionally unique logic gates simply by forming different dimeric combinations. An exhaustive search reveals that the simplest set of receptors (two single-ligand receptors and one double-ligand receptor) can realize several different groups of three unique gates, a result for which the parametric analysis of single receptors and dimers provides a clear interpretation. Both results underscore the surprising functional freedom readily available to cells at the single-protein level.

Indexed as

Computers, MolecularLogicModels, StatisticalSignal TransductionLigandsModels, BiologicalProtein MultimerizationProteinsProtein Structure, QuaternaryLigandsProteins

Identifiers

PMID23009860
PMCPMC3433606

What OpenQuestion holds

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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.