Evidence map›Paper›PMID 38822813›Full record

ArticleACS sensors2024

Development of an miRFP680-Based Fluorescent Calcium Ion Biosensor Using End-Optimized Transposons.

Fu Chai, Hajime Fujii, Giang N T Le, Chang Lin, Keisuke Ota, Karl Matthew Lin, Lam M T Pham, Peng Zou, Mikhail Drobizhev, Yusuke Nasu and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS sensors, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
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

13 authors.

Fu ChaiDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Hajime FujiiDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Giang N T LeDepartment of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada.
Chang LinCollege of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.ORCID 0000-0003-0445-6964
Keisuke OtaDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Karl Matthew LinDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Lam M T PhamDepartment of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada.
Peng ZouCollege of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.ORCID 0000-0002-9798-5242
Mikhail DrobizhevDepartment of Microbiology and Cell Biology, Montana State University, Bozeman, Montana 59717, United States.
Yusuke NasuDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.ORCID 0000-0002-3193-9104
Takuya TeraiDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.ORCID 0000-0002-3425-3589
Haruhiko BitoDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Robert E CampbellDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.ORCID 0000-0003-0604-092X

Funding

High-Resolution Bidirectional Optical-Acoustic Mesoscopic Neural Interface for Image-Guided Neuromodulation in Behaving Animals - RF1 Admin SupplementRF1NS126102 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI CAMPBELL, ROBERT E., RAZANSKY, DANIEL · 2022 to 2024
$3.1M
Resource for Multiphoton Characterization of Genetically-Encoded ProbesU24NS109107 · NINDS · MONTANA STATE UNIVERSITY - BOZEMAN · PI Mikhail Drobizhev · 2018 to 2026
$2.2M
NINDS NIH HHS RF1 NS126102NINDS NIH HHS U24 NS109107
6 · The paper itself

Abstract

The development of new or improved single fluorescent protein (FP)-based biosensors (SFPBs), particularly those with excitation and emission at near-infrared wavelengths, is important for the continued advancement of biological imaging applications. In an effort to accelerate the development of new SFPBs, we report modified transposons for the transposase-based creation of libraries of FPs randomly inserted into analyte binding domains, or vice versa. These modified transposons feature ends that are optimized to minimize the length of the linkers that connect the FP to the analyte binding domain. We rationalized that shorter linkers between the domains should result in more effective allosteric coupling between the analyte binding-dependent conformational change in the binding domain and the fluorescence modulation of the chromophore of the FP domain. As a proof of concept, we employed end-modified Mu transposons for the discovery of SFPB prototypes based on the insertion of two circularly permuted red FPs (mApple and FusionRed) into binding proteins for l-lactate and spermidine. Using an analogous approach, we discovered calcium ion (Ca

Indexed as

Biosensing TechniquesCalciumDNA Transposable ElementsLuminescent ProteinsCalmodulinHumansCalciumCalmodulinDNA Transposable ElementsLuminescent Proteinsbiliverdin-binding fluorescent proteincell signalingdirected evolutionfluorescence microscopyheme oxygenaseprotein engineeringtransposons

Identifiers

PMID38822813
PMCPMC11218748

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.