Evidence map›Paper›PMID 32961013›Full record

ArticleChembiochem : a European journal of chemical biology2021

Site-Specific Incorporation of a Photoactivatable Fluorescent Amino Acid.

Juan Tang, Chenfei Yu, Axel Loredo, Yuda Chen, Han Xiao

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. A hydrophobic photouncaging reaction to profile the lipid droplet interactome in tissues.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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

5 authors.

Juan TangDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
Chenfei YuDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
Axel LoredoDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
Yuda ChenDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
Han XiaoDepartment of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.ORCID 0000-0002-4311-971X

Funding

Engineering Proteins with Noncanonical Amino AcidsR35GM133706 · NIGMS · RICE UNIVERSITY · PI Han Xiao · 2019 to 2026
$2.9M
NIGMS NIH HHS R35 GM133706
6 · The paper itself

Abstract

Photoactivatable fluorophores are emerging optical probes for biological applications. Most photoactivatable fluorophores are relatively large in size and need to be activated by ultraviolet light; this dramatically limits their applications. To introduce photoactivatable fluorophores into proteins, recent investigations have explored several protein-labeling technologies, including fluorescein arsenical hairpin (FlAsH) Tag, HaloTag labeling, SNAPTag labeling, and other bioorthogonal chemistry-based methods. However, these technologies require a multistep labeling process. Here, by using genetic code expansion and a single sulfur-for-oxygen atom replacement within an existing fluorescent amino acid, we have site-specifically incorporated the photoactivatable fluorescent amino acid thioacridonylalanine (SAcd) into proteins in a single step. Moreover, upon exposure to visible light, SAcd can be efficiently desulfurized to its oxo derivatives, thus restoring the strong fluorescence of labeled proteins.

Indexed as

AlanineFluorescent DyesLightMolecular StructurePhotochemical ProcessesAlanineFluorescent Dyesgenetic code expansionnoncanonical amino acidsoptical probesphotoactivatable fluorophoresprotein labeling

Identifiers

PMID32961013
PMCPMC8011588

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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.