Evidence map›Paper›PMID 26317656›Full record

ArticlePloS one2015

An Engineered Split Intein for Photoactivated Protein Trans-Splicing.

Stanley Wong, Abdullah A Mosabbir, Kevin Truong

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Int&in: A machine learning-based web server for active split site identification in inteins.Protein science : a publication of the Protein Society · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. A light way for nuclear cell biologists.Journal of biochemistry · 2021
    Review
  12. Engineering an Allosteric Control of Protein Function.The journal of physical chemistry. B · 2021
    Review
  13. Article
  14. Article
  15. Proximity Induced Splicing Utilizing Caged Split Inteins.Journal of the American Chemical Society · 2019
    Article
  16. Article
  17. Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019
    Review
  18. Article
  19. Review
  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

3 authors at 1 institution in 1 country.

Stanley WongInstitute of Biomaterials and Biomedical Engineering, University of Toronto, 164 College Street, Toronto, Ontario, M5S 3G9, Canada.
Abdullah A MosabbirInstitute of Biomaterials and Biomedical Engineering, University of Toronto, 164 College Street, Toronto, Ontario, M5S 3G9, Canada.
Kevin TruongInstitute of Biomaterials and Biomedical Engineering, University of Toronto, 164 College Street, Toronto, Ontario, M5S 3G9, Canada; Edward S. Rogers Sr. Department of Electrical and Computer Engineering, University of Toronto, 10 King's College Circle, Toronto, Ontario, M5S 3G4, Canada.
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein splicing is mediated by inteins that auto-catalytically join two separated protein fragments with a peptide bond. Here we engineered a genetically encoded synthetic photoactivatable intein (named LOVInC), by using the light-sensitive LOV2 domain from Avena sativa as a switch to modulate the splicing activity of the split DnaE intein from Nostoc punctiforme. Periodic blue light illumination of LOVInC induced protein splicing activity in mammalian cells. To demonstrate the broad applicability of LOVInC, synthetic protein systems were engineered for the light-induced reassembly of several target proteins such as fluorescent protein markers, a dominant positive mutant of RhoA, caspase-7, and the genetically encoded Ca2+ indicator GCaMP2. Spatial precision of LOVInC was demonstrated by targeting activity to specific mammalian cells. Thus, LOVInC can serve as a general platform for engineering light-based control for modulating the activity of many different proteins.

Indexed as

InteinsProtein SplicingAmino Acid SequenceAvenaBiosensing TechniquesCaspase 3HeLa CellsHumansLuminescent ProteinsMolecular Sequence DataPlant ProteinsProtein Structure, TertiaryRecombinant ProteinsCaspase 3Luminescent ProteinsPlant ProteinsRecombinant Proteins

Identifiers

PMID26317656
PMCPMC4552755
OpenAlexW2103631798

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.