Evidence map›Paper›PMID 37218904›Full record

ArticleMethods and protocols2023

A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch-Agarose Mixture and Its Application for Convenient Protein-Protein Interaction Analysis.

Yuri Emoto, Ryoya Katayama, Emi Hibino, Sho Ishihara, Natsuko Goda, Takeshi Tenno, Yoshihiro Kobashigawa, Hiroshi Morioka, Hidekazu Hiroaki

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods and protocols, 2023. 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, top 77% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

9 authors at 2 institutions in 1 country.

Yuri EmotoLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Ryoya KatayamaDivision of Biological Sciences, Graduate School of Science, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Emi HibinoLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Sho IshiharaLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Natsuko GodaLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Takeshi TennoLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.
Yoshihiro KobashigawaDepartment of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University; 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Kumamoto, Japan.
Hiroshi MoriokaDepartment of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University; 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Kumamoto, Japan.
Hidekazu HiroakiLaboratory of Structural Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Aichi, Japan.ORCID 0000-0003-1621-5893
Nagoya University · JPKumamoto University · JP

Funding

The Public Foundation of Elizabeth Arnold－Fuji FY2021
6 · The paper itself

Abstract

The detection and quantification of protein-protein interactions (PPIs) is a crucial technique that often involves the use of recombinant proteins with fusion protein tags, such as maltose-binding protein (MBP) and glutathione-S-transferase (GST). In this study, we improved the cohesive and sticky properties of gelatinized starch by supplementing it with agarose, resulting in a harder gel that could coat the bottom of a microtiter plate. The resulting gelatinized starch/agarose mixture allowed for the efficient immobilization of MBP-tagged proteins on the coated plates, enabling the use of indirect ELISA-like PPI assays. By using the enzymatic activity of GST as an indicator, we succeeded in determining the dissociation constants between MBP-tagged and GST-tagged proteins on 96-well microtiter plates and a microplate reader without any expensive specialized equipment.

Indexed as

dissociation constant determinationgelatinized starchmaltose-binding proteinmicroplate-based assayprotein–protein interaction

Identifiers

PMID37218904
PMCPMC10204415
OpenAlexW4366826653

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Registered trials

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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.