Evidence map›Paper›PMID 36052548›Full record

ArticleDisease models & mechanisms2022

Integrated multi-omics analysis of Huntington disease identifies pathways that modulate protein aggregation.

Sai S Pradhan, Sai M Thota, Saiswaroop Rajaratnam, Sai K S Bhagavatham, Sujith K Pulukool, Sriram Rathnakumar, Kanikaram S Phalguna, Rajesh B Dandamudi, Ashish Pargaonkar, Prasanth Joseph and 2 more

Open access · goldAbstract read
In one paragraph

Article in Disease models & mechanisms, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 21 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

12 authors at 3 institutions in 1 country.

Sai S PradhanDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0002-5461-8047
Sai M ThotaDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0003-1710-5645
Saiswaroop RajaratnamDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0001-7163-5263
Sai K S BhagavathamDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0003-2236-5847
Sujith K PulukoolDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0003-4098-6233
Sriram RathnakumarDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0002-7656-4027
Kanikaram S PhalgunaDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0001-8972-7983
Rajesh B DandamudiDepartment of Chemistry, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh 515 134, India.ORCID 0000-0002-5638-2242
Ashish PargaonkarApplication Division, Agilent Technologies Ltd., Bengaluru 560048, India.
Prasanth JosephApplication Division, Agilent Technologies Ltd., Bengaluru 560048, India.
E V JoshyDepartment of Neurology, Sri Sathya Sai Institute of Higher Medical Sciences, Whitefield, Bengaluru, Karnataka 560066, India.
Venketesh SivaramakrishnanDisease Biology Lab, Department of Biosciences, Sri Sathya Sai Institute of Higher Learning, Prasanthi Nilayam, Anantapur, Andhra Pradesh, India515134.ORCID 0000-0003-3094-5905
Sri Sathya Sai Institute of Higher Learning · INAgilent Technologies (India) · INSri Sathya Sai Institute of Higher Medical Sciences · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Huntington disease (HD) is a neurodegenerative disease associated with polyglutamine expansion in the protein huntingtin (HTT). Although the length of the polyglutamine repeat correlates with age at disease onset and severity, psychological, cognitive and behavioral complications point to the existence of disease modifiers. Mitochondrial dysfunction and metabolic deregulation are both associated with the HD but, despite multi-omics characterization of patients and model systems, their mechanisms have remained elusive. Systems analysis of multi-omics data and its validation by using a yeast model could help to elucidate pathways that modulate protein aggregation. Metabolomics analysis of HD patients and of a yeast model of HD was, therefore, carried out. Our analysis showed a considerable overlap of deregulated metabolic pathways. Further, the multi-omics analysis showed deregulated pathways common in human, mice and yeast model systems, and those that are unique to them. The deregulated pathways include metabolic pathways of various amino acids, glutathione metabolism, longevity, autophagy and mitophagy. The addition of certain metabolites as well as gene knockouts targeting the deregulated metabolic and autophagy pathways in the yeast model system showed that these pathways do modulate protein aggregation. Taken together, our results showed that the modulation of deregulated pathways influences protein aggregation in HD, and has implications for progression and prognosis. This article has an associated First Person interview with the first author of the paper.

Indexed as

Huntington DiseaseNeurodegenerative DiseasesAnimalsDisease Models, AnimalHumansHuntingtin ProteinMiceNerve Tissue ProteinsProtein AggregatesSaccharomyces cerevisiaeHuntingtin ProteinNerve Tissue ProteinsProtein AggregatesHD yeast modelHuntington diseaseMetabolomicsMulti-omics analysisNeurodegenerative diseaseProtein aggregation

Identifiers

PMID36052548
PMCPMC10655815
OpenAlexW4294190643

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.