Evidence map›Paper›PMID 36346585›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Structural Classification of CDR-H3 in Single-Domain V

Daisuke Kuroda, Kouhei Tsumoto

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Structural insights into the role and targeting of EGFRvIII.Structure (London, England : 1993) · 2024
    Article
  15. Article
  16. Phage display-derived alpaca nanobodies as potential therapeutics forApplied and environmental microbiology · 2024
    Article
  17. Magnetogenetic cell activation using endogenous ferritin.bioRxiv : the preprint server for biology · 2024
    Article
  18. Article
  19. Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 2023
    Article
  20. Application Progress of the Single Domain Antibody in Medicine.International journal of molecular sciences · 2023
    Review
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

2 authors at 1 institution in 1 country.

Daisuke KurodaMedical Device Development and Regulation Research Center, School of Engineering, The University of Tokyo, Tokyo, Japan. dkuroda1981@gmail.com.
Kouhei TsumotoMedical Device Development and Regulation Research Center, School of Engineering, The University of Tokyo, Tokyo, Japan. tsumoto@bioeng.t.u-tokyo.ac.jp.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The immune systems protect vertebrates from foreign molecules or antigens, and antibodies are important mediators of this system. The sequences and structural features of antibodies vary depending on species. Many of antibodies from vertebrates, including camelids, have both heavy and light chain variable domains, but camelids also have antibodies that lack the light chains. In antibodies that lack light chains, the C-terminal variable region is called the V

Indexed as

Single-Domain AntibodiesAnimalsAntibodiesAntigensComplementarity Determining RegionsDatabases, ProteinModels, MolecularProtein ConformationAntibodiesAntigensComplementarity Determining RegionsSingle-Domain AntibodiesAntibody designAntibody modelingCanonical structureCDR-H3Nanobody

Identifiers

PMID36346585
OpenAlexW4308584019

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.