Evidence map›Paper›PMID 32409675›Full record

ArticleScientific reports2020

Giant magnetoresistive biosensors for real-time quantitative detection of protease activity.

Sandeep Adem, Sonal Jain, Michael Sveiven, Xiahan Zhou, Anthony J O'Donoghue, Drew A Hall

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
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

12 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Surface-modified CMOS biosensors.Frontiers in bioengineering and biotechnology · 2024
    Review
  3. A GMR enzymatic assay for quantifying nuclease and peptidase activity.Frontiers in bioengineering and biotechnology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Giant Magnetoresistance Biosensors in Biomedical Applications.ACS applied materials & interfaces · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. 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 at 2 institutions in 1 country.

Sandeep AdemUniversity of California - San Diego, Department of Bioengineering, La Jolla, CA, 92093, USA.
Sonal JainUniversity of California - San Diego, Department of Bioengineering, La Jolla, CA, 92093, USA.
Michael SveivenUniversity of California - San Diego, Department of Bioengineering, La Jolla, CA, 92093, USA.
Xiahan ZhouUniversity of California - San Diego, Department of Electrical and Computer Engineering, La Jolla, CA, 92093, USA.
Anthony J O'DonoghueUniversity of California - San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA, 92093, USA. ajodonoghue@ucsd.edu.
Drew A HallUniversity of California - San Diego, Department of Bioengineering, La Jolla, CA, 92093, USA. drewhall@ucsd.edu.
La Jolla Bioengineering Institute · USUniversity of California, San Diego · US

Funding

UC San Diego Clinical and Translational Research InstituteUL1TR001442 · NCATS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FIRESTEIN, GARY S, HOGARTH, MICHAEL · 2015 to 2024
$88.3M
Point-of-Care Quantitation of Sputum Neutrophil Elastase Activity in Chronic Airway DiseaseR21EB028485 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HALL, DREW ALEXANDER, O'DONOGHUE, ANTHONY JOHN · 2019 to 2021
$631k
NCATS NIH HHS UL1 TR001442NIBIB NIH HHS R21 EB028485
6 · The paper itself

Abstract

Proteases are enzymes that cleave proteins and are crucial to physiological processes such as digestion, blood clotting, and wound healing. Unregulated protease activity is a biomarker of several human diseases. Synthetic peptides that are selectively hydrolyzed by a protease of interest can be used as reporter substrates of unregulated protease activity. We developed an activity-based protease sensor by immobilizing magnetic nanoparticles (MNPs) to the surface of a giant magnetoresistive spin-valve (GMR SV) sensor using peptides. Cleavage of these peptides by a protease releases the magnetic nanoparticles resulting in a time-dependent change in the local magnetic field. Using this approach, we detected a significant release of MNPs after 3.5 minutes incubation using just 4 nM of the cysteine protease, papain. In addition, we show that proteases in healthy human urine do not release the MNPs, however addition of 20 nM of papain to the urine samples resulted in a time-dependent change in magnetoresistance. This study lays the foundation for using GMR SV sensors as a platform for real-time, quantitative detection of protease activity in biological fluids.

Indexed as

Magnetic PhenomenaAmino Acid SequenceBiosensing TechniquesEnzyme AssaysEnzymes, ImmobilizedMagnetite NanoparticlesPapainPeptide HydrolasesPeptidesSurface PropertiesTime FactorsEnzymes, ImmobilizedMagnetite NanoparticlesPapainPeptide HydrolasesPeptides

Identifiers

PMID32409675
PMCPMC7224196
OpenAlexW3024537662

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.