Evidence map›Paper›PMID 42847424›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2026

Protein-Ratio Rheostats: Integrating Stoichiometry, Abundance, and Binding Affinity in Cellular Function.

Subbaya Subramanian, Reena V Kartha

Abstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 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

2 authors.

Subbaya SubramanianDepartment of Surgery, University of Minnesota Medical School, Minneapolis, Minnesota, USA.ORCID https://orcid.org/0000-0002-2544-480X
Reena V KarthaDepartment of Experimental & Clinical Pharmacology, College of Pharmacy, University of Minnesota, Minneapolis, Minnesota, USA.ORCID https://orcid.org/0000-0002-1692-1539

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular function is frequently interpreted in terms of gene presence, protein abundance, and dose-response relationships. Yet interacting proteins operate within binding and assembly regimes in which relative abundance can alter which molecular complexes predominate. We propose a protein-ratio rheostat framework in which functional output depends jointly on component ratios, absolute concentrations relative to binding affinities, interaction stoichiometry, and in multivalent systems, valency and cooperativity. The same protein ratio can therefore generate different molecular and functional states under different concentration or affinity regimes. We develop testable predictions of this framework, illustrate its application to competitive protein interactions and biomolecular condensates, and outline experimental strategies for identifying composition-sensitive behavior within defined abundance and affinity regimes.

Indexed as

ProteinsAnimalsHumansModels, BiologicalProtein BindingProteinsbinding affinitymolecular assemblyprotein–protein interactionsprotein‐ratio rheostatprotein stoichiometryrelative protein abundance

Identifiers

PMID42847424
PMCPMC13647476

What OpenQuestion holds

Textmetadata
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.