Evidence map›Paper›PMID 28271446›Full record

ReviewProtein & cell2018

In vitro-engineered non-antibody protein therapeutics.

Rudo Simeon, Zhilei Chen

Abstract readReview
In one paragraph

Review in Protein & cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
–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

94 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Progress in Designing Cytokine Antagonist Antibodies for Cancer Therapy.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  3. Review
  4. Article
  5. Engineering Bispecific Peptides for Precision Immunotherapy and Beyond.International journal of molecular sciences · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Versatile Features of an Antibody Mimetic Peptide and Its Variants.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Evaluation of a novelEuropean journal of nuclear medicine and molecular imaging · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

34 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

2 authors.

Rudo SimeonDepartment of Microbial Pathogenesis and Immunology, Texas A&M University Health Science Center, College Station, TX, 77845, USA.
Zhilei ChenDepartment of Microbial Pathogenesis and Immunology, Texas A&M University Health Science Center, College Station, TX, 77845, USA. zchen4@tamu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies have proved to be a valuable mode of therapy for numerous diseases, mainly owing to their high target binding affinity and specificity. Unfortunately, antibodies are also limited in several respects, chief amongst those being the extremely high cost of manufacture. Therefore, non-antibody binding proteins have long been sought after as alternative therapies. New binding protein scaffolds are constantly being designed or discovered with some already approved for human use by the FDA. This review focuses on protein scaffolds that are either already being used in humans or are currently being evaluated in clinical trials. Although not all are expected to be approved, the significant benefits ensure that these molecules will continue to be investigated and developed as therapeutic alternatives to antibodies. Based on the location of the amino acids that mediate ligand binding, we place all the protein scaffolds under clinical development into two general categories: scaffolds with ligand-binding residues located in exposed flexible loops, and those with the binding residues located in protein secondary structures, such as α-helices. Scaffolds that fall under the first category include adnectins, anticalins, avimers, Fynomers, Kunitz domains, and knottins, while those belonging to the second category include affibodies, β-hairpin mimetics, and designed ankyrin repeat proteins (DARPins). Most of these scaffolds are thermostable and can be easily produced in microorganisms or completely synthesized chemically. In addition, many of these scaffolds derive from human proteins and thus possess very low immunogenic potential. Additional advantages and limitations of these protein scaffolds as therapeutics compared to antibodies will be discussed.

Indexed as

Amino AcidsAnimalsAntibodiesHumansLigandsProtein EngineeringProtein Structure, SecondaryRecombinant ProteinsAmino AcidsAntibodiesLigandsRecombinant Proteinsantibody surrogatemultivalentphageribosomescaffoldyeast

Identifiers

PMID28271446
PMCPMC5777970

What OpenQuestion holds

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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.