Evidence map›Paper›PMID 29952121›Full record

ReviewProteomics2018

The Utility of Nanopore Technology for Protein and Peptide Sensing.

Joseph W F Robertson, Joseph E Reiner

Abstract readReview
In one paragraph

Review in Proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

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  18. Review
  19. Article
  20. Real-Time and Label-Free Measurement of Deubiquitinase Activity with a MspA Nanopore.Chembiochem : a European journal of chemical biology · 2021
    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

2 authors.

Joseph W F RobertsonPhysical Measurement Laboratory, National Institute of Standards and Technology, Gaithersburg, MD, 20899, USA.
Joseph E ReinerDepartment of Physics, Virginia Commonwealth University, Richmond, VA, 23284, USA.

Funding

Intramural NIST DOC 9999-NIST
6 · The paper itself

Abstract

Resistive pulse nanopore sensing enables label-free single-molecule analysis of a wide range of analytes. An increasing number of studies have demonstrated the feasibility and usefulness of nanopore sensing for protein and peptide characterization. Nanopores offer the potential to study a variety of protein-related phenomena that includes unfolding kinetics, differences in unfolding pathways, protein structure stability, and free-energy profiles of DNA-protein and RNA-protein binding. In addition to providing a tool for fundamental protein characterization, nanopores have also been used as highly selective protein detectors in various solution mixtures and conditions. This review highlights these and other developments in the area of nanopore-based protein and peptide detection.

Indexed as

NanoporesAnimalsBiosensing TechniquesHumansNanotechnologyPeptide FragmentsProteinsPeptide FragmentsProteinsbiosensorsnanoporesnanotechnologypeptide sensingprotein identification

Identifiers

PMID29952121
PMCPMC10935609

What OpenQuestion holds

Textmetadata
LicenceTDM
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.