Evidence map›Paper›PMID 24574026›Full record

ArticleMolecular bioSystems2014

Structure-based engineering and comparison of novel split inteins for protein ligation.

A Sesilja Aranko, Jesper S Oeemig, Dongwen Zhou, Tommi Kajander, Alexander Wlodawer, Hideo Iwaï

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular bioSystems, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

27 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. A Unique THN Motif Is Critical for Enabling Efficient C-Terminal Traceless Cleavage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  3. Article
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  5. Review
  6. A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022
    Article
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  11. Article
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  15. Article
  16. Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020
    Article
  17. Article
  18. Article
  19. A mesophilic cysteine-less split intein for proteinProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Off-Pathway-Sensitive Protein-Splicing Screening Based on a Toxin/Antitoxin System.Chembiochem : a European journal of chemical biology · 2019
    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

6 authors at 5 institutions in 3 countries.

A Sesilja ArankoResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki, FIN-00014, Finland. hideo.iwai@helsinki.fi.
Jesper S Oeemig
Dongwen Zhou
Tommi Kajander
Alexander Wlodawer
Hideo Iwaï
Helsinki Institute of Physics · FICenter for Cancer Research · USCzech Academy of Sciences, Institute of Biotechnology · CZFrederick National Laboratory for Cancer Research · USUniversity of Helsinki · FI

Funding

Protein StructureZIABC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2009 to 2025
$27.5M
PROTEIN STRUCTUREZ01BC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2000 to 2008
$3.2M
Intramural NIH HHS Z01 BC010348
6 · The paper itself

Abstract

Protein splicing is an autocatalytic process involving self-excision of an internal protein domain, the intein, and concomitant ligation of the two flanking sequences, the exteins, with a peptide bond. Protein splicing can also take place in trans by naturally split inteins or artificially split inteins, ligating the exteins on two different polypeptide chains into one polypeptide chain. Protein trans-splicing could work in foreign contexts by replacing the native extein sequences with other protein sequences. Protein ligation using protein trans-splicing increasingly becomes a useful tool for biotechnological applications such as semi-synthesis of proteins, segmental isotopic labeling, and in vivo protein engineering. However, only a few split inteins have been successfully applied for protein ligation. Naturally split inteins have been widely used, but they are cross-reactive to each other, limiting their applications to multiple-fragment ligation. Based on the three-dimensional structures including two newly determined intein structures, we derived 21 new split inteins from four highly efficient cis-splicing inteins, in order to develop novel split inteins suitable for protein ligation. We systematically compared trans-splicing of 24 split inteins and tested the cross-activities among them to identify orthogonal split intein fragments that could be used in chemical biology and biotechnological applications.

Indexed as

InteinsProtein SplicingCrystallography, X-RayKineticsModels, BiologicalModels, MolecularProtein EngineeringTerminology as TopicTrans-Splicing

Identifiers

PMID24574026
PMCPMC7709711
OpenAlexW2056443924

What OpenQuestion holds

Textmetadata
LicenceTDM
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.