Evidence map›Paper›PMID 16373474›Full record

ReviewProtein science : a publication of the Protein Society2006

A new generation of protein display scaffolds for molecular recognition.

Ralf J Hosse, Achim Rothe, Barbara E Power

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed.

  1. Review
  2. Article
  3. Targeted Cancer Therapy-on-A-Chip.Advanced healthcare materials · 2024
    Review
  4. Article
  5. Article
  6. Towards better antivenoms: navigating the road to new types of snakebite envenoming therapies.The journal of venomous animals and toxins including tropical diseases · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. DAKS1, a Kunitz Scaffold Peptide from the Venom Gland ofPharmaceuticals (Basel, Switzerland) · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Affibody-Binding Ligands.International journal of molecular sciences · 2020
    Article
  17. OncoTargets and therapy · 2020
    Article
  18. Article
  19. Microbial Proteases Applications.Frontiers in bioengineering and biotechnology · 2019
    Review
  20. Article

1 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.

Ralf J HossePreventative Health National Research Flagship, Parkville, Victoria 3052, Australia.
Achim Rothe
Barbara E Power

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered antibodies and their fragments are invaluable tools for a vast range of biotechnological and pharmaceutical applications. However, they are facing increasing competition from a new generation of protein display scaffolds, specifically selected for binding virtually any target. Some of them have already entered clinical trials. Most of these nonimmunoglobulin proteins are involved in natural binding events and have amazingly diverse origins, frameworks, and functions, including even intrinsic enzyme activity. In many respects, they are superior over antibody-derived affinity molecules and offer an ever-extending arsenal of tools for, e.g., affinity purification, protein microarray technology, bioimaging, enzyme inhibition, and potential drug delivery. As excellent supporting frameworks for the presentation of polypeptide libraries, they can be subjected to powerful in vitro or in vivo selection and evolution strategies, enabling the isolation of high-affinity binding reagents. This article reviews the generation of these novel binding reagents, describing validated and advanced alternative scaffolds as well as the most recent nonimmunoglobulin libraries. Characteristics of these protein scaffolds in terms of structural stability, tolerance to multiple substitutions, ease of expression, and subsequent applications as specific targeting molecules are discussed. Furthermore, this review shows the close linkage between these novel protein tools and the constantly developing display, selection, and evolution strategies using phage display, ribosome display, mRNA display, cell surface display, or IVC (in vitro compartmentalization). Here, we predict the important role of these novel binding reagents as a toolkit for biotechnological and biomedical applications.

Indexed as

Peptide LibraryAnimalsCombinatorial Chemistry TechniquesHumansProtein BindingProtein Interaction MappingProteinsPeptide LibraryProteins

Identifiers

PMID16373474
PMCPMC2242358

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.