Evidence map›Paper›PMID 22577864›Full record

ArticleJournal of the American Chemical Society2012

Engineering a rigid protein tunnel for biomolecular detection.

Mohammad M Mohammad, Raghuvaran Iyer, Khalil R Howard, Mark P McPike, Philip N Borer, Liviu Movileanu

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  12. Article
  13. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  14. Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  15. Review
  16. Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020
    Review
  17. Review
  18. Article
  19. Article
  20. 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

6 authors.

Mohammad M MohammadDepartment of Physics, Syracuse University, New York 13244-1130, United States.
Raghuvaran Iyer
Khalil R Howard
Mark P McPike
Philip N Borer
Liviu Movileanu

Funding

Engineered Nanopores for Single-Molecule Stochastic SensingR01GM088403 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2009 to 2022
$3.8M
PACKAGING SIGNAL STRUCTURES OF HIV AND OTHER RNA VIRUSESR01GM032691 · NIGMS · SYRACUSE UNIVERSITY AT SYRACUSE · PI BORER, PHILIP N · 1985 to 2006
$1.1M
Microarray Chips for Rapid Detection of High Affinity Nucleic Acid Sequences.R44GM076811 · NIGMS · APTAMATRIX, INC. · PI MCPIKE, MARK PATRICK · 2008 to 2009
$1.1M
NIGMS NIH HHS R01 GM032691NIGMS NIH HHS R01 GM088403NIGMS NIH HHS R44 GM076811
6 · The paper itself

Abstract

One intimidating challenge in protein nanopore-based technologies is designing robust protein scaffolds that remain functionally intact under a broad spectrum of detection conditions. Here, we show that an extensively engineered bacterial ferric hydroxamate uptake component A (FhuA), a β-barrel membrane protein, functions as a robust protein tunnel for the sampling of biomolecular events. The key implementation in this work was the coupling of direct genetic engineering with a refolding approach to produce an unusually stable protein nanopore. More importantly, this nanostructure maintained its stability under many experimental circumstances, some of which, including low ion concentration and highly acidic aqueous phase, are normally employed to gate, destabilize, or unfold β-barrel membrane proteins. To demonstrate these advantageous traits, we show that the engineered FhuA-based protein nanopore functioned as a sensing element for examining the proteolytic activity of an enzyme at highly acidic pH and for determining the kinetics of protein-DNA aptamer interactions at physiological salt concentration.

Indexed as

Genetic EngineeringAptamers, NucleotideBacterial Outer Membrane ProteinsEscherichia coli ProteinsModels, MolecularProtein FoldingAptamers, NucleotideBacterial Outer Membrane ProteinsEscherichia coli ProteinsFhuA protein, E coli

Identifiers

PMID22577864
PMCPMC3415594

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.