Evidence map›Paper›PMID 34407725›Full record

ArticleAutophagy2021

Protein aggregation and autophagy dysfunction: new lessons from mucopolysaccharidoses.

Antonio Monaco, Alessandro Fraldi

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 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
1.3field-weighted citation impact, top 20% 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, 13 citations in OpenAlex.

  1. Cystinosis and Cellular Energy Failure: Mitochondria at the Crossroads.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Roles of the Oxytocin Receptor (OXTR) in Human Diseases.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Review
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

2 authors at 1 institution in 1 country.

Antonio MonacoCEINGE Biotecnologie Avanzate, Naples, Italy; Department of Translational Medicine, University of Naples "Federico II", Naples, Italy.
Alessandro FraldiCEINGE Biotecnologie Avanzate, Naples, Italy; Department of Translational Medicine, University of Naples "Federico II", Naples, Italy.ORCID 0000-0002-7795-0720
Ceinge Biotecnologie Avanzate (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mucopolysaccharidoses (MPS) are inherited metabolic diseases with strong neurological involvement. MPSs are caused by defects in lysosomal enzymes involved in the degradation of glycosaminoglycans (GAGs), which consequently accumulate into the lysosomes as primary storage. Macroautophagy/autophagy impairment is well known to drive neurodegeneration in MPSs, however, mechanisms underlying such dysfunction are still poorly understood. Recently, by studying a mouse model for MPS-III (Sanfilippo syndrome) we have shown that the progressive aggregation of amyloid proteins in neuronal cell bodies occurs downstream of the GAG storage and, in turn, impairs the autophagy pathway by affecting lysosomal-dependent autophagosome clearance.

Indexed as

AutophagyAnimalsHumansLysosomesMucopolysaccharidosesProtein Aggregation, PathologicalAutophagylysosomal storage diseaseslysosomemucopolysaccharidosesprotein aggregation

Identifiers

PMID34407725
PMCPMC8632274
OpenAlexW3193912813

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.