Evidence map›Paper›PMID 42427238›Full record

ArticleProtein science : a publication of the Protein Society2026

Evolution of N-terminal mechanical lability as a determinant for Type III secretion.

Katherine E DaPron, Alexandre M Plastow, Morgan R Fink, Brandon Dzuba, Marc-Andre LeBlanc, Thomas T Perkins, Emad Tajkhorshid, Marcelo C Sousa

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. 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. Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026
    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

8 authors.

Katherine E DaPronDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado, USA.
Alexandre M PlastowTheoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.
Morgan R FinkDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado, USA.
Brandon DzubaJILA, National Institute of Standards and Technology and University of Colorado Boulder, Boulder, Colorado, USA.
Marc-Andre LeBlancDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado, USA.
Thomas T PerkinsDepartment of Molecular, Cellular and Developmental Biology, University of Colorado Boulder, Boulder, Colorado, USA.
Emad TajkhorshidTheoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.ORCID 0000-0001-8434-1010
Marcelo C SousaDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado, USA.

Funding

Resource for Macromolecular Modeling and VisualizationR24GM145965 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Emad Tajkhorshid · 2022 to 2026
$6.2M
Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
National Science Foundation MCB-2139572National Science Foundation MCB-2145848NIGMS NIH HHS R24 GM145965NIGMS NIH HHS T32 GM065103NIH HHS R24-GM145965NIH HHS T32-GM065103
6 · The paper itself

Abstract

Many Gram-negative pathogens critically depend on the Type III secretion system (T3SS) to inject effector proteins into host cells for colonization. Because the channel of the T3SS is narrow (~2 nm), effectors must be unfolded for secretion. However, the T3SS cannot unfold mechanically robust substrates (GFP, ubiquitin, and dihydrofolate reductase), severely impairing their secretion. Consistent with this, effectors are exceptionally mechanically labile, unfolding at low forces. Thus, secretion competency is correlated with mechanical properties. Effector sequences have significantly diverged from non-effectors, suggesting that secretion exerts evolutionary pressure selecting mechanical lability. Here, using atomic-force-microscopy-based force spectroscopy, we show that effector NleC is mechanically labile (F

Indexed as

Bacterial ProteinsEvolution, MolecularType III Secretion SystemsMicroscopy, Atomic ForceProtein UnfoldingBacterial ProteinsType III Secretion Systemsatomic‐force microscopyprotein evolutionsingle‐molecule force spectroscopysteered molecular dynamicsType III secretion system

Identifiers

PMID42427238
PMCPMC13351618

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.