Evidence map›Paper›PMID 35222926›Full record

ArticleChemical science2022

An "OFF-ON-OFF" fluorescence protein-labeling probe for real-time visualization of the degradation of short-lived proteins in cellular systems.

Shahi Imam Reja, Yuichiro Hori, Takuya Kamikawa, Kohei Yamasaki, Miyako Nishiura, Steven D Bull, Kazuya Kikuchi

Abstract read
In one paragraph

Article in Chemical science, 2022. 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. 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

7 authors.

Shahi Imam RejaDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.ORCID https://orcid.org/0000-0003-2287-3817
Yuichiro HoriDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.ORCID https://orcid.org/0000-0002-2905-5502
Takuya KamikawaDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.
Kohei YamasakiDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.
Miyako NishiuraDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.
Steven D BullDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK.ORCID https://orcid.org/0000-0001-8244-5123
Kazuya KikuchiDivision of Applied Chemistry, Graduate School of Engineering, Osaka University Suita Osaka 565-0871 Japan kkikuchi@mls.eng.osaka-u.ac.jp horiy@mls.eng.osaka-u.ac.jp.ORCID https://orcid.org/0000-0001-7103-1275

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to monitor proteolytic pathways that remove unwanted and damaged proteins from cells is essential for understanding the multiple processes used to maintain cellular homeostasis. In this study, we have developed a new protein-labeling probe that employs an 'OFF-ON-OFF' fluorescence switch to enable real-time imaging of the expression (fluorescence ON) and degradation (fluorescence OFF) of PYP-tagged protein constructs in living cells. Fluorescence switching is modulated by intramolecular contact quenching interactions in the unbound probe (fluorescence OFF) being disrupted upon binding to the PYP-tag protein, which turns fluorescence ON. Quenching is then restored when the PYP-tag-probe complex undergoes proteolytic degradation, which results in fluorescence being turned OFF. Optimization of probe structures and PYP-tag mutants has enabled this fast reacting 'OFF-ON-OFF' probe to be used to fluorescently image the expression and degradation of short-lived proteins.

Identifiers

PMID35222926
PMCPMC8809410

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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.