Evidence map›Paper›PMID 9326633›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution.

V Derbyshire, D W Wood, W Wu, J T Dansereau, J Z Dalgaard, M Belfort

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.1field-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

46 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Biotechnological Applications of Protein Splicing.Current protein & peptide science · 2019
    Review
  11. Cisplatin protects mice from challenge ofEmerging microbes & infections · 2019
    Article
  12. Article
  13. Dynamics differentiate between active and inactive inteins.European journal of medicinal chemistry · 2015
    Article
  14. Nature's recipe for splitting inteins.Protein engineering, design & selection : PEDS · 2014
    Review
  15. Protein splicing: how inteins escape from precursor proteins.The Journal of biological chemistry · 2014
    Review
  16. Enigmatic distribution, evolution, and function of inteins.The Journal of biological chemistry · 2014
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 4 institutions in 1 country.

V DerbyshireNew York State Department of Health, School of Public Health, State University of New York at Albany, Albany, NY 12201-2002, USA.
D W Wood
W Wu
J T Dansereau
J Z Dalgaard
M Belfort
National Cancer Institute · USWadsworth Center · USBioScience Laboratories (United States) · USRensselaer Polytechnic Institute · US

Funding

SELF-SPLICING INTEINS: FUNCTION, EVOLUTION, APPLICATIONR01GM044844 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 1990 to 2019
$8.9M
SELF-SPLICING INTRONS IN THE PHAGE T4/E COLI SYSTEMR01GM039422 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 1988 to 2019
$5.3M
INTRON DYNAMICS IN BACTERIAR37GM039422 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 2001 to 2010
$4.0M
NIGMS NIH HHS GM39422NIGMS NIH HHS GM44844NIGMS NIH HHS R01 GM039422NIGMS NIH HHS R01 GM044844NIGMS NIH HHS R37 GM039422
6 · The paper itself

Abstract

Inteins are protein-splicing elements, most of which contain conserved sequence blocks that define a family of homing endonucleases. Like group I introns that encode such endonucleases, inteins are mobile genetic elements. Recent crystallography and computer modeling studies suggest that inteins consist of two structural domains that correspond to the endonuclease and the protein-splicing elements. To determine whether the bipartite structure of inteins is mirrored by the functional independence of the protein-splicing domain, the entire endonuclease component was deleted from the Mycobacterium tuberculosis recA intein. Guided by computer modeling studies, and taking advantage of genetic systems designed to monitor intein function, the 440-aa Mtu recA intein was reduced to a functional mini-intein of 137 aa. The accuracy of splicing of several mini-inteins was verified. This work not only substantiates structure predictions for intein function but also supports the hypothesis that, like group I introns, mobile inteins arose by an endonuclease gene invading a sequence encoding a small, functional splicing element.

Indexed as

Evolution, MolecularModels, GeneticAmino Acid SequenceArtificial Gene FusionComputer SimulationConserved SequenceEndonucleasesIntronsMycobacterium tuberculosisPlasmidsProtein SplicingRec A RecombinasesSequence DeletionEndonucleasesRec A Recombinases

Identifiers

PMID9326633
PMCPMC23508
OpenAlexW1982656848

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.