Evidence map›Paper›PMID 37059690›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Rational Design of the β-Bulge Gate in a Green Fluorescent Protein Accelerates the Kinetics of Sulfate Sensing.

Whitney S Y Ong, Ke Ji, Vishaka Pathiranage, Caden Maydew, Kiheon Baek, Rhiza Lyne E Villones, Gabriele Meloni, Alice R Walker, Sheel C Dodani

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
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

10 citing papers in PubMed, 13 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Whitney S Y OngDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0001-9821-9972
Ke JiDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0002-0085-9646
Vishaka PathiranageDepartment of Chemistry, Wayne State University, 42 W. Warren Ave., Detroit, MI 48202, USA.ORCID 0000-0002-0432-8973
Caden MaydewDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0002-7579-6109
Kiheon BaekDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0001-7342-040X
Rhiza Lyne E VillonesDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0002-0865-5189
Gabriele MeloniDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0003-4976-1401
Alice R WalkerDepartment of Chemistry, Wayne State University, 42 W. Warren Ave., Detroit, MI 48202, USA.ORCID 0000-0002-8617-3425
Sheel C DodaniDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX 75080-3021, USA.ORCID 0000-0003-0271-6080
The University of Texas at Dallas · USWayne State University · US

Funding

Principles of selectivity and translocation in transition metal transporters, metallochaperones, and associated metalloproteinsR35GM128704 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Gabriele Meloni · 2018 to 2026
$3.5M
Optical Imaging Tools for Elucidating the Roles of Anions and Anionic Modifications in Cellular SignalingR35GM128923 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Sheel Dodani · 2018 to 2026
$3.4M
NIGMS NIH HHS R35 GM128704NIGMS NIH HHS R35 GM128923
6 · The paper itself

Abstract

Detection of anions in complex aqueous media is a fundamental challenge with practical utility that can be addressed by supramolecular chemistry. Biomolecular hosts such as proteins can be used and adapted as an alternative to synthetic hosts. Here, we report how the mutagenesis of the β-bulge residues (D137 and W138) in mNeonGreen, a bright, monomeric fluorescent protein, unlocks and tunes the anion preference at physiological pH for sulfate, resulting in the turn-off sensor SulfOFF-1. This unprecedented sensing arises from an enhancement in the kinetics of binding, largely driven by position 138. In line with these data, molecular dynamics (MD) simulations capture how the coordinated entry and gating of sulfate into the β-barrel is eliminated upon mutagenesis to facilitate binding and fluorescence quenching.

Indexed as

SulfatesAnionsFluorescenceGreen Fluorescent ProteinsKineticsAnionsGreen Fluorescent ProteinsSulfatesAnionsMolecular DynamicsProtein EngineeringSensorsSupramolecular Chemistry

Identifiers

PMID37059690
PMCPMC10330437
OpenAlexW4365503124

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.