Evidence map›Paper›PMID 38979642›Full record

ArticleACS applied materials & interfaces2024

Improved Imaging Surface for Quantitative Single-Molecule Microscopy.

Yu P Zhang, Evgeniia Lobanova, Asher Dworkin, Martin Furlepa, Woo Suk Yang, Melanie Burke, Jonathan X Meng, Natalie Potter, Renata Lang Sala, Lakmini Kahanawita and 4 more

Abstract read
In one paragraph

Article in ACS applied materials & interfaces, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. DNA Hanger: Surface-Minimized Single-Molecule Immunoassay Platform.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  6. Article
  7. Reusable Microfluidic Chambers for Single-Molecule Microscopy.ACS applied materials & interfaces · 2024
    Article
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

14 authors.

Yu P ZhangDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.ORCID 0000-0001-5486-278X
Evgeniia LobanovaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Asher DworkinDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Martin FurlepaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Woo Suk YangDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Melanie BurkeDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Jonathan X MengDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Natalie PotterDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Renata Lang SalaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Lakmini KahanawitaDepartment of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0PY, U.K.
Florence LayburnDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Oren A SchermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.ORCID 0000-0001-8032-7166
Caroline H Williams-GrayDepartment of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0PY, U.K.
David KlenermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Preventing nonspecific binding is essential for sensitive surface-based quantitative single-molecule microscopy. Here we report a much-simplified RainX-F127 (RF-127) surface with improved passivation. This surface achieves up to 100-fold less nonspecific binding from protein aggregates compared to commonly used polyethylene glycol (PEG) surfaces. The method is compatible with common single-molecule techniques including single-molecule pull-down (SiMPull), super-resolution imaging, antibody-binding screening and single exosome visualization. This method is also able to specifically detect alpha-synuclein (α-syn) and tau aggregates from a wide range of biofluids including human serum, brain extracts, cerebrospinal fluid (CSF) and saliva. The simplicity of this method further allows the functionalization of microplates for robot-assisted high-throughput single-molecule experiments. Overall, this simple but improved surface offers a versatile platform for quantitative single-molecule microscopy without the need for specialized equipment or personnel.

Indexed as

alpha-SynucleinSingle Molecule Imagingtau ProteinsHumansPolyethylene GlycolsProtein AggregatesSurface Propertiesalpha-SynucleinPolyethylene GlycolsProtein Aggregatestau Proteinsimaging surfaceprotein aggregatessingle-molecule microscopysuper-resolution microscopysurface chemistrysurface passivation

Identifiers

PMID38979642
PMCPMC11261557

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.