Evidence map›Paper›PMID 34199513›Full record

ReviewInternational journal of molecular sciences2021

Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications.

Niccolò Candelise, Silvia Scaricamazza, Illari Salvatori, Alberto Ferri, Cristiana Valle, Valeria Manganelli, Tina Garofalo, Maurizio Sorice, Roberta Misasi

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

44 citing papers in PubMed, 1 synthesis or guideline pooled it.

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  9. Evaluation of a New Methylimidazole-Containing Thiosemicarbazone as a CuChemistry (Weinheim an der Bergstrasse, Germany) · 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

9 authors.

Niccolò CandeliseFondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
Silvia ScaricamazzaFondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
Illari SalvatoriFondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
Alberto FerriFondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
Cristiana ValleFondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
Valeria ManganelliDepartment of Experimental Medicine, University of Rome "La Sapienza", 00161 Rome, Italy.
Tina GarofaloDepartment of Experimental Medicine, University of Rome "La Sapienza", 00161 Rome, Italy.ORCID 0000-0003-0645-2510
Maurizio SoriceDepartment of Experimental Medicine, University of Rome "La Sapienza", 00161 Rome, Italy.
Roberta MisasiDepartment of Experimental Medicine, University of Rome "La Sapienza", 00161 Rome, Italy.

Funding

Fondazione Umberto Veronesi PostDoc fellowship 2021 NCMinistero dell'Istruzione, dell'Università e della Ricerca PRIN 2017 SNRXH3
6 · The paper itself

Abstract

Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined three-dimensional structure. Conformational changes in intrinsically disordered regions of a protein lead to unstable β-sheet enriched intermediates, which are stabilized by intermolecular interactions with other β-sheet enriched molecules, producing stable proteinaceous aggregates. Upon misfolding, several pathways may be undertaken depending on the composition of the amino acidic string and the surrounding environment, leading to different structures. Accumulating evidence is suggesting that the conformational state of a protein may initiate signalling pathways involved both in pathology and physiology. In this review, we will summarize the heterogeneity of structures that are produced from intrinsically disordered protein domains and highlight the routes that lead to the formation of physiological liquid droplets as well as pathogenic aggregates. The most common proteins found in aggregates in neurodegenerative diseases and their structural variability will be addressed. We will further evaluate the clinical relevance and future applications of the study of the structural heterogeneity of protein aggregates, which may aid the understanding of the phenotypic diversity observed in neurodegenerative disorders.

Indexed as

Protein Conformation, beta-Strandalpha-SynucleinAmyloidHumansIntrinsically Disordered ProteinsNeurodegenerative DiseasesProtein AggregatesProtein Aggregation, Pathologicaltau Proteinsalpha-SynucleinAmyloidIntrinsically Disordered ProteinsProtein Aggregatestau Proteinsalpha synucleinamyloid betaintrinsic disorderneurodegenerative diseasephase separationprion proteinprotein aggregationtauTDP-43

Identifiers

PMID34199513
PMCPMC8199687

What OpenQuestion holds

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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.