Evidence map›Paper›PMID 40315756›Full record

ArticleJournal of inorganic biochemistry2025

Structure-function relationships in solvatochromic fluorophores targeting human and bovine carbonic anhydrases.

Alyssa R Malto, Radhika Mehta, Abigail Hinojosa, Dominique Tan, Alex L Rerick, M Haziq Qureshi, Meredith K Purchal, Emily L Que

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2025. 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

8 authors.

Alyssa R MaltoDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Radhika MehtaDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Abigail HinojosaDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Dominique TanDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Alex L RerickDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
M Haziq QureshiDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Meredith K PurchalDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America.
Emily L QueDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, United States of America. 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
Bruker AVANCE III HD 500 MHz NMRS10OD021508 · OD · UNIVERSITY OF TEXAS AT AUSTIN · PI SESSLER, JONATHAN L · 2016 to 2016
$529k
NIGMS NIH HHS R35 GM133612NIH HHS S10 OD021508
6 · The paper itself

Abstract

The development of reversible, selective, small molecule fluorescent probes displaying high fluorescence turn-on responses and tight binding affinity with specific metalloenzymes requires consideration of multiple factors. In this study, we report a library of fluorescent probes for two carbonic anhydrases: human carbonic anhydrase II (hCAII) and bovine carbonic anhydrase II (bCAII) and compare differences in fluorescence turn-on and binding affinity with molecular docking to gain insight into structure-function relationships. We analyze the roles of electrostatics, hydrophobics, and sterics in influencing the fluorescence response of the probes with hCAII and bCAII which have 80 % sequence identity but drastically different fluorescence turn-on values with amino(na)phthalimide-based fluorophores.

Indexed as

Carbonic Anhydrase IIFluorescent DyesAnimalsCattleHumansMolecular Docking SimulationStructure-Activity RelationshipCarbonic Anhydrase IIFluorescent DyesActive site bindingCarbonic anhydraseElectrostaticsSolvatochromic fluorophoresSulfonamideZinc

Identifiers

PMID40315756
PMCPMC12249940

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.