Evidence map›Paper›PMID 21068165›Full record

ReviewProtein engineering, design & selection : PEDS2011

Adnectins: engineered target-binding protein therapeutics.

D Lipovsek

Abstract readReview
In one paragraph

Review in Protein engineering, design & selection : PEDS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing 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

98 citing papers in PubMed.

  1. Trial
  2. Review
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  4. VNpj viruses · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Improving the diffraction quality of heat-shock protein 47 crystals.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. The evolving landscape of PCSK9 inhibition in cancer.European journal of pharmacology · 2023
    Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article

38 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

1 author.

D LipovsekDepartment of Protein Design, Adnexus, Bristol-Myers Squibb R&D Company, Waltham, MA 02453, USA. dlipovsek@adnexustx.com

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adnectins™ are a new family of therapeutic proteins based on the 10th fibronectin type III domain, and designed to bind with high affinity and specificity to therapeutically relevant targets. Adnectins share with antibody variable domains a beta-sheet sandwich fold with diversified loops, but differ from antibodies in primary sequence and have a simpler, single-domain structure without disulfide bonds. As a consequence, Adnectins bind targets with affinity and specificity as high as those of antibodies, but are easier to manipulate genetically and compatible with bacterial expression systems. Adnectins that bind macromolecular targets with nanomolar and picomolar affinity have been selected using in vitro evolution methods, including mRNA display, phage display and yeast display. CT-322, a PEGylated, anti-angiogenic Adnectin that binds vascular endothelial growth factor (VEGF) receptor 2 and blocks its interaction with VEGF A, C and D, is being evaluated in Phase II clinical trials for efficacy in several oncology indications.

Indexed as

AnimalsFibronectinsHumansModels, MolecularProtein BindingProtein EngineeringProtein Structure, TertiaryVascular Endothelial Growth FactorsFibronectinsVascular Endothelial Growth Factors

Identifiers

PMID21068165
PMCPMC3003446

What OpenQuestion holds

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LicenceCC BY-NC
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.