Evidence map›Paper›PMID 38478911›Full record

ArticleACS nano2024

Resolving the Nanoscale Structure of β-Sheet Peptide Self-Assemblies Using Single-Molecule Orientation-Localization Microscopy.

Weiyan Zhou, Conor L O'Neill, Tianben Ding, Oumeng Zhang, Jai S Rudra, Matthew D Lew

Abstract read
In one paragraph

Article in ACS nano, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
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  5. Article
  6. Designing the Next Generation of Biomaterials through Nanoengineering.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  7. Article
  8. Review
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  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Weiyan ZhouPreston M. Green Department of Electrical and Systems Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0002-5995-4728
Conor L O'NeillDepartment of Biomedical Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0003-0714-8828
Tianben DingPreston M. Green Department of Electrical and Systems Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0003-0710-2344
Oumeng ZhangPreston M. Green Department of Electrical and Systems Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0001-7318-2130
Jai S RudraDepartment of Biomedical Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0002-7837-4980
Matthew D LewPreston M. Green Department of Electrical and Systems Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0002-5614-3292

Funding

Six-Dimensional Single-Molecule Nanoscopy for Elucidating the Dynamic Organization of BiomoleculesR35GM124858 · NIGMS · WASHINGTON UNIVERSITY · PI Matthew D Lew · 2017 to 2026
$3.3M
NIGMS NIH HHS R35 GM124858
6 · The paper itself

Abstract

Synthetic peptides that self-assemble into cross-β fibrils are versatile building blocks for engineered biomaterials due to their modularity and biocompatibility, but their structural and morphological similarities to amyloid species have been a long-standing concern for their translation. Further, their polymorphs are difficult to characterize by using spectroscopic and imaging techniques that rely on ensemble averaging to achieve high resolution. Here, we utilize Nile red (NR), an amyloidophilic fluorogenic probe, and single-molecule orientation-localization microscopy (SMOLM) to characterize fibrils formed by the designed amphipathic enantiomers KFE8

Indexed as

Amyloid beta-PeptidesMicroscopyAmyloidProtein Conformation, beta-StrandProtein Structure, SecondaryAmyloidAmyloid beta-Peptidesfluorogenic probespolymorphismself-assemblysuper-resolution microscopysupramolecular helix

Identifiers

PMID38478911
PMCPMC11025465

What OpenQuestion holds

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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.