Allostery Beyond Amplification: Temporal Regulation of Signaling Information.

Pedro Pessoa, Steve Pressé, S Banu Ozkan

Abstract readPreprint

In one paragraph

Article in ArXiv, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Pedro PessoaCenter for Biological Physics, Arizona State University, Tempe, AZ, USA.

Steve PresséCenter for Biological Physics, Arizona State University, Tempe, AZ, USA.

S Banu OzkanCenter for Biological Physics, Arizona State University, Tempe, AZ, USA.

Funding

Using dynamic network models to quantitatively predict changes in binding affinity/specificity that arise from long-range amino acid substitutionsR01GM147635 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI OZKAN, SEFIKA BANU, SWINT-KRUSE, LISKIN · 2022 to 2025

$1.8M

Toward high spatiotemporal resolution models of single molecules for in vivo applicationsR35GM148237 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI Steve Presse · 2023 to 2026

$1.7M

NIGMS NIH HHS R01 GM147635NIGMS NIH HHS R35 GM148237

6 · The paper itself

Abstract

Allostery is a fundamental mechanism of protein regulation and is commonly interpreted as modulating enzymatic activity or product abundance. Here we show that this view is incomplete. Using a stochastic model of allosteric regulation combined with an information-theoretic analysis, we quantify the mutual information between an enzyme's regulatory state and the states of downstream signaling components. Beyond controlling steady-state production levels, allostery also regulates the timing and duration over which information is transmitted. By tuning the temporal operating regime of signaling pathways, allosteric regulation enables distinct dynamical outcomes from identical molecular components, providing a physical mechanism for temporal information flow, signaling specificity, and coordination without changes in metabolic pathways.

Identifiers

PMID41542160

PMCPMC12803326

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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.