Evidence map›Paper›PMID 39207057›Full record

ReviewChemical reviews2024

Genetic Code Expansion for Mechanistic Studies in Ion Channels: An (Un)natural Union of Chemistry and Biology.

Daniel T Infield, Miranda E Schene, Jason D Galpin, Christopher A Ahern

Abstract 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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. 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.

Daniel T InfieldDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242, United States.
Miranda E ScheneDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242, United States.
Jason D GalpinDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242, United States.
Christopher A AhernDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242, United States.ORCID 0000-0002-7975-2744

Funding

Chemical biology of voltage-gated cation channelsR35GM148239 · NIGMS · UNIVERSITY OF IOWA · PI Christopher A Ahern · 2023 to 2026
$2.5M
The Facility for Atomic MutagenesisR24NS104617 · NINDS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2018 to 2021
$1.0M
Using a Molecular Toolkit to Examine Potassium Channel Gating and RegulationF30HL165692 · NHLBI · UNIVERSITY OF IOWA · PI SCHENE, MIRANDA · 2022 to 2025
$178k
Chemical Biology of CFTR RegulationF32HL149184 · NHLBI · UNIVERSITY OF IOWA · PI INFIELD, DANIEL T · 2019 to 2021
$136k
NHLBI NIH HHS F30 HL165692NHLBI NIH HHS F32 HL149184NIGMS NIH HHS R35 GM148239NINDS NIH HHS R24 NS104617
6 · The paper itself

Abstract

Ion channels play central roles in biology and human health by catalyzing the transmembrane flow of electrical charge. These proteins are ideal targets for genetic code expansion (GCE) methods because it is feasible to measure ion channel activity from miniscule amounts of protein and to analyze the resulting data via rigorous, established biophysical methods. In an ideal scenario, the encoding of synthetic, noncanonical amino acids via GCE allows the experimenter to ask questions inaccessible to traditional methods. For this reason, GCE has been successfully applied to a variety of ligand- and voltage-gated channels wherein extensive structural, functional, and pharmacological data exist. Here, we provide a comprehensive summary of GCE as applied to ion channels. We begin with an overview of the methods used to encode noncanonical amino acids in channels and then describe mechanistic studies wherein GCE was used for photochemistry (cross-linking; caged amino acids) and atomic mutagenesis (isosteric manipulation of charge and aromaticity; backbone mutation). Lastly, we cover recent advances in the encoding of fluorescent amino acids for the real-time study of protein conformational dynamics.

Indexed as

Genetic CodeIon ChannelsAmino AcidsAnimalsHumansAmino AcidsIon Channels

Identifiers

PMID39207057
PMCPMC11503617

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.