Evidence map›Paper›PMID 41325488›Full record

ArticlePLoS computational biology2025

Automated registration and clustering for enhanced localization atomic force microscopy of flexible membrane proteins.

Creighton M Lisowski, Gavin M King, Ioan Kosztin

Abstract read
In one paragraph

Article in PLoS computational biology, 2025. 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

3 authors.

Creighton M LisowskiDepartment of Physics and Astronomy, University of Missouri, Columbia, Missouri, United States of America.
Gavin M KingDepartment of Physics and Astronomy, University of Missouri, Columbia, Missouri, United States of America.
Ioan KosztinDepartment of Physics and Astronomy, University of Missouri, Columbia, Missouri, United States of America.ORCID 0009-0000-7801-235X

Funding

US National Science Foundation 2122027
6 · The paper itself

Abstract

Atomic Force Microscopy (AFM) can create images of biomolecules under near-native conditions but suffers from limited lateral resolution due to the finite AFM tip size and recording frequency. The recently developed Localization Atomic Force Microscopy or LAFM (Heath et al., Nature 594, 385 (2021)) enhances lateral resolution by reconstructing peak positions in AFM image stacks, but it is less effective for flexible proteins with multiple conformations. Here we introduce an unsupervised deep learning algorithm that simultaneously registers and clusters images by protein conformation, thus making LAFM applicable to more flexible proteins. Using simulated AFM images from molecular dynamics simulations of the SecYEG translocon as a model membrane protein system, we demonstrate improved resolution for individual protein conformations. This work represents a step towards a more general LAFM algorithm that can handle biological macromolecules with multiple distinct conformational states such as SecYEG.

Indexed as

Image Processing, Computer-AssistedMembrane ProteinsMicroscopy, Atomic ForceAlgorithmsCluster AnalysisComputational BiologyDeep LearningMolecular Dynamics SimulationProtein ConformationSEC Translocation ChannelsMembrane ProteinsSEC Translocation Channels

Identifiers

PMID41325488
PMCPMC12680352

What Socratic holds

Textmetadata
LicenceCC BY
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.