Evidence map›Paper›PMID 38923711›Full record

ArticleProtein science : a publication of the Protein Society2024

Thermostability and binding properties of single-chained Fv fragments derived from therapeutic antibodies.

Takashi Tadokoro, Harumi Tsuboi, Kota Nakamura, Tetsushi Hayakawa, Reo Ohmura, Izumi Kato, Masaki Inoue, Shin-Ichi Tsunoda, Sayaka Niizuma, Yukari Okada and 2 more

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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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

12 authors.

Takashi TadokoroLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Harumi TsuboiLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kota NakamuraLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Tetsushi HayakawaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Reo OhmuraLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Izumi KatoCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Masaki InoueLaboratory of Cellular and Molecular Physiology, The Faculty of Pharmaceutical Sciences, Kobe Gakuin University, Kobe, Japan.
Shin-Ichi TsunodaLaboratory of Cellular and Molecular Physiology, The Faculty of Pharmaceutical Sciences, Kobe Gakuin University, Kobe, Japan.
Sayaka NiizumaCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Yukari OkadaCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Satoko OtsuguroCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Katsumi MaenakaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-5459-521X

Funding

Japan Agency for Medical Research and Development (AMED) JP20ae0101047Japan Agency for Medical Research and Development (AMED) JP21am0101093Japan Agency for Medical Research and Development (AMED) JP21fk0108463Japan Agency for Medical Research and Development (AMED) JP223fa627005Japan Agency for Medical Research and Development (AMED) JP22ama121037Ministry of Education, Culture, Sports, Science and Technology/Japan Society for the Promotion of Science JP 20K05721Scientific Research on Innovative Areas and International Group from the Ministry of Education, Culture, Sports, Science and Technology/Japan Society for the Promotion of Science JP20H05873Takeda Science Foundation
6 · The paper itself

Abstract

Small antibody fragments have recently been used as alternatives to full-length monoclonal antibodies in therapeutic applications. One of the most popular fragment antibodies is single-chain fragment variables (scFvs), consisting of variable heavy (V

Indexed as

Protein StabilitySingle-Chain AntibodiesAntibodies, MonoclonalCalorimetry, Differential ScanningHumansProtein BindingAntibodies, MonoclonalSingle-Chain Antibodiesantibodysingle chain fragment variablethermal stability

Identifiers

PMID38923711
PMCPMC11201803

What OpenQuestion holds

Textmetadata
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.