References

Adapting proteostasis for disease intervention

10.1126/science.1141448 · 2008 · External reference

Biological and chemical approaches to diseases of proteostasis deficiency

10.1146/annurev.biochem.052308.114844 · 2009 · External reference

The biology of proteostasis in aging and disease

10.1146/annurev-biochem-060614-033955 · 2015 · External reference

The proteostasis network and its decline in ageing

10.1038/s41580-019-0101-y · 2019 · External reference

The amyloid state and its association with protein misfolding diseases

10.1038/nrm3810 · 2014 · External reference

Liquid–liquid phase separation in biology

10.1146/annurev-cellbio-100913-013325 · 2014 · External reference

Biomolecular condensates: organizers of cellular biochemistry

10.1038/nrm.2017.7 · 2017 · External reference

Liquid phase condensation in cell physiology and disease

10.1126/science.aaf4382 · 2017 · External reference

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing

10.1038/s41580-020-00326-6 · 2021 · External reference

Generic nature of the condensed states of proteins

10.1038/s41556-021-00697-8 · 2021 · External reference

Amyloid formation as a protein phase transition

10.1038/s42254-023-00598-9 · 2023 · External reference

Molecular determinants of condensate composition

10.1016/j.molcel.2024.12.021 · 2025 · External reference

The molecular basis for cellular function of intrinsically disordered protein regions

10.1038/s41580-023-00673-0 · 2024 · External reference

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins

10.1016/j.celrep.2013.09.043 · 2013 · External reference

Proteome-wide observation of the phenomenon of life on the edge of solubility

10.1073/pnas.1910444117 · 2020 · External reference

The thermodynamic hypothesis of protein aggregation

10.1016/j.mam.2025.101364 · 2025 · External reference

Unresolved reference

1990 · External reference

Conformational selection in the molten globule state of the nuclear coactivator binding domain of cbp

10.1073/pnas.1001693107 · 2010 · External reference

A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins

10.1073/pnas.2113572119 · 2022 · External reference

Substitutions at nonconserved rheostat positions modulate function by rewiring long-range, dynamic interactions

10.1093/molbev/msaa202 · 2021 · External reference

Rheostats and toggle switches for modulating protein function

10.1371/journal.pone.0083502 · 2013 · External reference

Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms

10.1073/pnas.2313465121 · 2024 · External reference

Aggregation of α-synuclein splice isoforms through a phase separation pathway

10.1126/sciadv.adq5396 · 2025 · External reference

How many human proteoforms are there?

10.1038/nchembio.2576 · 2018 · External reference

Widespread occurrence of the droplet state of proteins in the human proteome

10.1073/pnas.2007670117 · 2020 · External reference

Tunable metastability of condensates reconciles their dual roles in amyloid fibril formation

10.1016/j.molcel.2025.05.011 · 2025 · External reference

Misfolded proteins partition between two distinct quality control compartments

10.1038/nature07195 · 2008 · External reference

Differential scales of protein quality control

10.1016/j.cell.2014.03.007 · 2014 · External reference

Aging as an event of proteostasis collapse

10.1101/cshperspect.a004440 · 2011 · External reference

Proteostasis and aging

10.1038/nm.4001 · 2015 · External reference

Friend or foe—post-translational modifications as regulators of phase separation and RNP granule dynamics

10.1074/jbc.tm118.001189 · 2019 · External reference

Post-translational modifications in liquid–liquid phase separation: a comprehensive review

10.1186/s43556-022-00075-2 · 2022 · External reference

Modulating biomolecular condensates: a novel approach to drug discovery

10.1038/s41573-022-00505-4 · 2022 · External reference

Protein condensation diseases: therapeutic opportunities

10.1038/s41467-022-32940-7 · 2022 · External reference

Adapting the proteostasis capacity to sustain brain healthspan

10.1016/j.cell.2021.02.007 · 2021 · External reference

A CFTR potentiator in patients with cystic fibrosis and the g551d mutation

10.1056/nejmoa1105185 · 2011 · External reference

Elexacaftor–tezacaftor–ivacaftor for cystic fibrosis with a single phe508del allele

10.1056/nejmoa1908639 · 2019 · External reference

Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade

10.1073/pnas.1121005109 · 2012 · External reference

Small-molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregation

10.1016/j.sbi.2021.11.009 · 2022 · External reference

Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation

10.1080/17460441.2023.2221024 · 2023 · External reference

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

10.1038/s41467-024-47585-x · 2024 · External reference

Interplay of proteostasis capacity and protein aggregation: implications for cellular function and disease

10.1016/j.jmb.2024.168615 · 2024 · External reference

Reshaping endoplasmic reticulum quality control through the unfolded protein response

10.1016/j.molcel.2022.03.025 · 2022 · External reference

Systems-level organization of extracellular proteostasis

10.1126/science.aed3712 · 2026 · External reference