Evidence map›Paper›PMID 35225868›Full record

ArticleAntibodies (Basel, Switzerland)2022

Construction of a Humanized Artificial VHH Library Reproducing Structural Features of Camelid VHHs for Therapeutics.

Taihei Murakami, Shigefumi Kumachi, Yasuhiro Matsunaga, Miwa Sato, Kanako Wakabayashi-Nakao, Hidekazu Masaki, Ryo Yonehara, Maiko Motohashi, Naoto Nemoto, Masayuki Tsuchiya

Abstract read
In one paragraph

Article in Antibodies (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
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  5. Article
  6. Article
  7. Review
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  9. Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Distinct types of VHHs in Alpaca.Frontiers in immunology · 2024
    Article
  19. Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 2023
    Article
  20. Evaluation of the Potential Impact of In Silico Humanization on VInternational journal of molecular sciences · 2023
    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

10 authors.

Taihei MurakamiEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Shigefumi KumachiEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Yasuhiro MatsunagaGraduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.ORCID 0000-0003-2872-3908
Miwa SatoMitsui Knowledge Industry Co., Ltd., Tokyo 164-0003, Japan.
Kanako Wakabayashi-NakaoEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Hidekazu MasakiEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Ryo YoneharaEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Maiko MotohashiEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Naoto NemotoEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.
Masayuki TsuchiyaEpsilon Molecular Engineering, Inc., Saitama 338-8570, Japan.ORCID 0000-0002-7136-3111

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A variable domain of heavy chain antibody (VHH) has different binding properties than conventional antibodies. Conventional antibodies prefer binding to the convex portion of the antigen, whereas VHHs prefer epitopes, such as crevices and clefts on the antigen. Therefore, developing candidates with the binding characteristics of camelid VHHs is important. Thus, To this end, a synthetic VHH library that reproduces the structural properties of camelid VHHs was constructed. First, the characteristics of VHHs were classified according to the paratope formation based on crystal structure analyses of the complex structures of VHHs and antigens. Then, we classified 330 complementarity-determining region 3 (CDR3) structures of VHHs from the Protein Data Bank (PDB) into three loop structures:

Indexed as

cDNA displayhigh throughput screeningsynthetic librarytherapeutic antibodiesvariable domain of heavy chain antibodies

Identifiers

PMID35225868
PMCPMC8884020

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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.