Evidence map›Paper›PMID 37916305›Full record

ArticleProtein science : a publication of the Protein Society2023

Conformational features and interaction mechanisms of V

Koichi Yamamoto, Satoru Nagatoishi, Ryo Matsunaga, Makoto Nakakido, Daisuke Kuroda, Kouhei Tsumoto

Abstract readCase Reports
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025
    Article
  2. Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025
    Article
  3. Review
  4. Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 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

6 authors.

Koichi YamamotoDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.
Satoru NagatoishiDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.
Ryo MatsunagaDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-7702-9176
Makoto NakakidoDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-0328-9914
Daisuke KurodaDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-2390-4785
Kouhei TsumotoDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.

Funding

Japan Agency for Medical Research and Development JP22ama121033jJapan Society for the Promotion of Science JP19H05766Japan Society for the Promotion of Science JP20H02531JST CREST JPMJCR20H8Research Support Project for Life Science and Drug Discovery 22ama121033
6 · The paper itself

Abstract

The β-hairpin conformation is regarded as an important basic motif to form and regulate protein-protein interactions. Single-domain V

Indexed as

Immunoglobulin Heavy ChainsImmunoglobulin Variable RegionAmino Acid SequenceAntibodiesComplementarity Determining RegionsHumansAntibodiesComplementarity Determining RegionsImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionCDR3FR3VHH antibodyβ-hairpin

Identifiers

PMID37916305
PMCPMC10661080

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.