Evidence map›Paper›PMID 23265282›Full record

ArticleJournal of the American Chemical Society2013

Streamlined expressed protein ligation using split inteins.

Miquel Vila-Perelló, Zhihua Liu, Neel H Shah, John A Willis, Juliana Idoyaga, Tom W Muir

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.4field-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

46 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Synthesis of Peptides and Proteins with Site-Specific Glutamate Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Protein Synthesis via Activated Cysteine-Directed Protein Ligation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Semisynthesis of Functional Glycosylphosphatidylinositol-Anchored Proteins.Angewandte Chemie (International ed. in English) · 2020
    Article
  19. 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
  20. Expressed Protein Ligation without Intein.Journal of the American Chemical Society · 2020
    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 2 institutions in 1 country.

Miquel Vila-PerellóDepartment of Chemistry, Princeton University, Frick Laboratory, Princeton, New Jersey 08544, United States.
Zhihua Liu
Neel H Shah
John A Willis
Juliana Idoyaga
Tom W Muir
Princeton University · USRockefeller 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
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NIGMS NIH HHS GM086868NIGMS NIH HHS R01 GM086868NIGMS NIH HHS R01 GM107047NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Chemically modified proteins are invaluable tools for studying the molecular details of biological processes, and they also hold great potential as new therapeutic agents. Several methods have been developed for the site-specific modification of proteins, one of the most widely used being expressed protein ligation (EPL) in which a recombinant α-thioester is ligated to an N-terminal Cys-containing peptide. Despite the widespread use of EPL, the generation and isolation of the required recombinant protein α-thioesters remain challenging. We describe here a new method for the preparation and purification of recombinant protein α-thioesters using engineered versions of naturally split DnaE inteins. This family of autoprocessing enzymes is closely related to the inteins currently used for protein α-thioester generation, but they feature faster kinetics and are split into two inactive polypeptides that need to associate to become active. Taking advantage of the strong affinity between the two split intein fragments, we devised a streamlined procedure for the purification and generation of protein α-thioesters from cell lysates and applied this strategy for the semisynthesis of a variety of proteins including an acetylated histone and a site-specifically modified monoclonal antibody.

Indexed as

InteinsAntibodies, MonoclonalEstersProtein EngineeringRecombinant ProteinsAntibodies, MonoclonalEstersRecombinant Proteins

Identifiers

PMID23265282
PMCPMC3544275
OpenAlexW138094741

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.