Evidence map›Paper›PMID 26381943›Full record

ReviewAdvances in experimental medicine and biology2015

Incorporation of Non-Canonical Amino Acids.

Lilia Leisle, Francis Valiyaveetil, Ryan A Mehl, Christopher A Ahern

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Synthetic Biology Approaches to Enzymology in Food and Agriculture Systems.Journal of agricultural and food chemistry · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Conformational photo-trapping in NaBiophysical journal · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Expanding the Genetic Code for Neuronal Studies.Chembiochem : a European journal of chemical biology · 2020
    Review
  14. Post-Translational Modifications of CytochromeInternational journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 3 institutions in 1 country.

Lilia LeisleDepartment of Molecular Physiology and Biophysics, University of Iowa, 51 Newton Road, 52246, Iowa City, IA, USA.
Francis ValiyaveetilDepartment of Physiology and Pharmacology, Oregon Health and Sciences University, 97239, Portland, OR, USA.
Ryan A MehlDepartment of Biochemistry and Biophysics, Oregon State University Corvallis, 97331, Corvallis, OR, USA.
Christopher A AhernDepartment of Molecular Physiology and Biophysics, University of Iowa, 51 Newton Road, 52246, Iowa City, IA, USA. christopher-ahern@uiowa.edu.
University of Iowa · USOregon Health & Science University · USOregon State University · US

Funding

Probing functional mechanisms in K+ channels using unnatural mutagenesisR01GM087546 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI VALIYAVEETIL, FRANCIS · 2009 to 2022
$4.0M
Chemical Biology of Voltage-Gated Sodium and Potassium ChannelsR01GM106569 · NIGMS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2013 to 2022
$2.7M
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
Designer DHPRs, EC coupling and an expanded genetic code in skeletal muscleR21AR066802 · NIAMS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2014 to 2015
$358k
NIAMS NIH HHS R21 AR066802NIGMS NIH HHS R01 GM087546NIGMS NIH HHS R01 GM106569NIGMS NIH HHS R01 GM114653
6 · The paper itself

Abstract

In this chapter we discuss the strengths, caveats and technical considerations of three approaches for reprogramming the chemical composition of selected amino acids within a membrane protein. In vivo nonsense suppression in the Xenopus laevis oocyte, evolved orthogonal tRNA and aminoacyl-tRNA synthetase pairs and protein ligation for biochemical production of semisynthetic proteins have been used successfully for ion channel and receptor studies. The level of difficulty for the application of each approach ranges from trivial to technically demanding, yet all have untapped potential in their application to membrane proteins.

Indexed as

Amino AcidsAmino Acid SequenceAmino Acyl-tRNA SynthetasesAnimalsCodonHumansInteinsIon ChannelsProtein EngineeringStructure-Activity RelationshipXenopus laevisAmino AcidsAmino Acyl-tRNA SynthetasesCodonIon ChannelsEvolved tRNA synthetase pairsIntein ligationNonsense suppressionProtein semi-synthesis

Identifiers

PMID26381943
PMCPMC6005199
OpenAlexW2211918045

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.