Evidence map›Paper›PMID 42818085›Full record

ArticlebioRxiv : the preprint server for biology2026

Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.

Eason Cao, Christopher Maffeo, Lukas Beckert, Larisa E Kapinos, Ryan J Malonis, Daniel Son, Kun Zhou, Zhuxi Wang, Qingzhou Feng, Sunandini Chandra and 6 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

16 authors.

Eason CaoDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Christopher MaffeoDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Lukas BeckertBiozentrum, University of Basel, Basel, Switzerland.
Larisa E KapinosBiozentrum, University of Basel, Basel, Switzerland.
Ryan J MalonisDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Daniel SonNanobiology Institute, Yale University, West Haven, CT, USA.
Kun ZhouDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Zhuxi WangDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Qingzhou FengDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Sunandini ChandraDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Qi ShenDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Yong XiongDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
C Patrick LuskDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0003-4703-0533
Roderick Y H LimBiozentrum, University of Basel, Basel, Switzerland.
Aleksei AksimentievDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Chenxiang LinDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-7041-1946

Funding

IMMUNOHEMATOLOGY/TRANSFUSION MEDICINE RESEARCH TRAININGT32HL007974 · NHLBI · YALE UNIVERSITY · PI JEANNE E HENDRICKSON, Diane S Krause · 2001 to 2026
$8.1M
A multiscale approach for elucidating nuclear entry mechanisms of HIV-1 capsidR01AI162260 · NIAID · YALE UNIVERSITY · PI LIN, CHENXIANG, XIONG, YONG · 2021 to 2025
$3.5M
MULTI-RESOLUTION COMPUTATIONAL PROBES OF BIOMOLECULAR STRUCTURE AND FUNCTIONR35GM164118 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Aleksei Aksimentiev · 2026 to 2026
$2.1M
NHLBI NIH HHS T32 HL007974NIAID NIH HHS R01 AI162260NIGMS NIH HHS R35 GM164118
6 · The paper itself

Abstract

Phe-Gly-rich nucleoporins (FG-Nups) within the nuclear pore complex (NPC) form a diffusion barrier that controls the exchange of macromolecules between the nucleus and cytoplasm. The behaviors of these intrinsically disordered FG-Nups are fundamental to the NPC function but remain difficult to probe within the dynamic, native nuclear pore. To bridge this knowledge gap, here we build expandable DNA-origami rings with tunable elasticity and study FG-Nups site-specifically tethered in such mechanically responsive NPC mimics. The elastic deformation of DNA rings, measured by single-particle TEM, reveals the type (attraction or repulsion) and strength of FG-Nup interactions that shape the collective morphology of these unstructured proteins. Analyzing homotypic interactions of five FG-Nup species finds diverse FG-Nup behaviors that can be classified as repulsive/extended (Nsp1), moderately cohesive/extended (Nup62, Nup153, and Nup214), and strongly cohesive/compact (Nup98). Furthermore, we examine how FG-Nups' primary sequence,

Identifiers

PMID42818085
PMCPMC13622263

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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.