ArticleMolecular biology and evolution2008
Natural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm.
Article in Molecular biology and evolution, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed.
- Protein Self-Interaction in Cellular Function and Network Evolution: Molecular Mechanisms, AI-Driven Insights, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- A widespread protein misfolding mechanism is differentially rescued in vitro by chaperones based on gene essentiality.Nature communications · 2025Article
- A widespread protein misfolding mechanism is differentially rescued by chaperones based on gene essentiality.bioRxiv : the preprint server for biology · 2025Article
- A3D Model Organism Database (A3D-MODB): a database for proteome aggregation predictions in model organisms.Nucleic acids research · 2024Article
- Robust and accurate prediction of self-interacting proteins from protein sequence information by exploiting weighted sparse representation based classifier.BMC bioinformatics · 2022Article
- Detection of Protein Aggregation in LiveAntimicrobial agents and chemotherapy · 2020Article
- Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.Computational and structural biotechnology journal · 2020Review
- Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation.Cells · 2019Article
- A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution.Genetics · 2019Article
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
- Random protein sequences can form defined secondary structures and are well-tolerated in vivo.Scientific reports · 2017Article
- Selection on protein structure, interaction, and sequence.Protein science : a publication of the Protein Society · 2016Review
- The influence of selection for protein stability on dN/dS estimations.Genome biology and evolution · 2014Article
- Computational approaches to understanding protein aggregation in neurodegeneration.Journal of molecular cell biology · 2014Review
- A model of proteostatic energy cost and its use in analysis of proteome trends and sequence evolution.PloS one · 2014Article
- Proteome-wide prediction of self-interacting proteins based on multiple properties.Molecular & cellular proteomics : MCP · 2013Article
- Evolutionary capacitance and control of protein stability in protein-protein interaction networks.PLoS computational biology · 2013Article
- Three independent determinants of protein evolutionary rate.Journal of molecular evolution · 2013Review
- Highly abundant proteins favor more stable 3D structures in yeast.Biophysical journal · 2013Article
- Population size dependence of fitness effect distribution and substitution rate probed by biophysical model of protein thermostability.Genome biology and evolution · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein aggregation is the phenomenon of protein self-association potentially leading to detrimental effects on physiology, which is closely related to numerous human diseases such as Alzheimer's and Parkinson's disease. Despite progress in understanding the mechanism of protein aggregation, how natural selection against protein aggregation acts on subunits of protein complexes and on proteins with different contributions to organism fitness remains largely unknown. Here, we perform a proteome-wide analysis by using an experimentally validated algorithm TANGO and utilizing sequence, interactomic and phenotype-based functional genomic data from yeast, fly, and nematode. We find that proteins that are capable of forming homooligomeric complex have lower aggregation propensity compared with proteins that do not function as homooligomer. Further, proteins that are essential to the fitness of an organism have lower aggregation propensity compared with nonessential ones. Our finding suggests that the selection force against protein aggregation acts across different hierarchies of biological system.
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Registered trials
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.