Evidence map›Paper›PMID 28652376›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.

Rishika Kundra, Prajwal Ciryam, Richard I Morimoto, Christopher M Dobson, Michele Vendruscolo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

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

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  11. Article
  12. Review
  13. Review
  14. Protein Aggregates and Aggrephagy in Myopathies.International journal of molecular sciences · 2023
    Review
  15. Structural polymorphism and cytotoxicity of brain-derived β-amyloid extracts.Protein science : a publication of the Protein Society · 2023
    Review
  16. Protein homeostasis in aging and cancer.Frontiers in cell and developmental biology · 2023
    Review
  17. Review
  18. Endosomal Acid-Base Homeostasis in Neurodegenerative Diseases.Reviews of physiology, biochemistry and pharmacology · 2023
    Article
  19. Review
  20. 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

5 authors.

Rishika KundraCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Prajwal CiryamCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Richard I MorimotoDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208.
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; mv245@cam.ac.uk.

Funding

C. elegans Model for Neurodegenerative Diseases of AgingR37AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2010 to 2019
$3.9M
Regulation of Peripheral ProteostasisRF1AG057296 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2017 to 2017
$3.0M
NIA NIH HHS R37 AG026647NIA NIH HHS RF1 AG057296
6 · The paper itself

Abstract

Alzheimer's disease is the most common cause of dementia. A hallmark of this disease is the presence of aberrant deposits containing by the Aβ peptide (amyloid plaques) and the tau protein (neurofibrillary tangles) in the brains of affected individuals. Increasing evidence suggests that the formation of these deposits is closely associated with the age-related dysregulation of a large set of highly expressed and aggregation-prone proteins, which make up a metastable subproteome. To understand in more detail the origins of such dysregulation, we identify specific components of the protein homeostasis system associated with these metastable proteins by using a gene coexpression analysis. Our results reveal the particular importance of the protein trafficking and clearance mechanisms, including specific branches of the endosomal-lysosomal and ubiquitin-proteasome systems, in maintaining the homeostasis of the metastable subproteome associated with Alzheimer's disease.

Indexed as

AgingHomeostasisAlzheimer DiseaseBrainCase-Control StudiesCluster AnalysisEndosomesGene Expression ProfilingGene Expression RegulationGenome-Wide Association StudyHippocampusHumansLysosomesNeurofibrillary TanglesOligonucleotide Array Sequence AnalysisPlaque, AmyloidProteasome Endopeptidase ComplexProteinsProteometau ProteinsUbiquitinAlzheimer’s diseaseprotein aggregationprotein homeostasissupersaturation

Identifiers

PMID28652376
PMCPMC5514703

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.