Evidence map›Paper›PMID 26030730›Full record

ArticleNature chemical biology2015

Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog.

Daniel T Rogerson, Amit Sachdeva, Kaihang Wang, Tamanna Haq, Agne Kazlauskaite, Susan M Hancock, Nicolas Huguenin-Dezot, Miratul M K Muqit, Andrew M Fry, Richard Bayliss and 1 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
146citing papers in PubMed, 1 pooled it
10.2field-weighted citation impact, top 1% 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

146 citing papers in PubMed, 1 synthesis or guideline pooled it, 238 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. In Vivo Biosynthesis and Direct Incorporation of Noncanonical Amino Acids into Proteins.Chembiochem : a European journal of chemical biology · 2025
    Review
  10. Article
  11. Article
  12. A Tailored Phospho-p53 Library Probes Antibody Specificity and Recognition Limitations.Chembiochem : a European journal of chemical biology · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Automated orthogonal tRNA generation.Nature chemical biology · 2025
    Article
  17. Review
  18. Article
  19. Review
  20. Article

86 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 1 country.

Daniel T RogersonMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Amit SachdevaMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Kaihang WangMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Tamanna HaqDepartment of Biochemistry, University of Leicester, Leicester, UK.
Agne KazlauskaiteMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Susan M HancockMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Nicolas Huguenin-DezotMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Miratul M K Muqit1] Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK. [2] College of Medicine, Dentistry and Nursing, University of Dundee, Dundee, UK.
Andrew M FryDepartment of Biochemistry, University of Leicester, Leicester, UK.
Richard BaylissDepartment of Biochemistry, University of Leicester, Leicester, UK.
Jason W ChinMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK.
Medical Research Council · GBUniversity of Leicester · GBMRC Laboratory of Molecular Biology · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Cancer Research UK 12772Cancer Research UK A12772Cancer Research UK C24461/A12772European Research Council 200583Medical Research Council MC_U105181009Medical Research Council MC_UP_A024_1008Medical Research Council U105181009Medical Research Council UD99999908Parkinson's UK G-1506Wellcome Trust 101022Wellcome Trust 101022/Z/13/ZWorldwide Cancer Research 13-0042
6 · The paper itself

Abstract

Serine phosphorylation is a key post-translational modification that regulates diverse biological processes. Powerful analytical methods have identified thousands of phosphorylation sites, but many of their functions remain to be deciphered. A key to understanding the function of protein phosphorylation is access to phosphorylated proteins, but this is often challenging or impossible. Here we evolve an orthogonal aminoacyl-tRNA synthetase/tRNACUA pair that directs the efficient incorporation of phosphoserine (pSer (1)) into recombinant proteins in Escherichia coli. Moreover, combining the orthogonal pair with a metabolically engineered E. coli enables the site-specific incorporation of a nonhydrolyzable analog of pSer. Our approach enables quantitative decoding of the amber stop codon as pSer, and we purify, with yields of several milligrams per liter of culture, proteins bearing biologically relevant phosphorylations that were previously challenging or impossible to access--including phosphorylated ubiquitin and the kinase Nek7, which is synthetically activated by a genetically encoded phosphorylation in its activation loop.

Indexed as

Gene Expression Regulation, BacterialProtein Processing, Post-TranslationalAmino Acyl-tRNA SynthetasesBase SequenceCodon, TerminatorEscherichia coliEscherichia coli ProteinsGenetic CodeModels, MolecularMolecular Sequence DataNIMA-Related KinasesNucleic Acid ConformationPhosphorylationPhosphoserineProtein EngineeringProtein Serine-Threonine KinasesAmino Acyl-tRNA SynthetasesCodon, TerminatorEscherichia coli ProteinsNEK7 protein, humanNIMA-Related KinasesPhosphoserineProtein Serine-Threonine KinasesRecombinant ProteinsUbiquitin

Identifiers

PMID26030730
PMCPMC4830402
OpenAlexW1607154936

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.