Evidence map›Paper›PMID 42416893›Full record

ReviewRSC chemical biology2026

Chemical basis of fluorogenic substrate probe design: revisiting the past to discover the new in biochemistry.

Toru Komatsu, Yasuteru Urano

Abstract readReview
In one paragraph

Review in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Toru KomatsuGraduate School of Pharmaceutical Sciences, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku Tokyo 113-0033 Japan tkomatsu@mol.f.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0002-9268-6964
Yasuteru UranoGraduate School of Pharmaceutical Sciences, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku Tokyo 113-0033 Japan tkomatsu@mol.f.u-tokyo.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme activity, rather than mere protein abundance, defines the functional state of the proteome. Fluorogenic probes are molecules that are designed to directly report the "activity" of enzymes by fluorescence changes. In this review, we present a comprehensive overview of chemical design strategies for enzyme-activatable fluorogenic substrate probes targeting various classes of enzymes. We discuss the chemical principles required to convert natural substrate reactions into functional molecular sensors that respond to target enzymes with high precision. We also examine how recent advances in these design strategies, together with their integration into innovative analytical platforms, are expanding the impact of enzyme-responsive probes in chemical, biological, and clinical research.

Identifiers

PMID42416893
PMCPMC13338860

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Registered trials

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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.