ArticlePLoS computational biology2011
An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.
Article in PLoS computational biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Article
- Synaptic proteins that aggregate and degrade slower with aging accumulate in microglia.bioRxiv : the preprint server for biology · 2025Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation.Nature communications · 2023Article
- LISTERIN E3 Ubiquitin Ligase and Ribosome-Associated Quality Control (RQC) Mechanism.Molecular neurobiology · 2021Review
- A large consanguineous family with a homozygous Metabotropic Glutamate Receptor 7 (mGlu7) variant and developmental epileptic encephalopathy: Effect on protein structure and ligand affinity.Orphanet journal of rare diseases · 2021Article
- Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association.Computational and structural biotechnology journal · 2021Article
- Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.Computational and structural biotechnology journal · 2020Review
- Hypothesis: protein and RNA attributes are continuously optimized over time.BMC genomics · 2019Article
- The fitness cost and benefit of phase-separated protein deposits.Molecular systems biology · 2019Article
- A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution.Genetics · 2019Article
- Protein Degradation Rate inThe Plant cell · 2017Article
- Structural hot spots for the solubility of globular proteins.Nature communications · 2016Article
- Positional proteomics reveals differences in N-terminal proteoform stability.Molecular systems biology · 2016Article
- Article
- Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms.PLoS computational biology · 2015Article
- Proteome response at the edge of protein aggregation.Open biology · 2015Article
- Evolution of Robustness to Protein Mistranslation by Accelerated Protein Turnover.PLoS biology · 2015Article
- Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.The Journal of biological chemistry · 2014Article
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6 authors.
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Abstract
We previously showed the existence of selective pressure against protein aggregation by the enrichment of aggregation-opposing 'gatekeeper' residues at strategic places along the sequence of proteins. Here we analyzed the relationship between protein lifetime and protein aggregation by combining experimentally determined turnover rates, expression data, structural data and chaperone interaction data on a set of more than 500 proteins. We find that selective pressure on protein sequences against aggregation is not homogeneous but that short-living proteins on average have a higher aggregation propensity and fewer chaperone interactions than long-living proteins. We also find that short-living proteins are more often associated to deposition diseases. These findings suggest that the efficient degradation of high-turnover proteins is sufficient to preclude aggregation, but also that factors that inhibit proteasomal activity, such as physiological ageing, will primarily affect the aggregation of short-living proteins.
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