Evidence map›Paper›PMID 21407148›Full record

ReviewMolecules (Basel, Switzerland)2011

Miniproteins as phage display-scaffolds for clinical applications.

Frederic Zoller, Uwe Haberkorn, Walter Mier

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Beyond Antibodies as Binding Partners: The Role of Antibody Mimetics in Bioanalysis.Annual review of analytical chemistry (Palo Alto, Calif.) · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Antibody phage display libraries: contributions to oncology.International journal of molecular sciences · 2012
    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

3 authors.

Frederic ZollerClinical Cooperation Unit Nuclear Medicine, German Cancer Research Center, INF 280, 69120 Heidelberg, Germany.
Uwe Haberkorn
Walter Mier

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Miniproteins are currently developed as alternative, non-immunoglobin proteins for the generation of novel binding motifs. Miniproteins are rigid scaffolds that are stabilised by alpha-helices, beta-sheets and disulfide-constrained secondary structural elements. They are tolerant to multiple amino acid substitutions, which allow for the integration of a randomised affinity function into the stably folded framework. These properties classify miniprotein scaffolds as promising tools for lead structure generation using phage display technologies. Owing to their high enzymatic resistance and structural stability, miniproteins are ideal templates to display binding epitopes for medical applications in vivo. This review summarises the characteristics and the engineering of miniproteins as a novel class of scaffolds to generate of alternative binding agents using phage display screening. Moreover, recent developments for therapeutic and especially diagnostic applications of miniproteins are reviewed.

Indexed as

Amino Acid SubstitutionBacteriophagesModels, MolecularProteinsProteins

Identifiers

PMID21407148
PMCPMC6259850

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.