Evidence map›Paper›PMID 42322049›Full record

ArticleBiophysical journal2026

AFM-Fold: Rapid reconstruction of protein conformations from AFM images.

Tsuyoshi Kawai, Yasuhiro Matsunaga

Abstract read
In one paragraph

Article in Biophysical journal, 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. 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

2 authors.

Tsuyoshi KawaiRIKEN Center for Computational Science, 7-1-26 Minatojima-minami-machi, Chuo-ku, Kobe, Hyogo 650-0047, Japan; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama-shi, Saitama 338-8570, Japan.
Yasuhiro MatsunagaRIKEN Center for Computational Science, 7-1-26 Minatojima-minami-machi, Chuo-ku, Kobe, Hyogo 650-0047, Japan; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama-shi, Saitama 338-8570, Japan. Electronic address: ymatsunaga@riken.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-speed atomic force microscopy (HS-AFM) enables direct visualization of protein dynamics under near-physiological conditions, yet its intrinsic limitation to surface topography prevents atomic-level structural characterization. We present AFM-Fold, a generative AI-based framework that reconstructs three-dimensional protein conformations directly from AFM images. AFM-Fold combines a group-equivariant convolutional neural network, which extracts low-dimensional collective variables (CVs) from AFM images, with a guided diffusion process that generates conformations consistent with the inferred CVs. Using pseudo-AFM images of adenylate kinase, AFM-Fold accurately reproduced not only the open and closed conformations, but also a continuous range of intermediate conformations spanning the open-closed transition. Application to 159 experimental HS-AFM frames of the flagellar protein FlhA

Indexed as

Image Processing, Computer-AssistedMicroscopy, Atomic ForceAdenylate KinaseConvolutional Neural NetworksGenerative Artificial IntelligenceProtein ConformationAdenylate Kinase

Identifiers

PMID42322049
PMCPMC13507418

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.