Evidence map›Paper›PMID 31240245›Full record

ArticleCommunications biology2019

THETA system allows one-step isolation of tagged proteins through temperature-dependent protein-peptide interaction.

Kota Miura, Yusuke Tsuji, Hiromasa Mitsui, Takuya Oshima, Yosei Noshi, Yudai Arisawa, Keiko Okano, Toshiyuki Okano

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

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 1 institution in 1 country.

Kota MiuraDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Yusuke TsujiDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Hiromasa MitsuiDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Takuya OshimaDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Yosei NoshiDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Yudai ArisawaDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Keiko OkanoDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.
Toshiyuki OkanoDepartment of Electrical Engineering and Bioscience, Graduate School of Sciences and Engineering, Waseda University, TWIns, Wakamatsucho 2-2, Shinjuku-Ku, Tokyo 162-8480 Japan.ORCID 0000-0001-6740-6265
Waseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tools to control protein-protein interactions by external stimuli have been extensively developed. For this purpose, thermal stimulation can be utilized in addition to light. In this study, we identify a monoclonal antibody termed C13 mAb, which shows an approximately 480-fold decrease in the affinity constant at 37 °C compared to that at 4 °C. Next, we apply this temperature-dependent protein-peptide interaction for one-step protein purifications. We term this THermal-Elution-based TAg system as the THETA system, in which gel-immobilized C13 mAb-derived single-chain variable fragment (scFv) (termed THETAL) is able to bind with proteins tagged by C13 mAb-epitope(s) (THETAS) at 4 °C and thermally release at 37-42 °C. Moreover, to reveal the temperature-dependent interaction mechanism, molecular dynamics simulations are performed along with epitope mapping experiments. Overall, the high specificity and reversibility of the temperature-dependent features of the THETA system will support a wide variety of future applications such as thermogenetics.

Indexed as

Epitope MappingAnimalsAntibodies, MonoclonalAntibody AffinityAntibody SpecificityBiocompatible MaterialsBiotinylationEpitopesHybridomasHydrogen-Ion ConcentrationMiceMice, Inbred BALB CMolecular Dynamics SimulationMutationPeptidesProteinsAntibodies, MonoclonalBiocompatible MaterialsEpitopesPeptidesProteinsAntibody isolation and purificationBiomaterials - proteins

Identifiers

PMID31240245
PMCPMC6572768
OpenAlexW2949525645

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.