ArticleNature chemical biology2016
An in vivo platform for identifying inhibitors of protein aggregation.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 85 citations in OpenAlex.
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- Complementation Dependent Enzyme Prodrug Therapy Enables Targeted Activation of Prodrug on HER2-Positive Cancer Cells.ACS medicinal chemistry letters · 2022Article
- The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An enzyme-based biosensor for monitoring and engineering protein stability in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Generation of highly selective monoclonal antibodies inhibiting a recalcitrant protease using decoy designs.Biotechnology and bioengineering · 2020Article
- Computational Investigation of Gantenerumab and Crenezumab Recognition of Aβ Fibrils in Alzheimer's Disease Brain Tissue.ACS chemical neuroscience · 2020Article
- Detecting protein-protein interactions by Xe-129 NMR.Chemical communications (Cambridge, England) · 2020Article
- An in vivo platform to select and evolve aggregation-resistant proteins.Nature communications · 2020Article
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
- Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity.Biochemistry · 2020Article
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10 authors at 3 institutions in 1 country.
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Abstract
Protein aggregation underlies an array of human diseases, yet only one small-molecule therapeutic targeting this process has been successfully developed to date. Here, we introduce an in vivo system, based on a β-lactamase tripartite fusion construct, that is capable of identifying aggregation-prone sequences in the periplasm of Escherichia coli and inhibitors that prevent their aberrant self-assembly. We demonstrate the power of the system using a range of proteins, from small unstructured peptides (islet amyloid polypeptide and amyloid β) to larger, folded immunoglobulin domains. Configured in a 48-well format, the split β-lactamase sensor readily differentiates between aggregation-prone and soluble sequences. Performing the assay in the presence of 109 compounds enabled a rank ordering of inhibition and revealed a new inhibitor of islet amyloid polypeptide aggregation. This platform can be applied to both amyloidogenic and other aggregation-prone systems, independent of sequence or size, and can identify small molecules or other factors able to ameliorate or inhibit protein aggregation.
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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.