Evidence map›Paper›PMID 31263208›Full record

ArticleNature chemistry2019

Protein engineering through tandem transamidation.

Robert E Thompson, Adam J Stevens, Tom W Muir

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  10. Sortase-Mediated Multi-Fragment Assemblies by Ligation Site Switching.Angewandte Chemie (International ed. in English) · 2022
    Article
  11. Review
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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 2 institutions in 1 country.

Robert E ThompsonDepartment of Chemistry, Princeton University, Frick Chemistry Laboratory, Princeton, NJ, USA.ORCID http://orcid.org/0000-0002-5729-9344
Adam J StevensDepartment of Chemistry, Princeton University, Frick Chemistry Laboratory, Princeton, NJ, USA.
Tom W MuirDepartment of Chemistry, Princeton University, Frick Chemistry Laboratory, Princeton, NJ, USA. muir@princeton.edu.ORCID http://orcid.org/0000-0001-9635-0344
Princeton University · USUniversity of California, San Francisco · US

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
NCI NIH HHS P01 CA196539NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Semisynthetic proteins engineered to contain non-coded elements such as post-translational modifications (PTMs) represent a powerful class of tools for interrogating biological processes. Here, we introduce a one-pot, chemoenzymatic method that allows broad access to chemically modified proteins. The approach involves a tandem transamidation reaction cascade that integrates intein-mediated protein splicing with enzyme-mediated peptide ligation. We show that this approach can be used to introduce PTMs and biochemical probes into a range of proteins including Cas9 nuclease and the transcriptional regulator MeCP2, which causes Rett syndrome when mutated. The versatility of the approach is further illustrated through the chemical tailoring of histone proteins within a native chromatin setting. We expect our approach will extend the scope of semisynthesis in protein engineering.

Indexed as

Protein EngineeringAmidesHumansMethyl-CpG-Binding Protein 2Protein Processing, Post-TranslationalProtein SplicingAmidesMECP2 protein, humanMethyl-CpG-Binding Protein 2

Identifiers

PMID31263208
PMCPMC6711197
OpenAlexW2956143076

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.