Evidence map›Paper›PMID 19541616›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Traceless protein splicing utilizing evolved split inteins.

Steve W Lockless, Tom W Muir

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

62 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. A Unique THN Motif Is Critical for Enabling Efficient C-Terminal Traceless Cleavage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Article
  9. 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
  10. Review
  11. Article
  12. Spatio-Temporal Photoactivation of Cytotoxic Proteins.Chembiochem : a European journal of chemical biology · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Live-cell protein engineering with an ultra-short split intein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Review
  19. Article
  20. Article

2 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

2 authors at 1 institution in 1 country.

Steve W LocklessLaboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, NY 10065, USA.
Tom W Muir
Rockefeller University · US

Funding

Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
Regulation and Folding of a Multidomain Adaptor ProteinR01GM055843 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2002 to 2009
$2.7M
CHEMICAL BASIS OF THE SH3 DOMAIN STRUCTURER29GM055843 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM W · 1997 to 2001
$217k
NIGMS NIH HHS GM086868NIGMS NIH HHS GM55843NIGMS NIH HHS R01 GM055843NIGMS NIH HHS R01 GM086868NIGMS NIH HHS R29 GM055843NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Split inteins are parasitic genetic elements frequently found inserted into reading frames of essential proteins. Their association and excision restore host protein function through a protein self-splicing reaction. They have gained an increasingly important role in the chemical modification of proteins to create cyclical, segmentally labeled, and fluorescently tagged proteins. Ideally, inteins would seamlessly splice polypeptides together with no remnant sequences and at high efficiency. Here, we describe experiments that identify the branched intermediate, a transient step in the overall splicing reaction, as a key determinant of the splicing efficiency at different splice-site junctions. To alter intein specificity, we developed a cell-based selection scheme to evolve split inteins that splice with high efficiency at different splice junctions and at higher temperatures. Mutations within these evolved inteins occur at sites distant from the active site. We present a hypothesis that a network of conserved coevolving amino acids in inteins mediates these long-range effects.

Indexed as

Evolution, MolecularProtein SplicingAmino Acid SequenceAnimalsDNA Polymerase IIIHeLa CellsHumansInteinsKanamycin ResistanceKineticsMammalsModels, MolecularMolecular Sequence DataMutationProtein Structure, TertiaryProto-Oncogene Proteins c-crkDNA Polymerase IIIDNA polymerase III, alpha subunitProto-Oncogene Proteins c-crk

Identifiers

PMID19541616
PMCPMC2708728
OpenAlexW2000630217

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.