ReviewCold Spring Harbor perspectives in biology2019
Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis.
Review in Cold Spring Harbor perspectives in biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Assessing Surface Binding Events on Golgi Microsomes Isolated from Cancer Cells by Capillary Electrophoresis.Analytical chemistry · 2026Article
- FuzDrop: sequence-based prediction of the propensity of proteins for liquid-liquid phase separation and aggregation.Nature protocols · 2026Review
- Shifts in protein aggregate stability define proteostasis decline in the aging human brain.bioRxiv : the preprint server for biology · 2026Article
- Development of production methodologies for scFv-Fc conjugated critical reagents to support CAR-T clinical programs.Bioanalysis · 2025Article
- Artificial intelligence in drug development for delirium and Alzheimer's disease.Acta pharmaceutica Sinica. B · 2025Review
- Amyloid-forming property of the N-terminal 1-70 residues of human apolipoprotein A-IV.Scientific reports · 2025Article
- A comprehensive overview of recent advances in generative models for antibodies.Computational and structural biotechnology journal · 2024Review
- Alzheimer's Disease Immunotherapy and Mimetic Peptide Design for Drug Development: Mutation Screening, Molecular Dynamics, and a Quantum Biochemistry Approach Focusing on Aducanumab::Aβ2-7 Binding Affinity.ACS chemical neuroscience · 2024Article
- Altered molecular and cellular mechanisms in KIF5A-associated neurodegenerative or neurodevelopmental disorders.Cell death & disease · 2024Article
- Automated optimization of the solubility of a hyper-stable α-amylase.Open biology · 2024Article
- ADH-Enhancer: an attention-based deep hybrid framework for enhancer identification and strength prediction.Briefings in bioinformatics · 2024Article
- Widespread amyloid aggregates formation by Zika virus proteins and peptides.Protein science : a publication of the Protein Society · 2023Article
- Automated optimisation of solubility and conformational stability of antibodies and proteins.Nature communications · 2023Article
- Multidimensional Protein Solubility Optimization with an Ultrahigh-Throughput Microfluidic Platform.Analytical chemistry · 2023Article
- Sequence-based prediction of pH-dependent protein solubility using CamSol.Briefings in bioinformatics · 2023Article
- The RESP AI model accelerates the identification of tight-binding antibodies.Nature communications · 2023Article
- An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.Chemical science · 2022Article
- Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.Biochemistry · 2022Article
- Cell-Penetrating Peptides with Unexpected Anti-Amyloid Properties.Pharmaceutics · 2022Review
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2 authors.
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Abstract
One of the major functions of the protein homeostasis system is to maintain proteins in their soluble states, and indeed several human disorders are associated with the aberrant aggregation of proteins. An active involvement of the protein homeostasis system is necessary to avoid aggregation because proteins are expressed at levels close to their solubility limits, hence being poorly soluble. The mechanisms by which the protein homeostasis system acts to control protein aggregation are, however, still not known in much detail. To facilitate systematic investigations of these mechanisms, we describe here the CamSol method of predicting protein solubility, and illustrate its initial applications. We anticipate that with the advent of powerful proteomics and transcriptomic methods, in combination with the use of the CamSol method and related approaches to predict the solubility and other biophysical properties of proteins, it will become possible to increase our understanding of the principles of protein homeostasis related to the maintenance of the proteome in its soluble form.
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