Evidence map›Paper›PMID 30405123›Full record

ArticleNature communications2018

Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors.

Benjamin Cressiot, Sandra J Greive, Mehrnaz Mojtabavi, Alfred A Antson, Meni Wanunu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  14. Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020
    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

5 authors at 2 institutions in 3 countries.

Benjamin CressiotDepartment of Physics, Northeastern University, Boston, MA, 02115, USA.ORCID http://orcid.org/0000-0001-9319-3152
Sandra J GreiveYork Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK.ORCID http://orcid.org/0000-0001-6067-2632
Mehrnaz MojtabaviDepartment of Bioengineering, Northeastern University, Boston, MA, 02115, USA.
Alfred A AntsonYork Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK. fred.antson@york.ac.uk.
Meni WanunuDepartment of Physics, Northeastern University, Boston, MA, 02115, USA. wanunu@neu.edu.ORCID http://orcid.org/0000-0002-9837-0004
Northeastern University · USUniversity of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanopore-based sensors are advancing the sensitivity and selectivity of single-molecule detection in molecular medicine and biotechnology. Current electrical sensing devices are based on either membrane protein pores supported in planar lipid bilayers or solid-state (SS) pores fabricated in thin metallic membranes. While both types of nanosensors have been used in a variety of applications, each has inherent disadvantages that limit its use. Hybrid nanopores, consisting of a protein pore supported within a SS membrane, combine the robust nature of SS membranes with the precise and simple engineering of protein nanopores. We demonstrate here a novel lipid-free hybrid nanopore comprising a natural DNA pore from a thermostable virus, electrokinetically inserted into a larger nanopore supported in a silicon nitride membrane. The hybrid pore is stable and easy to fabricate, and, most importantly, exhibits low peripheral leakage allowing sensing and discrimination among different types of biomolecules.

Indexed as

NanoporesTemperatureBiopolymersBiosensing TechniquesLipidsPeptidesProtein StabilityViral ProteinsBiopolymersLipidsPeptidesViral Proteins

Identifiers

PMID30405123
PMCPMC6220183
OpenAlexW2899271144

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.