Evidence map›Paper›PMID 34858964›Full record

ArticleFrontiers in bioengineering and biotechnology2021

Improving the Stability of Protein-Protein Interaction Assay FlimPIA Using a Thermostabilized Firefly Luciferase.

Yuki Ohmuro-Matsuyama, Keiko Gomi, Takuya Shimoda, Hideki Yamaji, Hiroshi Ueda

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

5 authors.

Yuki Ohmuro-MatsuyamaLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Keiko GomiKikkoman Co., Ltd., Noda, Japan.
Takuya ShimodaDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, Kobe, Japan.
Hideki YamajiDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, Kobe, Japan.
Hiroshi UedaLaboratory of Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein-protein interaction assay is a key technology in various fields, being applicable in drug screening as well as in diagnosis and inspection, wherein the stability of assays is important. In a previous study, we developed a unique protein-protein interaction assay "FlimPIA" based on the functional complementation of mutant firefly luciferases (Fluc). The catalytic step of Fluc was divided into two half steps: D-luciferin was adenylated in the first step, while adenylated luciferin was oxidized in the second step. We constructed two mutants of Fluc from

Indexed as

adenylationassay stabilitybioluminescencefirefly luciferase (Fluc)oxidative reactionprotein-protein interaction (PPI)thermostability

Identifiers

PMID34858964
PMCPMC8631863

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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.