Evidence map›Paper›PMID 25650429›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Tunable control of antibody immobilization using electric field.

Sam Emaminejad, Mehdi Javanmard, Chaitanya Gupta, Shuai Chang, Ronald W Davis, Roger T Howe

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Journal of chemical information and modeling · 2025
    Article
  3. Electric Field Cycling of Physisorbed Antibodies Reduces Biolayer Polarization Dispersion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

6 authors.

Sam EmaminejadDepartment of Electrical Engineering and Computer Sciences, University of California, Berkeley, CA 94720; Stanford Genome Technology Center, Stanford School of Medicine, Palo Alto, CA 94304; sam.e@berkeley.edu mehdi.javanmard@rutgers.edu jeanne.thompson@stanford.edu.
Mehdi JavanmardDepartment of Electrical and Computer Engineering, Rutgers University, Piscataway, NJ 08854; and sam.e@berkeley.edu mehdi.javanmard@rutgers.edu jeanne.thompson@stanford.edu.
Chaitanya GuptaDepartment of Electrical Engineering, Stanford University, Stanford, CA 94305.
Shuai ChangDepartment of Electrical Engineering, Stanford University, Stanford, CA 94305.
Ronald W DavisStanford Genome Technology Center, Stanford School of Medicine, Palo Alto, CA 94304; sam.e@berkeley.edu mehdi.javanmard@rutgers.edu jeanne.thompson@stanford.edu.
Roger T HoweDepartment of Electrical Engineering, Stanford University, Stanford, CA 94305.

Funding

WHOLE YEAST GENOME TRANSCRIPTIONAL AND FUNCTIONAL GENE MAPS--A FEASIBILITY STUDYP01HG000205 · NHGRI · STANFORD UNIVERSITY · PI DAVIS, RONALD WAYNE, HOWE, ROGER THOMAS · 1990 to 2016
$120.9M
NHGRI NIH HHS P01 HG000205
6 · The paper itself

Abstract

The controlled immobilization of proteins on solid-state surfaces can play an important role in enhancing the sensitivity of both affinity-based biosensors and probe-free sensing platforms. Typical methods of controlling the orientation of probe proteins on a sensor surface involve surface chemistry-based techniques. Here, we present a method of tunably controlling the immobilization of proteins on a solid-state surface using electric field. We study the ability to orient molecules by immobilizing IgG molecules in microchannels while applying lateral fields. We use atomic force microscopy to both qualitatively and quantitatively study the orientation of antibodies on glass surfaces. We apply this ability for controlled orientation to enhance the performance of affinity-based assays. As a proof of concept, we use fluorescence detection to indirectly verify the modulation of the orientation of proteins bound to the surface. We studied the interaction of fluorescently tagged anti-IgG with surface immobilized IgG controlled by electric field. Our study demonstrates that the use of electric field can result in more than 100% enhancement in signal-to-noise ratio compared with normal physical adsorption.

Indexed as

ElectricityAntibodiesImmunoglobulin GMicroscopy, Atomic ForceSpectrometry, FluorescenceAntibodiesImmunoglobulin Gelectrokineticmicrofluidicsprotein assayprotein immobilizationsample preparation

Identifiers

PMID25650429
PMCPMC4343132

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.