Evidence map›Paper›PMID 27419062›Full record

ArticleFEBS open bio2016

Anti-EGFR scFv tetramer (tetrabody) with a stable monodisperse structure, strong anticancer effect, and a long in vivo half-life.

Ryutaro Asano, Noriaki Koyama, Yasuyo Hagiwara, Yosuke Masakari, Ryota Orimo, Kyoko Arai, Hiromi Ogata, Shozo Furumoto, Mitsuo Umetsu, Izumi Kumagai

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

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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

10 authors at 1 institution in 1 country.

Ryutaro AsanoDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan; Present address: Department of Biotechnology and Life Science Graduate School of Engineering Tokyo University of Agriculture and Technology Tokyo 184-8588 Japan.
Noriaki KoyamaDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Yasuyo HagiwaraDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Yosuke MasakariDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Ryota OrimoDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Kyoko AraiDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Hiromi OgataDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Shozo FurumotoDepartment of Radiopharmaceutical Chemistry Graduate School of Pharmaceutical Sciences Tohoku University Sendai Japan.
Mitsuo UmetsuDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Izumi KumagaiDepartment of Biomolecular Engineering Graduate School of Engineering Tohoku University Sendai Japan.
Tohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of single-chain variable fragments (scFvs) as therapeutic agents has the potential to reduce the high cost of antibody production, but the development process often impairs scFv functions such as binding affinity and pharmacokinetics. Multimerization is one strategy for recovering or enhancing these lost functions. Previously, we constructed several antiepidermal growth factor receptor (EGFR) scFv multimers by modifying linker length and domain order. Antitumor effects comparable with those of the currently approved anti-EGFR therapeutic antibodies were observed for scFv trimers. In the present study, we fractionated an anti-EGFR scFv tetramer from the intracellular soluble fraction of an Escherichia coli transformant. Compared with the trimer, the tetramer showed higher affinity, greater cancer cell growth inhibition, and prolonged blood retention time. Furthermore, the tetramer did not dissociate into the trimer or other smaller species during long-term storage (up to 33 weeks). Thus, our developed scFv tetramer is an attractive candidate next-generation anti-EGFR therapeutic antibody that can be produced via a low-cost bacterial expression system.

Indexed as

anticancer effectEGFRScFvScFv multimertetrabody

Identifiers

PMID27419062
PMCPMC4887975
OpenAlexW2336579939

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.