Evidence map›Paper›PMID 15632292›Full record

ArticleProtein science : a publication of the Protein Society2005

Regulation of protein activity with small-molecule-controlled inteins.

Georgios Skretas, David W Wood

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
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

43 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. An intein-based biosensor to measure protein stability in vivo.Protein science : a publication of the Protein Society · 2024
    Article
  8. Enzyme Fragment Complementation Driven by Nucleic Acid Hybridization.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Methods to Study the Structure and Catalytic Activity of cis-Splicing Inteins.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  18. Review
  19. Proximity Induced Splicing Utilizing Caged Split Inteins.Journal of the American Chemical Society · 2019
    Article
  20. Article
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 at 1 institution in 1 country.

Georgios SkretasDepartment of Chemical Engineering, Princeton University, Engineering Quadrangle, Olden St., Princeton, NJ 08544, USA.
David W Wood
Princeton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inteins are the protein analogs of self-splicing RNA introns, as they post-translationally excise themselves from a variety of protein hosts. Intein insertion abolishes, in general, the activity of its host protein, which is subsequently restored upon intein excision. These protein elements therefore have the potential to be used as general molecular "switches" for the control of arbitrary target proteins. Based on rational design, an intein-based protein switch has been constructed whose splicing activity is conditionally triggered in vivo by the presence of thyroid hormone or synthetic analogs. This modified intein was used in Escherichia coli to demonstrate that a number of different proteins can be inactivated by intein insertion and then reactivated by the addition of thyroid hormone via ligand-induced splicing. This conditional activation was also found to occur in a dose-dependent manner. Rational protein engineering was then combined with genetic selection to evolve an additional intein whose activity is controlled by the presence of synthetic estrogen ligands. The ability to regulate protein function post-translationally through the use of ligand-controlled intein splicing will most likely find applications in metabolic engineering, drug discovery and delivery, biosensing, molecular computation, as well as many additional areas of biotechnology.

Indexed as

Genetic TechniquesAllosteric SiteAmino Acid Sequencebeta-Galactosidasebeta-LactamasesBiosensing TechniquesDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliEstrogensHumansInteinsKineticsLigandsMutagenesis, Site-DirectedMutationbeta-Galactosidasebeta-LactamasesEstrogensLigandsProteinsRNAThyroid Hormones

Identifiers

PMID15632292
PMCPMC2386410
OpenAlexW2165269455

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.