Evidence map›Paper›PMID 40181419›Full record

ArticleBiology direct2025

Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins.

Julian Toso, Valeria Pennacchietti, Mariana Di Felice, Eduarda S Ventura, Angelo Toto, Stefano Gianni

Abstract readComparative Study
In one paragraph

Article in Biology direct, 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. Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026
    Review
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

6 authors.

Julian Toso *Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy.
Valeria Pennacchietti *Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy.
Mariana Di FeliceDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy.
Eduarda S VenturaDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy.
Angelo TotoDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy.
Stefano GianniDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy. stefano.gianni@uniroma1.it.

Funding

Associazione Italiana per la Ricerca sul Cancro IG24551
6 · The paper itself

Abstract

Protein folding remains a fundamental challenge in molecular biology, particularly in understanding how polypeptide chains transition from denatured states to their functional conformations. Here we analyze the folding mechanisms of the engineered metamorphic proteins B4 and Sb3, which share highly similar sequences but adopt distinct topologies. Kinetic analyses revealed that B4 follows a two-state folding mechanism, whereas Sb3 involves the formation of an intermediate species. We further explore the role of topology in folding commitment using the metamorphic mutant Sb4, which can populate both conformations. By analyzing folding and unfolding behaviors under varying experimental conditions, our findings suggest that topology dictates folding mechanisms at an early stage. These results demonstrate that folding landscapes are primarily shaped by final native structures rather than sequence composition.

Indexed as

Protein FoldingKineticsProtein ConformationKineticsMetamorphic proteinsProtein foldingSite-directed mutagenesis

Identifiers

PMID40181419
PMCPMC11969826

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.