Evidence map›Paper›PMID 30778383›Full record

ArticleFrontiers in chemistry2019

Nanoplasmonic Sensor Detects Preferential Binding of IRSp53 to Negative Membrane Curvature.

Gustav Emilsson, Evelyn Röder, Bita Malekian, Kunli Xiong, John Manzi, Feng-Ching Tsai, Nam-Joon Cho, Marta Bally, Andreas Dahlin

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
18.7field-weighted citation impact, top 1% of its field
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

4 citing papers in PubMed, 331 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
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

9 authors at 5 institutions in 3 countries.

Gustav EmilssonPharmaceutical Sciences, AstraZeneca R&D, Mölndal, Sweden.
Evelyn RöderPharmaceutical Sciences, AstraZeneca R&D, Mölndal, Sweden.
Bita MalekianDepartment of Chemistry and Chemical Engineering, Chalmers University of Technology, Göteborg, Sweden.
Kunli XiongDepartment of Chemistry and Chemical Engineering, Chalmers University of Technology, Göteborg, Sweden.
John ManziLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, and Sorbonne Université, Paris, France.
Feng-Ching TsaiLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, and Sorbonne Université, Paris, France.
Nam-Joon ChoSchool of Materials Science and Engineering, Nanyang Technological University, Singapore, Singapore.
Marta BallyDepartment of Clinical Microbiology & Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden.
Andreas DahlinDepartment of Chemistry and Chemical Engineering, Chalmers University of Technology, Göteborg, Sweden.
Chalmers University of Technology · SEAstraZeneca (Sweden) · SECentre National de la Recherche Scientifique · FRNanyang Technological University · SGUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biosensors based on plasmonic nanostructures are widely used in various applications and benefit from numerous operational advantages. One type of application where nanostructured sensors provide unique value in comparison with, for instance, conventional surface plasmon resonance, is investigations of the influence of nanoscale geometry on biomolecular binding events. In this study, we show that plasmonic "nanowells" conformally coated with a continuous lipid bilayer can be used to detect the preferential binding of the insulin receptor tyrosine kinase substrate protein (IRSp53) I-BAR domain to regions of negative surface curvature, i.e., the interior of the nanowells. Two different sensor architectures with and without an additional niobium oxide layer are compared for this purpose. In both cases, curvature preferential binding of IRSp53 (at around 0.025 nm

Indexed as

curvatureinsulin receptor tyrosine kinase substrate p53IRSp53membranesplasmonssensors

Identifiers

PMID30778383
PMCPMC6369594
OpenAlexW2911391961

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.