Evidence map›Paper›PMID 40515853›Full record

ReviewCellular and molecular life sciences : CMLS2025

'Intelligent' proteins.

Timir Tripathi, Vladimir N Uversky, Alessandro Giuliani

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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.

Timir TripathiMolecular and Structural Biophysics Laboratory, Department of Zoology, School of Life Sciences, North-Eastern Hill University, Shillong, 793022, India.ORCID http://orcid.org/0000-0001-5559-289X
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, USF Health Byrd Alzheimer's Research Institute, University of South Florida, Tampa, FL, 33612, USA. vuversky@usf.edu.ORCID http://orcid.org/0000-0002-4037-5857
Alessandro GiulianiEnvironment and Health Department, Istituto Superiore di Sanità, Viale Regina Elena 299, Roma, 00161, Italy.ORCID http://orcid.org/0000-0002-4640-804X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present an idea of protein molecules that challenges the traditional view of proteins as simple molecular machines and suggests instead that they exhibit a basic form of "intelligence". The idea stems from suggestions coming from Integrated Information Theory (IIT), network theory, and allostery to explore how proteins process information, adapt to their environment, and even show memory-like behaviors. We define protein intelligence using IIT and focus on how proteins integrate information (in terms of the parameter Φ coming from IIT) and balance their core (stable, ordered regions) and periphery (flexible, disordered regions). This balance allows proteins to remain stable while adapting to changes and operating in a critical state where order and disorder coexist. We summarize recent findings on conformational memory, allosteric regulation, protein intrinsic disorder, liquid-liquid phase separation, and critical transitions, and compare protein behavior to other complex systems like ecosystems and neural networks. While our perspective offers a unified framework to understand proteins, it also raises questions about applying intelligence concepts to molecular systems. We discuss how this understanding could advance protein engineering, drug design, and synthetic biology, while at the same time acknowledging the challenges of creating adaptive, "intelligent" proteins. This concept bridges the gap between mechanistic and systems-level views of proteins and offers a comprehensive understanding of their dynamic and adaptive nature. We have tried to redefine the traditionally metaphorical concept of "intelligence" in biochemistry as a measurable property while simultaneously establishing the material foundation of protein intelligence through the identification of fundamental elements such as memory and learning in molecular systems.

Indexed as

ProteinsAllosteric RegulationHumansProtein ConformationProteinsAllosteryConformational memoryCore-periphery dynamicsCritical StatesIntegrated information theoryIntrinsically disordered proteinsLiquid-liquid phase separationPost-translational modificationsProtein intelligence

Identifiers

PMID40515853
PMCPMC12167427

What Socratic holds

Textmetadata
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 Socratic graph.