Evidence map›Paper›PMID 27120560›Full record

ReviewCellular and molecular life sciences : CMLS2016

The fine-tuning of proteolytic pathways in Alzheimer's disease.

Valentina Cecarini, Laura Bonfili, Massimiliano Cuccioloni, Matteo Mozzicafreddo, Mauro Angeletti, Jeffrey N Keller, Anna Maria Eleuteri

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Valentina CecariniDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy. valentina.cecarini@unicam.it.
Laura BonfiliDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy.
Massimiliano CuccioloniDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy.
Matteo MozzicafreddoDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy.
Mauro AngelettiDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy.
Jeffrey N KellerPennington Biomedical Research Centre, Louisiana State University System, Baton Rouge, LA, 70808, USA.
Anna Maria EleuteriDepartment of Biosciences and Veterinary Medicine, School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III da Varano, 62032, Camerino, Italy.
Università di Camerino · ITLouisiana State University System · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several integrated proteolytic systems contribute to the maintenance of cellular homeostasis through the continuous removal of misfolded, aggregated or oxidized proteins and damaged organelles. Among these systems, the proteasome and autophagy play the major role in protein quality control, which is a fundamental issue in non-proliferative cells such as neurons. Disturbances in the functionality of these two pathways are frequently observed in neurodegenerative diseases, like Alzheimer's disease, and reflect the accumulation of protease-resistant, deleterious protein aggregates. In this review, we explored the sophisticated crosstalk between the ubiquitin-proteasome system and autophagy in the removal of the harmful structures that characterize Alzheimer's disease neurons. We also dissected the role of the numerous shuttle factors and chaperones that, directly or indirectly interacting with ubiquitin and LC3, are used for cargo selection and delivery to one pathway or the other.

Indexed as

Alzheimer DiseaseAutophagyHumansMicrotubule-Associated ProteinsMolecular ChaperonesNeuronsProteasome Endopeptidase ComplexProteolysisUbiquitinMAP1LC3A protein, humanMicrotubule-Associated ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinAlzheimer’s diseaseAutophagyChaperoneProteasomeUbiquitin

Identifiers

PMID27120560
PMCPMC11108445
OpenAlexW2342707808

What OpenQuestion holds

Textmetadata
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.