Evidence map›Paper›PMID 24507610›Full record

ArticleBiophysical journal2014

High-bandwidth protein analysis using solid-state nanopores.

Joseph Larkin, Robert Y Henley, Murugappan Muthukumar, Jacob K Rosenstein, Meni Wanunu

Abstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing 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

98 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Metrology of Nanoscale Objects Using Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. Threading of Single Protein Molecules Through a Solid-State Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025
    Review
  18. Review
  19. Article
  20. Article

38 more citing papers are in PubMed but not listed here.

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.

Joseph LarkinDepartments of Physics and Chemistry/Chemical Biology, Northeastern University, Boston, Massachusetts.
Robert Y HenleyDepartments of Physics and Chemistry/Chemical Biology, Northeastern University, Boston, Massachusetts.
Murugappan MuthukumarDepartment of Polymer Science and Engineering, University of Massachusetts, Amherst, Massachusetts.
Jacob K RosensteinSchool of Engineering, Brown University, Providence, Rhode Island.
Meni WanunuDepartments of Physics and Chemistry/Chemical Biology, Northeastern University, Boston, Massachusetts. Electronic address: wanunu@neu.edu.

Funding

Modeling Macromolecular Transport through Protein Channels and NanoporesR01HG002776 · NHGRI · UNIVERSITY OF MASSACHUSETTS AMHERST · PI MUTHUKUMAR, MURUGAPPAN · 2003 to 2022
$5.3M
Single Molecule Sequencing by Nanopore induced Photon Emission (SM-SNIPE)R01HG005871 · NHGRI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI KLAPPERICH, CATHERINE M., MELLER, AMIT · 2010 to 2013
$4.0M
Picogram-level DNA sequencing using Nanopores and Zero-Mode WaveguidesR21HG006873 · NHGRI · NORTHEASTERN UNIVERSITY · PI KORLACH, JONAS, WANUNU, MENI · 2012 to 2014
$812k
NHGRI NIH HHS R01 HG002776NHGRI NIH HHS R01-HG002776NHGRI NIH HHS R01 HG005871NHGRI NIH HHS R01-HG005871NHGRI NIH HHS R21 HG006873NHGRI NIH HHS R21-HG006873
6 · The paper itself

Abstract

High-bandwidth measurements of the ion current through hafnium oxide and silicon nitride nanopores allow the analysis of sub-30 kD protein molecules with unprecedented time resolution and detection efficiency. Measured capture rates suggest that at moderate transmembrane bias values, a substantial fraction of protein translocation events are detected. Our dwell-time resolution of 2.5 μs enables translocation time distributions to be fit to a first-passage time distribution derived from a 1D diffusion-drift model. The fits yield drift velocities that scale linearly with voltage, consistent with an electrophoretic process. Further, protein diffusion constants (D) are lower than the bulk diffusion constants (D0) by a factor of ~50, and are voltage-independent in the regime tested. We reason that deviations of D from D0 are a result of confinement-driven pore/protein interactions, previously observed in porous systems. A straightforward Kramers model for this inhibited diffusion points to 9- to 12-kJ/mol interactions of the proteins with the nanopore. Reduction of μ and D are found to be material-dependent. Comparison of current-blockage levels of each protein yields volumetric information for the two proteins that is in good agreement with dynamic light scattering measurements. Finally, detection of a protein-protein complex is achieved.

Indexed as

Membrane PotentialsNanoporesAmino Acid SequenceBiosensing TechniquesHafniumMembranes, ArtificialMolecular Sequence DataOxidesPermeabilityProteinsSilicon CompoundsHafniumhafnium oxideMembranes, ArtificialOxidesProteinsSilicon Compoundssilicon nitride

Identifiers

PMID24507610
PMCPMC3944622

What OpenQuestion holds

Textmetadata
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.