ReviewCurrent genetics2016
Protein aggregation as a mechanism of adaptive cellular responses.
Review in Current genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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.
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.
Who cites it
39 citing papers in PubMed.
- VAEBAC: a representation-learning framework for proteome-scale prediction of amyloidogenic proteins and functional stratification of nucleic-acid-binding proteins.Bioinformatics (Oxford, England) · 2026Article
- Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum.BMC molecular and cell biology · 2026Article
- Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024Review
- Artificial Hsp104-mediated systems for re-localizing protein aggregates.Nature communications · 2023Article
- Human gasdermin D and MLKL disrupt mitochondria, endocytic traffic and TORC1 signalling in budding yeast.Open biology · 2023Article
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved.The Journal of cell biology · 2022Article
- Nst1, Densely Associated to P-Body in the Post-Exponential Phases ofInternational journal of molecular sciences · 2022Article
- Review
- Aggregation is a Context-Dependent Constraint on Protein Evolution.Frontiers in molecular biosciences · 2021Article
- ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.Nature communications · 2020Article
- Native aggregation is a common feature among triosephosphate isomerases of different species.Scientific reports · 2020Article
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
- HspX promotes the polar localization of mycobacterial protein aggregates.Scientific reports · 2019Article
- Proteostasis collapse, a hallmark of aging, hinders the chaperone-Start network and arrests cells in G1.eLife · 2019Article
- An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells.Current genetics · 2019Article
- Review
- Emerging roles for sphingolipids in cellular aging.Current genetics · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coalescence of proteins into different types of intracellular bodies has surfaced as a widespread adaptive mechanism to re-organize cells and cellular functions in response to specific cues. These structures, composed of proteins or protein-mRNA-complexes, regulate cellular processes through modulating enzymatic activities, gene expression or shielding macromolecules from damage. Accordingly, such bodies are associated with a wide-range of processes, including meiosis, memory-encoding, host-pathogen interactions, cancer, stress responses, as well as protein quality control, DNA replication stress and aneuploidy. Importantly, these distinct coalescence responses are controlled, and in many cases regulated by chaperone proteins. While cells can tolerate and proficiently coordinate numerous distinct types of protein bodies, some of them are also intimately linked to diseases or the adverse effects of aging. Several protein bodies that differ in composition, packing, dynamics, size, and localization were originally discovered in budding yeast. Here, we provide a concise and comparative review of their nature and nomenclature.
Indexed as
Identifiers
27032776What OpenQuestion holds
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.