Evidence map›Paper›PMID 28774114›Full record

ReviewMaterials (Basel, Switzerland)2016

Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides.

Weonu Choe, Trishaladevi A Durgannavar, Sang J Chung

Open access · goldAbstract readReview
In one paragraph

Review in Materials (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
13.7field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 197 citations in OpenAlex.

  1. Article
  2. Rapid Fc-mediated surface modification of liposomes with antibodies for selective targeting of pancreatic tumors.Journal of controlled release : official journal of the Controlled Release Society · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Step-by-Step Preparation of Immobilized RecombinantAvicenna journal of medical biotechnology · 2026
    Article
  7. A review of targeted drug delivery with antibody-drug complexes.The Journal of pharmacology and experimental therapeutics · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Cleavage Under Targets and Release Using Nuclease (CUT&RUN) in Macrophages.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

12 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

3 authors at 1 institution in 1 country.

Weonu ChoeDepartment of Chemistry, Seoul National University, Seoul 151-742, Korea. chweha@gmail.com.
Trishaladevi A DurgannavarResearch Institute of Biomolecular Chemistry, Dongguk University, Seoul 100-715, Korea. trishalad@gmail.com.
Sang J ChungResearch Institute of Biomolecular Chemistry, Dongguk University, Seoul 100-715, Korea. sjchung@dongguk.edu.
Dongguk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rapidly increasing application of antibodies has inspired the development of several novel methods to isolate and target antibodies using smart biomaterials that mimic the binding of Fc-receptors to antibodies. The Fc-binding domain of antibodies is the primary binding site for e.g., effector proteins and secondary antibodies, whereas antigens bind to the Fab region. Protein A, G, and L, surface proteins expressed by pathogenic bacteria, are well known to bind immunoglobulin and have been widely exploited in antibody purification strategies. Several difficulties are encountered when bacterial proteins are used in antibody research and application. One of the major obstacles hampering the use of bacterial proteins is sample contamination with trace amounts of these proteins, which can invoke an immune response in the host. Many research groups actively develop synthetic ligands that are able to selectively and strongly bind to antibodies. Among the reported ligands, peptides that bind to the Fc-domain of antibodies are attractive tools in antibody research. Besides their use as high affinity ligands in antibody purification chromatography, Fc-binding peptides are applied e.g., to localize antibodies on nanomaterials and to increase the half-life of proteins in serum. In this review, recent developments of Fc-binding peptides are presented and their binding characteristics and diverse applications are discussed.

Indexed as

affinity column chromatographyantibodyFc-binding peptideProtein AProtein A mimicsProtein GProtein Ltargeted drug delivery

Identifiers

PMID28774114
PMCPMC5456964
OpenAlexW2560263475

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.