Optofluidic Waveguides for the Label-Free Study of Silk Protein Aggregates.

Jan R Heck, Zenon Toprakcioglu, Tobias E Naegele, Michael H Frosz, Tuomas P J Knowles, Tijmen G Euser

Abstract read

In one paragraph

Article in ACS omega, 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

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

6 authors.

Jan R HeckDepartment of Physics, Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom.ORCID https://orcid.org/0000-0002-8450-9212

Zenon ToprakciogluYusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID https://orcid.org/0000-0003-1964-8432

Tobias E NaegeleDepartment of Engineering, University of Cambridge, CB3 0FA Cambridge, United Kingdom.ORCID https://orcid.org/0000-0002-1842-6750

Michael H FroszMax Planck Institute for the Science of Light, Erlangen 91058, Germany.ORCID https://orcid.org/0000-0002-8857-0029

Tuomas P J KnowlesYusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID https://orcid.org/0000-0002-7879-0140

Tijmen G EuserDepartment of Physics, Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom.ORCID https://orcid.org/0000-0002-8305-9598

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methods for studying protein aggregation are crucial to understanding the associated disease pathologies and for functional biomaterial synthesis in nature and in the laboratory. The ideal measurement platform is low-volume, label-free, and noncontact, as well as easily integrated into continuous-flow microfluidic experiments to provide scalability. Current approaches realize only a subset of these requirements. Here, we demonstrate a new technique for studying protein aggregates and

Identifiers

PMID41078746

DOI10.1021/acsomega.5c07826

PMCPMC12509126

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.