Evidence map›Paper›PMID 34604227›Full record

ArticleFrontiers in cell and developmental biology2021

β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation.

Jacopo Lesma, Faustine Bizet, Corentin Berardet, Nicolo Tonali, Sara Pellegrino, Myriam Taverna, Lucie Khemtemourian, Jean-Louis Soulier, Carine van Heijenoort, Frédéric Halgand and 3 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 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
0.7field-weighted citation impact, top 34% 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, 16 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

13 authors at 7 institutions in 2 countries.

Jacopo LesmaBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Faustine BizetBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Corentin BerardetBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Nicolo TonaliBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Sara PellegrinoDISFARM, Sezione di Chimica Generale e Organica "A. Marchesini," Università degli Studi di Milano, Milan, Italy.
Myriam TavernaInstitute Galien Paris-Saclay, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Lucie KhemtemourianInstitute of Chemistry and Biology of Membranes and Nanoobjects, Institut Polytechnique Bordeaux, CNRS UMR 5248, Université de Bordeaux, Pessac, France.
Jean-Louis SoulierBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Carine van HeijenoortICSN, Equipe Biologie et Chimie Structurales, Département de Chimie et Biologie Structurales et Analytiques, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Frédéric HalgandInstitut de Chimie Physique, Equipe Chimie Analytique Physicochimie Réactivité des Ions, CNRS, Université Paris-Saclay, Orsay, France.
Tâp Ha-DuongBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Julia KaffyBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Sandrine OngeriBioCIS, CNRS, Université Paris-Saclay, Châtenay-Malabry, France.
Centre National de la Recherche Scientifique · FRInstitut Galien Paris-Saclay · FRUniversité Paris-Saclay · FRInstitut de Biologie Physico-Chimique · FRLaboratoire des Biomolécules · FRUniversité de Bordeaux · FRUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid diseases are degenerative pathologies, highly prevalent today because they are closely related to aging, that have in common the erroneous folding of intrinsically disordered proteins (IDPs) which aggregate and lead to cell death. Type 2 Diabetes involves a peptide called human islet amyloid polypeptide (hIAPP), which undergoes a conformational change, triggering the aggregation process leading to amyloid aggregates and fibers rich in β-sheets mainly found in the pancreas of all diabetic patients. Inhibiting the aggregation of amyloid proteins has emerged as a relevant therapeutic approach and we have recently developed the design of acyclic flexible hairpins based on peptidic recognition sequences of the amyloid β peptide (Aβ

Indexed as

aggregationamyloidaza-peptidehIAPPpeptidomimeticstype 2 diabetesβ-hairpin

Identifiers

PMID34604227
PMCPMC8481668
OpenAlexW3200744244

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.