Evidence map›Paper›PMID 24194548›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Stochastic detection of Pim protein kinases reveals electrostatically enhanced association of a peptide substrate.

Leon Harrington, Stephen Cheley, Leila T Alexander, Stefan Knapp, Hagan Bayley

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
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  16. Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  17. Article
  18. Article
  19. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  20. Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020
    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

5 authors.

Leon HarringtonDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom.
Stephen Cheley
Leila T Alexander
Stefan Knapp
Hagan Bayley

Funding

Biotechnology and Biological Sciences Research CouncilCIHRWellcome Trust 092809
6 · The paper itself

Abstract

In stochastic sensing, the association and dissociation of analyte molecules is observed as the modulation of an ionic current flowing through a single engineered protein pore, enabling the label-free determination of rate and equilibrium constants with respect to a specific binding site. We engineered sensors based on the staphylococcal α-hemolysin pore to allow the single-molecule detection and characterization of protein kinase-peptide interactions. We enhanced this approach by using site-specific proteolysis to generate pores bearing a single peptide sensor element attached by an N-terminal peptide bond to the trans mouth of the pore. Kinetics and affinities for the Pim protein kinases (Pim-1, Pim-2, and Pim-3) and cAMP-dependent protein kinase were measured and found to be independent of membrane potential and in good agreement with previously reported data. Kinase binding exhibited a distinct current noise behavior that forms a basis for analyte discrimination. Finally, we observed unusually high association rate constants for the interaction of Pim kinases with their consensus substrate Pimtide (~10(7) to 10(8) M(-1) · s(-1)), the result of electrostatic enhancement, and propose a cellular role for this phenomenon.

Indexed as

Bacterial ToxinsHemolysin ProteinsKineticsPeptidesProtein BindingProtein EngineeringProteolysisProto-Oncogene Proteins c-pim-1Signal TransductionStatic ElectricityStochastic ProcessesBacterial ToxinsHemolysin ProteinsPeptidesProto-Oncogene Proteins c-pim-1proto-oncogene proteins pimstaphylococcal alpha-toxinCoulombic interactionphosphorylationsingle-molecule sensorsubstrate binding kinetics

Identifiers

PMID24194548
PMCPMC3839778

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.