Evidence map›Paper›PMID 25386560›Full record

ReviewBioMed research international2014

Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin.

Panchanan Maiti, Jayeeta Manna, Shobi Veleri, Sally Frautschy

Open access · hybridAbstract readReview
In one paragraph

Review in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 117 citations in OpenAlex.

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  19. Beneficial Effects of Epigallocatechin-3-Molecules (Basel, Switzerland) · 2021
    Review
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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

4 authors at 3 institutions in 1 country.

Panchanan MaitiDepartment of Neurology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.ORCID 0000-0001-5151-3330
Jayeeta MannaDepartment of Physiology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.ORCID 0000-0002-2839-510X
Shobi VeleriNeurobiology-Neurodegeneration and Repair Laboratory, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0002-9653-6939
Sally FrautschyVeteran's Greater Los Angeles Healthcare System, Geriatric Research and Educational Core, Los Angeles, CA 90073, USA ; Departments of Neurology and Medicine, University of California at Los Angeles, Los Angeles, CA 90095, USA.
University of Tennessee Health Science Center · USNational Institutes of Health · USUniversity of California, Los Angeles · US

Funding

Transgenic Mouse Models of Huntington's DiseaseR01NS041574 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEVINE, MICHAEL S. · 2002 to 2016
$5.4M
Preclinical Pharmacogenomics and Synaptic Biomarkers for Alzheimer's DiseaseR01AT006816 · NCCIH · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COLE, GREGORY M, FRAUTSCHY, SALLY ANN · 2011 to 2015
$1.9M
Human tau neurodegeneration in Alzheimer'sR01AG021975 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FRAUTSCHY, SALLY ANN · 2004 to 2008
$1.2M
Polyphenolic Interventions for tau Pathogenesis in Alzheimers ModelsI01BX001257 · VA · VA GREATER LOS ANGELES HEALTHCARE SYSTEM · PI FRAUTSCHY, SALLY ANN · 2013 to 2016
–
Curcumin and Yoga Exercise Effects in Veterans at Risk for Alzheimer's DiseaseI01RX000669 · VA · VA GREATER LOS ANGELES HEALTHCARE SYSTEM · PI FRAUTSCHY, SALLY ANN · 2015 to 2015
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BLRD VA I01 BX001257NCCIH NIH HHS R01 AT006816NCCIH NIH HHS RC1AT006816NIA NIH HHS R01 AG021975NIA NIH HHS R01AG021975NINDS NIH HHS R01 NS041574NINDS NIH HHS R01 (NS41574)RRD VA I01 RX000669
6 · The paper itself

Abstract

The intra- and extracellular accumulation of misfolded and aggregated amyloid proteins is a common feature in several neurodegenerative diseases, which is thought to play a major role in disease severity and progression. The principal machineries maintaining proteostasis are the ubiquitin proteasomal and lysosomal autophagy systems, where heat shock proteins play a crucial role. Many protein aggregates are degraded by the lysosomes, depending on aggregate size, peptide sequence, and degree of misfolding, while others are selectively tagged for removal by heat shock proteins and degraded by either the proteasome or phagosomes. These systems are compromised in different neurodegenerative diseases. Therefore, developing novel targets and classes of therapeutic drugs, which can reduce aggregates and maintain proteostasis in the brains of neurodegenerative models, is vital. Natural products that can modulate heat shock proteins/proteosomal pathway are considered promising for treating neurodegenerative diseases. Here we discuss the current knowledge on the role of HSPs in protein misfolding diseases and knowledge gained from animal models of Alzheimer's disease, tauopathies, and Huntington's diseases. Further, we discuss the emerging treatment regimens for these diseases using natural products, like curcumin, which can augment expression or function of heat shock proteins in the cell.

Indexed as

Alzheimer DiseaseCurcuminHeat-Shock ProteinsHumansHuntington DiseaseMolecular ChaperonesNeurodegenerative DiseasesProtein Aggregation, PathologicalProtein FoldingProteostasis DeficienciesUbiquitinCurcuminHeat-Shock ProteinsMolecular ChaperonesUbiquitin

Identifiers

PMID25386560
PMCPMC4217372
OpenAlexW2087647407

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.