Evidence map›Paper›PMID 38852500›Full record

ReviewCurrent opinion in chemical biology2024

Probing metalloenzyme dynamics in living systems: Contemporary advances in fluorescence imaging tools and applications.

Sky Price, Emily L Que

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2024. 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.

Sky PriceDepartment of Chemistry, The University of Texas at Austin, Austin, TX 78712, USA.
Emily L QueDepartment of Chemistry, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: emilyque@cm.utexas.edu.

Funding

Targeted molecular strategies for cellular investigation of metalloproteinsR35GM133612 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Emily L Que · 2019 to 2026
$2.8M
NIGMS NIH HHS R35 GM133612
6 · The paper itself

Abstract

Metalloenzymes are essential to cellular function, and their overexpression or enhanced activation are potential therapeutic targets. However, the study of metalloenzymes in vitro presents various challenges, leading many to develop tools to study them in their native cellular environment. Small-molecule fluorescence probes are commonly used to monitor metalloenzyme function, activity, and distribution in situ. These include probes that are activity-based (fluorescence is mediated by enzyme activity) or binding-based (fluorescence is mediated by interactions with the enzyme upon binding its metal cofactor). We discuss recent innovations that overcome key design challenges, such as the rapid diffusion of activity-based probes, the difficulty of probing redox-active enzymes, the selectivity of binding-based probes, and the poor penetration depth of fluorescence, and describe novel applications of these tools.

Indexed as

Fluorescent DyesMetalloproteinsOptical ImagingAnimalsEnzymesHumansEnzymesFluorescent DyesMetalloproteins

Identifiers

PMID38852500
PMCPMC11715550

What OpenQuestion holds

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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 OpenQuestion graph.