ArticleMethods in molecular biology (Clifton, N.J.)2012
Cyclic amplification of prion protein misfolding.
Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Quantitative measurements of α-synuclein seeds in CSF inform diagnosis of synucleinopathies.Journal of Parkinson's disease · 2025Article
- Protein mimetic 2D FAST rescues alpha synuclein aggregation mediated early and post disease Parkinson's phenotypes.Nature communications · 2024Article
- Unveiling the Potential of Enzymatic Detergents to Deactivate Infectious Prions.Biomedical instrumentation & technology · 2024Article
- Conservation of vCJD Strain Properties After Extraction and In Vitro Propagation of PrPMolecular neurobiology · 2023Article
- Development of a sensitive real-time quaking-induced conversion (RT-QuIC) assay for application in prion-infected blood.PloS one · 2023Article
- A microfluidic biosensor for the diagnosis of chronic wasting disease.Microsystems & nanoengineering · 2023Article
- Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly.Nature communications · 2022Article
- Pursuing Multiple Biomarkers for Early Idiopathic Parkinson's Disease Diagnosis.Molecular neurobiology · 2021Review
- Aldehyde Production as a Calibrant of Ultrasonic Power Delivery During Protein Misfolding Cyclic Amplification.The protein journal · 2020Article
- Proteopathic Seed Amplification Assays for Neurodegenerative Disorders.Clinics in laboratory medicine · 2020Review
- Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation.PLoS pathogens · 2020Article
- ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization.Frontiers in molecular neuroscience · 2019Article
- Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Modified Protein Misfolding Cyclic Amplification Overcomes Real-Time Quaking-Induced Conversion Assay Inhibitors in Deer Saliva To Detect Chronic Wasting Disease Prions.Journal of clinical microbiology · 2018Article
- Prion disease: experimental models and reality.Acta neuropathologica · 2017Review
- Prions efficiently cross the intestinal barrier after oral administration: Study of the bioavailability, and cellular and tissue distribution in vivo.Scientific reports · 2016Article
- Review
- Molecular barriers to zoonotic transmission of prions.Emerging infectious diseases · 2014Article
- Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seeds.The Journal of biological chemistry · 2013Article
- Article
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3 authors.
Funding
Abstract
Protein misfolding cyclic amplification (PMCA) is a technique that takes advantage of the nucleation-dependent prion replication process to accelerate the conversion of PrP(C) into PrP(Sc) in the test tube. PMCA uses ultrasound waves to fragment the PrP(Sc) polymers, increasing the amount of seeds present in the infected sample without affecting their ability to act as conversion nuclei. Over the past 5 years, PMCA has become an invaluable technique to study diverse aspects of prions. The PMCA technology has been used by several groups to understand the molecular mechanism of prion replication, the cellular factors involved in prion propagation, the intriguing phenomena of prion strains and species barriers, to detect PrP(Sc) in tissues and biological fluids, and to screen for inhibitors against prion replication. In this chapter, we describe a detailed protocol of the PMCA technique, highlighting some of the important technical aspects to obtain a successful and reproducible application of the technology.
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