Evidence map›Paper›PMID 33681610›Full record

ArticleACS omega2021

Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG)

Keitaro Suyama, Mika Mawatari, Daiki Tatsubo, Iori Maeda, Takeru Nose

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2021. 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
1.4field-weighted citation impact, top 18% 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, 13 citations in OpenAlex.

  1. Review
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  8. Peptide-based coacervates in therapeutic applications.Frontiers in bioengineering and biotechnology · 2022
    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

5 authors at 3 institutions in 1 country.

Keitaro SuyamaLaboratory of Biomolecular Chemistry, Faculty of Arts and Science, Kyushu University, Fukuoka 819-0395, Japan.
Mika MawatariDepartment of Chemistry, Faculty and Graduate School of Science, Fukuoka 819-0395, Japan.
Daiki TatsuboDepartment of Chemistry, Faculty and Graduate School of Science, Fukuoka 819-0395, Japan.
Iori MaedaDepartment of Physics and Information Technology, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Japan.
Takeru NoseLaboratory of Biomolecular Chemistry, Faculty of Arts and Science, Kyushu University, Fukuoka 819-0395, Japan.
Fukuoka University · JPKyushu University · JPKyushu Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elastin comprises hydrophobic repetitive sequences, such as Val-Pro-Gly-Val-Gly, which are thought to be important for the temperature-dependent reversible self-association (coacervation). Elastin and elastin-like peptides (ELPs), owing to their characteristics, are expected to be applied as base materials for the development of new molecular tools, such as drug-delivery system carrier and metal-scavenging agents. Recently, several studies have been reported on the dendritic or branching ELP analogues. Although the topological difference of the branched ELPs compared to their linear counterparts may lead to useful properties in biomaterials, the available information regarding the effect of branching on molecular architecture and thermoresponsive behavior of ELPs is scarce. To obtain further insight into the thermoresponsive behavior of branched ELPs, novel ELPs, such as nitrilotriacetic acid (NTA)-(FPGVG)

Identifiers

PMID33681610
PMCPMC7931394
OpenAlexW3130450663

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.