Evidence map›Paper›PMID 28451272›Full record

ArticleChemical science2017

β-Hairpin mimics containing a piperidine-pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species.

S Pellegrino, N Tonali, E Erba, J Kaffy, M Taverna, A Contini, M Taylor, D Allsop, M L Gelmi, S Ongeri

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
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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

10 authors at 3 institutions in 4 countries.

S PellegrinoDISFARM-Sez. Chimica Generale e Organica "A. Marchesini" , Universitá degli Studi di Milano , via Venezian 21 , 20133 Milano , Italy . Email: sara.pellegrino@unimi.it.ORCID 0000-0002-2325-3583
N TonaliMolécules Fluorées et Chimie Médicinale , BioCIS , Univ. Paris-Sud , CNRS , Université Paris Saclay , 5 rue Jean-Baptiste Clément , 92296 Châtenay-Malabry Cedex , France . Email: Sandrine.ongeri@u-psud.fr.
E ErbaDISFARM-Sez. Chimica Generale e Organica "A. Marchesini" , Universitá degli Studi di Milano , via Venezian 21 , 20133 Milano , Italy . Email: sara.pellegrino@unimi.it.
J KaffyMolécules Fluorées et Chimie Médicinale , BioCIS , Univ. Paris-Sud , CNRS , Université Paris Saclay , 5 rue Jean-Baptiste Clément , 92296 Châtenay-Malabry Cedex , France . Email: Sandrine.ongeri@u-psud.fr.
M TavernaProtéines et Nanotechnologies en Sciences Séparatives , Institut Galien Paris-Sud , Univ. Paris-Sud , CNRS , Université Paris Saclay , 5 rue Jean-Baptiste Clément , 92296 Châtenay-Malabry Cedex , France.ORCID 0000-0002-3656-8293
A ContiniDISFARM-Sez. Chimica Generale e Organica "A. Marchesini" , Universitá degli Studi di Milano , via Venezian 21 , 20133 Milano , Italy . Email: sara.pellegrino@unimi.it.ORCID 0000-0002-4394-8956
M TaylorLancaster University , Division of Biomedical and Life Sciences , Faculty of Health and Medicine , Lancaster LA1 4YQ , UK.
D AllsopLancaster University , Division of Biomedical and Life Sciences , Faculty of Health and Medicine , Lancaster LA1 4YQ , UK.
M L GelmiDISFARM-Sez. Chimica Generale e Organica "A. Marchesini" , Universitá degli Studi di Milano , via Venezian 21 , 20133 Milano , Italy . Email: sara.pellegrino@unimi.it.
S OngeriMolécules Fluorées et Chimie Médicinale , BioCIS , Univ. Paris-Sud , CNRS , Université Paris Saclay , 5 rue Jean-Baptiste Clément , 92296 Châtenay-Malabry Cedex , France . Email: Sandrine.ongeri@u-psud.fr.ORCID 0000-0002-2118-7324
Université Paris-Sud · FRUniversity of Milan · ITLancaster University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease is a neurodegenerative disorder linked to oligomerization and fibrillization of amyloid β peptides, with Aβ

Identifiers

PMID28451272
PMCPMC5359901
OpenAlexW2528907270

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.