Evidence map›Paper›PMID 36583150›Full record

ArticleFrontiers in chemistry2022

Conformational switch and multiple supramolecular structures of a newly identified self-assembling protein-mimetic peptide from

Elettra Fasola, Giulia Alboreggia, Stefano Pieraccini, Francesco Oliva, Fatima Ezzahra Agharbaoui, Michela Bollati, Giovanni Bertoni, Sandro Recchia, Marcello Marelli, Umberto Piarulli and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

12 authors at 3 institutions in 1 country.

Elettra FasolaScience and High Technology Department, University of Insubria, Como, Italy.
Giulia AlboreggiaScience and High Technology Department, University of Insubria, Como, Italy.
Stefano PieracciniChemistry Department, University of Milan, Milan, Italy.
Francesco OlivaChemistry Department, University of Milan, Milan, Italy.
Fatima Ezzahra AgharbaouiChemistry Department, University of Milan, Milan, Italy.
Michela BollatiCNR and Department of Biosciences, Institute of Biophysics, University of Milan, Milan, Italy.
Giovanni BertoniDepartment of Bioscience, University of Milan, Milan, Italy.
Sandro RecchiaScience and High Technology Department, University of Insubria, Como, Italy.
Marcello MarelliCNR-SCITEC-Istituto di Scienze e Tecnologie Chimiche "Giulio Natta", Milan, Italy.
Umberto PiarulliScience and High Technology Department, University of Insubria, Como, Italy.
Sara PellegrinoPharmaceutical Science Department, University of Milan, Milan, Italy.
Silvia GazzolaScience and High Technology Department, University of Insubria, Como, Italy.
University of Milan · ITUniversity of Insubria · ITIstituto di Scienze e Tecnologie Chimiche "Giulio Natta"

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-mimetic peptides (PMPs) are shorter sequences of self-assembling proteins, that represent remarkable building blocks for the generation of bioinspired functional supramolecular structures with multiple applications. The identification of novel aminoacidic sequences that permit the access to valuable biocompatible materials is an attractive area of research. In this work,

Indexed as

motif designpeptide materialprotein-mimetic peptideself-assemblysupramolecular gelYeaZ protein

Identifiers

PMID36583150
PMCPMC9792601
OpenAlexW4311319897

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.