Evidence map›Paper›PMID 41003994›Full record

ReviewSub-cellular biochemistry2025

Effects of Molecular Crowding on the Structural, Dynamic, and Functional Properties of Biological Macromolecules: A General Overview.

Altijana Hromić-Jahjefendić, Hana Krnjić, Vladimir N Uversky

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In one paragraph

Review in Sub-cellular biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Altijana Hromić-JahjefendićDepartment of Genetics and Bioengineering, Faculty of Engineering and Natural Sciences, International University of Sarajevo, Sarajevo, Bosnia and Herzegovina. ahromic@ius.edu.ba.
Hana KrnjićDepartment of Genetics and Bioengineering, Faculty of Engineering and Natural Sciences, International University of Sarajevo, Sarajevo, Bosnia and Herzegovina.
Vladimir N UverskyDepartment of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA. vuversky@usf.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular environment is characterized by high content of various biomacromolecules, limited amount of free water, and almost complete lack of unoccupied space. Since such extremely crowded milieu is poorly modeled by slightly salted aqueous solutions of low concentrations of a biomolecule of interest, in the laboratory practice, it is typically mimicked by concentrated solutions of various polymers or inert proteins that serve as model "crowding agents". Analysis of the behavior of different proteins under these conditions that model the effects of macromolecular crowding in vitro revealed that protein structure, folding, shape, conformational stability, binding of small molecules, enzymatic activity, protein-protein interactions, protein-nucleic acid interactions, and pathological aggregation are all affected by the presence of crowders. The goal of this chapter is to provide an overview of the variety of effects of macromolecular crowding on a protein molecule.

Indexed as

Macromolecular SubstancesProteinsAnimalsHumansNucleic AcidsProtein ConformationProtein FoldingMacromolecular SubstancesNucleic AcidsProteinsExcluded volumeIntrinsically disordered proteinMacromolecular crowdingProtein aggregationProtein foldingProtein functionProtein-protein interactionProtein structure

Identifiers

PMID41003994

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.