Evidence map›Paper›PMID 41937569›Full record

ArticleNano letters2026

Hydration-Mediated Energy Landscapes Govern Rotational Flexibility in Membrane-Bound Annexin V Assemblies.

Ayhan Yurtsever, Kien Xuan Ngo, Takashi Sumikama, Ayaka Imamura, Shunsuke Mochizuki, Kaito Hirata, Haohui Zhang, Hiroki Konno, Kazuki Miyata, Takeshi Fukuma

Abstract read
In one paragraph

Article in Nano letters, 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

10 authors.

Ayhan YurtseverNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0003-3779-5196
Kien Xuan NgoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0002-9710-5452
Takashi SumikamaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0003-3696-5720
Ayaka ImamuraNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.
Shunsuke MochizukiDivision of Frontier Engineering, Kanazawa University, Kanazawa 920-1192, Japan.
Kaito HirataDepartment of Physical Science and Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan.ORCID 0000-0003-1489-2938
Haohui ZhangDivision of Nano Life Science, Kanazawa University, Kanazawa 920-1192, Japan.
Hiroki KonnoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0002-1712-171X
Kazuki MiyataNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0002-1641-2160
Takeshi FukumaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0001-8971-6002

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interfacial water organization and dynamics govern protein stability and function across molecular to supramolecular scales. Annexin V (AnxA5), a membrane repair protein, forms 2D assemblies on lipid membranes, yet the hydration role in repair remains unexplored. Combining three-dimensional atomic force microscopy (3D-AFM) and molecular dynamics (MD) simulations, we resolve the 3D hydration architecture of AnxA5 assemblies at molecular resolution. AnxA5 is enveloped by a continuous, nonlayered hydration network extending 1.5-2 nm into bulk solvent, exhibiting quasi-periodic lateral organization across crystalline and noncrystalline trimer domains. MD simulations indicate this network forms dynamic hydrogen-bonded bridges that may stabilize interdomain junctions, thereby modulating the local energy landscape. This hydration-dependent configurational flexibility, coupled with thermal fluctuations, drives stochastic, reversible trimer rotation, potentially modulating membrane interactions and Ca

Indexed as

Annexin A5Cell MembraneWaterHumansHydrogen BondingMicroscopy, Atomic ForceMolecular Dynamics SimulationAnnexin A5ANXA5 protein, humanWaterAnnexin A5Atomic Force MicroscopyInterfacial Water StructureMolecular Dynamics SimulationsProtein AssemblyProtein Hydration Shell

Identifiers

PMID41937569
PMCPMC13088367

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Registered trials

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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.