Evidence map›Paper›PMID 42712006›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

An Unbiased Geometry-Resolved Membrane Platform for Proteome-Scale Discovery of Membrane Curvature Sensors.

Takumi Komikawa, Rikuto Kawakami, Kunanon Chattrairat, Tatsuya Niwa, Taiga Ajiri, Takao Yasui, Masayoshi Tanaka

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. 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

7 authors.

Takumi KomikawaSchool of Materials and Chemical Technology, Institute of Science Tokyo, Yokohama, Japan.ORCID https://orcid.org/0009-0006-8198-7143
Rikuto KawakamiSchool of Materials and Chemical Technology, Institute of Science Tokyo, Yokohama, Japan.
Kunanon ChattrairatGraduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID https://orcid.org/0000-0001-7587-6777
Tatsuya NiwaInstitute of Integrated Research, Institute of Science Tokyo, Yokohama, Japan.ORCID https://orcid.org/0000-0002-1330-8974
Taiga AjiriGraduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID https://orcid.org/0000-0002-9019-9935
Takao YasuiGraduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID https://orcid.org/0000-0003-0333-3559
Masayoshi TanakaSchool of Materials and Chemical Technology, Institute of Science Tokyo, Yokohama, Japan.ORCID https://orcid.org/0000-0002-4701-5352

Funding

JSPS KAKENHI 24H00792JSPS KAKENHI 24K01265JSPS KAKENHI 25H01415JSPS KAKENHI 25K22179JSPS-NRF Bilateral Program 120248806JST CREST JPMJCR2576Moonshot Research and Development Program JP22zf0127009Nagase Science and Technology FoundationNew Energy and Industrial Technology Development Organization (NEDO) JPNP20004
6 · The paper itself

Abstract

Membrane curvature organizes protein-driven biochemistry on cellular membranes. Conventional membrane curvature assays are inherently limited by both candidate-based experimental designs and restricted membrane geometries, preventing proteome-scale discovery of curvature-sensing proteins. Here, we present a geometry-resolved membrane platform that enables hypothesis-agnostic identification of curvature-sensing proteins. A supported lipid bilayer on a hemispherical microwell array simultaneously presents convex rims, concave well interiors, and flat planar regions, while providing sufficient membrane surface area for shotgun proteomics. Following validation using canonical BAR domain proteins, we applied the platform to proteomic screening of a cell-derived peripheral membrane protein fraction. This analysis identified 671 proteins, including 71 curvature-responsive candidates spanning preferences for positively curved, negatively curved, and flat membranes. Subsequent candidate prioritization using a protein-protein interaction-guided workflow, followed by validation with purified proteins, demonstrated that the platform provides a comprehensive pipeline linking proteomics-based discovery to imaging-based evaluation. By interrogating membranes of positive, negative, and zero curvature in parallel, this platform eliminates geometric bias, expands the experimentally accessible landscape of membrane curvature sensing, and enables the discovery of previously overlooked modes of membrane curvature recognition.

Indexed as

geometry‐resolved platformmembrane curvature sensorproteome analysissupported lipid bilayer

Identifiers

PMID42712006
PMCPMC13554497

What Socratic 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 Socratic graph.