Evidence map›Paper›PMID 34163777›Full record

ArticleChemical science2021

A single point mutation converts a proton-pumping rhodopsin into a red-shifted, turn-on fluorescent sensor for chloride.

Jasmine N Tutol, Jessica Lee, Hsichuan Chi, Farah N Faizuddin, Sameera S Abeyrathna, Qin Zhou, Faruck Morcos, Gabriele Meloni, Sheel C Dodani

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

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  11. Biophysical andChemical communications (Cambridge, England) · 2022
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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 1 institution in 1 country.

Jasmine N TutolDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.ORCID https://orcid.org/0000-0001-8493-4203
Jessica LeeDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.
Hsichuan ChiDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.
Farah N FaizuddinDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.
Sameera S AbeyrathnaDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.
Qin ZhouDepartment of Biological Sciences, The University of Texas at Dallas Richardson TX 75080 USA.
Faruck MorcosDepartment of Biological Sciences, The University of Texas at Dallas Richardson TX 75080 USA.
Gabriele MeloniDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.ORCID https://orcid.org/0000-0003-4976-1401
Sheel C DodaniDepartment of Chemistry and Biochemistry, The University of Texas at Dallas Richardson TX 75080 USA sheel.dodani@utdallas.edu.ORCID https://orcid.org/0000-0003-0271-6080
The University of Texas at Dallas · 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
Computational Tools to Characterize the Effects of Protein and RNA Variability in Function and InteractionsR35GM133631 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Alonso Faruck Morcos · 2019 to 2026
$3.0M
NIGMS NIH HHS R35 GM128704NIGMS NIH HHS R35 GM128923NIGMS NIH HHS R35 GM133631
6 · The paper itself

Abstract

The visualization of chloride in living cells with fluorescent sensors is linked to our ability to design hosts that can overcome the energetic penalty of desolvation to bind chloride in water. Fluorescent proteins can be used as biological supramolecular hosts to address this fundamental challenge. Here, we showcase the power of protein engineering to convert the fluorescent proton-pumping rhodopsin GR from

Identifiers

PMID34163777
PMCPMC8179538
OpenAlexW3144035713

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.