Excited State Vibrational Dynamics Reveals a Photocycle That Enhances the Photostability of the TagRFP-T Fluorescent Protein.

Atsushi Yabushita, Chia-Yun Cheng, Ying Kuan Ko, Takayoshi Kobayashi, Izumi Iwakura, Ralph Jimenez

Abstract read

In one paragraph

Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

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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

1 citing paper in PubMed.

Directly adopting inverse biosensors to image live cell enzyme activities in nanodomains.Proceedings of the National Academy of Sciences of the United States of America · 2026
Article

4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Atsushi YabushitaDepartment of Electrophysics, National Yang Ming Chiao Tung University, Hsinchu 300, Taiwan.ORCID 0000-0001-9308-4298

Chia-Yun ChengDepartment of Electrophysics, National Yang Ming Chiao Tung University, Hsinchu 300, Taiwan.

Ying Kuan KoDepartment of Electrophysics, National Yang Ming Chiao Tung University, Hsinchu 300, Taiwan.

Takayoshi KobayashiDepartment of Electrophysics, National Yang Ming Chiao Tung University, Hsinchu 300, Taiwan.

Izumi IwakuraDepartment of Chemistry, Faculty of Engineering, Kanagawa University, Yokohama 2218686, Japan.

Ralph JimenezJILA, National Institute of Standards and Technology and University of Colorado Boulder, Boulder, Colorado 80309, United States.ORCID 0000-0002-8989-405X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High photostability is a desirable property of fluorescent proteins (FPs) for imaging, yet its molecular basis is poorly understood. We performed ultrafast spectroscopy on TagRFP and its 9-fold more photostable variant TagRFP-T (TagRFP S158T) to characterize their initial photoreactions. We find significant differences in their electronic and vibrational dynamics, including faster excited-state proton transfer and transient changes in the frequency of the

Indexed as

ProtonsGreen Fluorescent ProteinsGreen Fluorescent ProteinsProtons

Identifiers

PMID38282329

DOI10.1021/acs.jpcb.3c07212

PMCPMC10860143

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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.