Evidence map›Paper›PMID 19204698›Full record

ReviewNature biotechnology2009

Protein promiscuity and its implications for biotechnology.

Irene Nobeli, Angelo D Favia, Janet M Thornton

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 197 papers.

0numbers the graph read from it
0cells of the map it votes in
197citing 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

197 citing papers in PubMed.

  1. Article
  2. Article
  3. Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Identification and Characterization of WOX Gene Family in Flax (International journal of molecular sciences · 2025
    Article
  15. Article
  16. Frontiers in plant science · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

137 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Irene NobeliInstitute of Structural and Molecular Biology, School of Crystallography, Birkbeck, University of London, Malet Street, London, WC1E 7HX, UK. i.nobeli@bbk.ac.uk
Angelo D Favia
Janet M Thornton

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular recognition between proteins and their interacting partners underlies the biochemistry of living organisms. Specificity in this recognition is thought to be essential, whereas promiscuity is often associated with unwanted side effects, poor catalytic properties and errors in biological function. Recent experimental evidence suggests that promiscuity, not only in interactions but also in the actual function of proteins, is not as rare as was previously thought. This has implications not only for our fundamental understanding of molecular recognition and how protein function has evolved over time but also in the realm of biotechnology. Understanding protein promiscuity is becoming increasingly important not only to optimize protein engineering applications in areas as diverse as synthetic biology and metagenomics but also to lower attrition rates in drug discovery programs, identify drug interaction surfaces less susceptible to escape mutations and potentiate the power of polypharmacology.

Indexed as

Protein ConformationProteinsAnimalsBiotechnologyComputational BiologyDrug DesignEnvironmentEvolution, MolecularGene Expression RegulationHumansLigandsModels, MolecularPliabilityProtein BindingProtein EngineeringProtein FoldingLigandsProteinsSolvents

Identifiers

PMID19204698

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.