Evidence map›Paper›PMID 35056828›Full record

ArticleMolecules (Basel, Switzerland)2022

Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR.

Yu Suzuki, Takanori Higashi, Takahiro Yamamoto, Hideyasu Okamura, Takehiro K Sato, Tetsuo Asakura

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. 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 at 3 institutions in 1 country.

Yu SuzukiDepartment of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1, Bunkyo, Fukui 910-8507, Japan.
Takanori HigashiDepartment of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1, Bunkyo, Fukui 910-8507, Japan.
Takahiro YamamotoDepartment of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1, Bunkyo, Fukui 910-8507, Japan.
Hideyasu OkamuraDepartment of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1, Bunkyo, Fukui 910-8507, Japan.
Takehiro K SatoSpiber Inc., 234-1 Mizukami, Kakuganji, Tsuruoka 998-0052, Japan.
Tetsuo AsakuraDepartment of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, Tokyo 184-8588, Japan.
University of Fukui · JPSpiber (Japan) · JPTokyo University of Agriculture and Technology · JP

Funding

Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Culture and Supports of Japan 26248050Impulsing Paradigm Change through Disruptive Technologies Program no grant number
6 · The paper itself

Abstract

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated

Indexed as

AnimalsBombyxFormatesInsect ProteinsMagnetic Resonance SpectroscopyProtein ConformationRecombinant ProteinsSilkFormatesformic acidInsect ProteinsRecombinant ProteinsSilkformic acidNMRspider silk

Identifiers

PMID35056828
PMCPMC8778467
OpenAlexW4205829242

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.