Evidence map›Paper›PMID 36430461›Full record

ArticleInternational journal of molecular sciences2022

Rational Design of a Peptidomimetic Inhibitor of Gelsolin Amyloid Aggregation.

Michela Bollati, Kaliroi Peqini, Luigi Barone, Carmina Natale, Marten Beeg, Marco Gobbi, Luisa Diomede, Michelangelo Trucchi, Matteo de Rosa, Sara Pellegrino

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 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
0.8field-weighted citation impact, top 30% 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, 10 citations in OpenAlex.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025
    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

10 authors at 2 institutions in 1 country.

Michela BollatiInstitute of Biophysics, National Research Council (IBF-CNR), c/o Department of Biosciences, University of Milano, Via Celoria 26, 20133 Milano, Italy.ORCID 0000-0001-6579-2043
Kaliroi PeqiniDepartment of Pharmaceutical Science, "A. Marchesini" General and Organic Chemistry Section, University of Milano, Via Venezian 21, 20133 Milano, Italy.
Luigi BaroneDepartment of Pharmaceutical Science, "A. Marchesini" General and Organic Chemistry Section, University of Milano, Via Venezian 21, 20133 Milano, Italy.
Carmina NataleDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156 Milano, Italy.
Marten BeegDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156 Milano, Italy.ORCID 0000-0001-7201-6704
Marco GobbiDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156 Milano, Italy.ORCID 0000-0003-1014-6225
Luisa DiomedeDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156 Milano, Italy.ORCID 0000-0002-2258-0531
Michelangelo TrucchiInstitute of Biophysics, National Research Council (IBF-CNR), c/o Department of Biosciences, University of Milano, Via Celoria 26, 20133 Milano, Italy.
Matteo de RosaInstitute of Biophysics, National Research Council (IBF-CNR), c/o Department of Biosciences, University of Milano, Via Celoria 26, 20133 Milano, Italy.ORCID 0000-0002-8634-5426
Sara PellegrinoDepartment of Pharmaceutical Science, "A. Marchesini" General and Organic Chemistry Section, University of Milano, Via Venezian 21, 20133 Milano, Italy.ORCID 0000-0002-2325-3583
University of Milan · ITMario Negri Institute for Pharmacological Research · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gelsolin amyloidosis (AGel) is characterized by multiple systemic and ophthalmic features resulting from pathological tissue deposition of the gelsolin (GSN) protein. To date, no cure is available for the treatment of any form of AGel. More than ten single-point substitutions in the

Indexed as

AmyloidosisAmyloidosis, FamilialPeptidomimeticsAmyloidAmyloidogenic ProteinsAnimalsCaenorhabditis elegansGelsolinPeptidesAmyloidAmyloidogenic ProteinsGelsolinPeptidesPeptidomimeticsaggregationamyloidosisC. elegansgelsolinpeptidomimetics

Identifiers

PMID36430461
PMCPMC9698219
OpenAlexW4309008659

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.