Evidence map›Paper›PMID 28811487›Full record

ArticleScientific reports2017

A Tri-part Protein Complementation System Using Antibody-Small Peptide Fusions Enables Homogeneous Immunoassays.

Andrew S Dixon, Sun Jin Kim, Brett K Baumgartner, Sylvia Krippner, Shawn C Owen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Luciferase complementation for cellular assays beyond protein-protein interactions.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  4. Review
  5. Article
  6. Split-Protein Therapeutic Platforms: Identifying Binder Pairs.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Rapid Quantification ofAnalytical chemistry · 2022
    Article
  14. Technologies for Frugal and Sensitive Point-of-Care Immunoassays.Annual review of analytical chemistry (Palo Alto, Calif.) · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Andrew S DixonDepartment of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, University of Utah, 30 South 2000 East, Room 301, Salt Lake City, UT, 84112, USA.
Sun Jin KimDepartment of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, University of Utah, 30 South 2000 East, Room 301, Salt Lake City, UT, 84112, USA.
Brett K BaumgartnerDepartment of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, University of Utah, 30 South 2000 East, Room 301, Salt Lake City, UT, 84112, USA.
Sylvia KrippnerDepartment of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, University of Utah, 30 South 2000 East, Room 301, Salt Lake City, UT, 84112, USA.
Shawn C OwenDepartment of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, University of Utah, 30 South 2000 East, Room 301, Salt Lake City, UT, 84112, USA. shawn.owen@hsc.utah.edu.ORCID 0000-0001-5996-7679
University of Utah · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-fragment complementation is a valuable tool for monitoring protein interactions. In complementation assays, the reporter fragments are directly fused to the interacting proteins, eliminating the possibility of monitoring native interactions. In principle, complementation could be achieved by placing the reporter fragments on antibodies which bind to the proteins of interest, enabling the monitoring of endogenous protein interactions or detection of a single protein in a homogeneous immunoassay. Previous reports have demonstrated proof-of-concept of this approach; however, current complementation systems have not met the practical requirements as suitable fusion partners for antibodies while providing the sensitivity needed for immunoassays. To surmount these challenges, we created a first-in-class, tri-part split luciferase consisting of two 11-residue peptides that are used as the antibody appendages. As an initial proof-of-concept, we used antibody-peptide fusions and found them to be capable of quantifying pg/mL concentrations of soluble or cell-bound HER2, proving this unique complementation system overcomes previous limitations and transforms this approach from merely possible to practical and useful. As shown herein, this dual-peptide system provides a rapid, simple, and sensitive "add-and-read" homogeneous immunoassay platform that can be broadly adapted as an alternative to traditional immunoassays, and in the future should enable complementation to be expanded to monitoring endogenous protein interactions.

Indexed as

AntibodiesImmunoassayBinding SitesCell Line, TumorEnzyme-Linked Immunosorbent AssayErb-b2 Receptor Tyrosine KinasesGenetic Complementation TestHumansModels, MolecularPeptide FragmentsProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingProteinsRecombinant Fusion ProteinsReproducibility of ResultsAntibodiesErb-b2 Receptor Tyrosine KinasesPeptide FragmentsProteinsRecombinant Fusion Proteins

Identifiers

PMID28811487
PMCPMC5557857
OpenAlexW2745087918

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.