Evidence map›Paper›PMID 38691379›Full record

ReviewChemical reviews2024

Genetic Encoding of Phosphorylated Amino Acids into Proteins.

Michael C Allen, P Andrew Karplus, Ryan A Mehl, Richard B Cooley

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.5field-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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  5. Article
  6. Article
  7. AJournal of bacteriology · 2025
    Article
  8. Article
  9. Biological Regulation StudiedAccounts of chemical research · 2025
    Article
  10. Article
  11. Review
  12. Review
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

4 authors at 1 institution in 1 country.

Michael C AllenDepartment of Biochemistry and Biophysics, Oregon State University, GCE4All Research Center, 2011 Agricultural and Life Sciences, Corvallis, Oregon 97331 United States.ORCID 0009-0007-0577-6739
P Andrew KarplusDepartment of Biochemistry and Biophysics, Oregon State University, GCE4All Research Center, 2011 Agricultural and Life Sciences, Corvallis, Oregon 97331 United States.
Ryan A MehlDepartment of Biochemistry and Biophysics, Oregon State University, GCE4All Research Center, 2011 Agricultural and Life Sciences, Corvallis, Oregon 97331 United States.ORCID 0000-0003-2932-4941
Richard B CooleyDepartment of Biochemistry and Biophysics, Oregon State University, GCE4All Research Center, 2011 Agricultural and Life Sciences, Corvallis, Oregon 97331 United States.ORCID 0000-0003-3928-2757
Oregon State University · US

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
Equipment supplement: Defining Roles Of NitroTyrosine In Disease Via Genetic Code ExpansionR01GM114653 · NIGMS · OREGON STATE UNIVERSITY · PI MEHL, RYAN A · 2015 to 2024
$2.6M
NIGMS NIH HHS R01 GM114653NIGMS NIH HHS RM1 GM144227
6 · The paper itself

Abstract

Reversible phosphorylation is a fundamental mechanism for controlling protein function. Despite the critical roles phosphorylated proteins play in physiology and disease, our ability to study individual phospho-proteoforms has been hindered by a lack of versatile methods to efficiently generate homogeneous proteins with site-specific phosphoamino acids or with functional mimics that are resistant to phosphatases. Genetic code expansion (GCE) is emerging as a transformative approach to tackle this challenge, allowing direct incorporation of phosphoamino acids into proteins during translation in response to amber stop codons. This genetic programming of phospho-protein synthesis eliminates the reliance on kinase-based or chemical semisynthesis approaches, making it broadly applicable to diverse phospho-proteoforms. In this comprehensive review, we provide a brief introduction to GCE and trace the development of existing GCE technologies for installing phosphoserine, phosphothreonine, phosphotyrosine, and their mimics, discussing both their advantages as well as their limitations. While some of the technologies are still early in their development, others are already robust enough to greatly expand the range of biologically relevant questions that can be addressed. We highlight new discoveries enabled by these GCE approaches, provide practical considerations for the application of technologies by non-GCE experts, and also identify avenues ripe for further development.

Indexed as

Genetic CodeHumansPhosphoamino AcidsPhosphorylationProteinsPhosphoamino AcidsProteins

Identifiers

PMID38691379
PMCPMC11658404
OpenAlexW4396544109

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.