ArticleScientific reports2016
Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Nascent protein retention at polysomes reduces kinetic barriers to self-assembly.bioRxiv : the preprint server for biology · 2026Article
- Shifts in protein aggregate stability define proteostasis decline in the aging human brain.bioRxiv : the preprint server for biology · 2026Article
- Proteostasis breakdown and aggregate diversity in aging and neurodegenerative disease.Frontiers in aging neuroscience · 2026Review
- Transcription factor MITF regulates masseter muscle growth and development.Physiological reports · 2025Article
- Insulin resistance: fueling oxidative stress and neurodegeneration.Journal of neural transmission (Vienna, Austria : 1996) · 2025Review
- Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging.Journal of experimental botany · 2025Review
- Lon-dependent proteolysis in oxidative stress responses.Journal of bacteriology · 2025Review
- Explainable Deep Multilevel Attention Learning for Predicting Protein Carbonylation Sites.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Chronic Vanadium Exposure Promotes Aggregation of Alpha-Synuclein, Tau and Amyloid Beta in Mouse Brain.Journal of neurochemistry · 2025Article
- Exercise training decreases the load and changes the content of circulating SDS-resistant protein aggregates in patients with heart failure with reduced ejection fraction.Molecular and cellular biochemistry · 2024Article
- Nitrooxidative Stress and Neuroinflammation Caused by Air Pollutants Are Associated with the Biological Markers of Neurodegenerative Diseases.Antioxidants (Basel, Switzerland) · 2024Review
- Emerging Microfluidic Tools for Simultaneous Exosomes and Cargo Biosensing in Liquid Biopsy: New Integrated Miniaturized FFF-Assisted Approach for Colon Cancer Diagnosis.Sensors (Basel, Switzerland) · 2023Review
- A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.PLoS biology · 2023Article
- Article
- Age-Related Changes in Post-Translational Modifications of Proteins from Whole Male and Female Skeletal Elements.Molecules (Basel, Switzerland) · 2023Article
- Iron scavenging and suppression of collagen cross-linking underlie antifibrotic effects of carnosine in the heart with obesity.Frontiers in pharmacology · 2023Article
- Protein homeostasis in the aged and diseased heart.The journal of cardiovascular aging · 2023Article
- A Proteome-Centric View of Ageing, including that of the Skin and Age-Related Diseases: Considerations of a Common Cause and Common Preventative and Curative Interventions.Clinical, cosmetic and investigational dermatology · 2023Review
- Young transgenic hMTH1 mice are protected against dietary fat-induced metabolic stress-implications for enhanced longevity.Aging cell · 2022Article
- Estimation of Redox Status in Military Pilots during Hypoxic Flight-Simulation Conditions-A Pilot Study.Antioxidants (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Protein aggregation is a common biological phenomenon, observed in different physiological and pathological conditions. Decreased protein solubility and a tendency to aggregate is also observed during physiological aging but the causes are currently unknown. Herein we performed a biophysical separation of aging-related high molecular weight aggregates, isolated from the bone marrow and splenic cells of aging mice and followed by biochemical and mass spectrometric analysis. The analysis indicated that compared to younger mice an increase in protein post-translational carbonylation was observed. The causative role of these modifications in inducing protein misfolding and aggregation was determined by inducing carbonyl stress in young mice, which recapitulated the increased protein aggregation observed in old mice. Altogether our analysis indicates that oxidative stress-related post-translational modifications accumulate in the aging proteome and are responsible for increased protein aggregation and altered cell proteostasis.
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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.