Evidence map›Paper›PMID 41019633›Full record

ArticlebioRxiv : the preprint server for biology2025

Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.

Wancheng Zhao, Wai-Ming Yau, Robert Tycko

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for 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

5 · Who and what money

Authors and funding

3 authors.

Wancheng ZhaoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.ORCID 0000-0001-6727-5533
Wai-Ming YauLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.ORCID 0000-0002-7668-7780
Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.ORCID 0000-0001-7039-7275

Funding

Structural Studies of Prion Fibrils and Other Protein FibrilsZIADK075031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$7.3M
Intramural NIH HHS ZIA DK075031
6 · The paper itself

Abstract

The central channels of nuclear pore complexes (NPCs) in eukaryotic cells are filled with protein chains whose sequences contain characteristic phenylalanine-glycine motifs. Properties of these nanopore-confined FG-repeat sequences are of central importance to NPC function. Here we demonstrate an approach to nuclear magnetic resonance (NMR) studies of FG-repeat sequences (or other polypeptides) that are tethered within pores with diameters similar to those of NPC channels. By attaching alkyl phosphonate groups to the N-terminus of a 30-residue peptide that contains four FG repeats, called FG30, we tether FG30 chains to walls of 20-nm-diameter pores in anodic aluminum oxide (AAO) wafers through phosphonate-surface bonds. Quantitative

Identifiers

PMID41019633
PMCPMC12466779

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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.