ArticleBiochemistry2011
Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Observation of pH-Dependent Residual Structure in the Pmel17 Repeat Domain and the Implication for Its Amyloid Formation.Biochemistry · 2023Article
- Monitoring Kinetics of pH-Dependent Aggregation and Disaggregation of the Pmel17 Repeat Domain.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Purification and characterization of an amyloidogenic repeat domain from the functional amyloid Pmel17.Protein expression and purification · 2021Article
- Linking Parkinson's Disease and Melanoma: Interplay Between α-Synuclein and Pmel17 Amyloid Formation.Movement disorders : official journal of the Movement Disorder Society · 2021Review
- Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17.The Journal of biological chemistry · 2020Article
- Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17.Journal of molecular biology · 2018Review
- Why are Functional Amyloids Non-Toxic in Humans?Biomolecules · 2017Review
- Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Israel journal of chemistry · 2017Article
- A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.Journal of computer-aided molecular design · 2016Article
- Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Journal of molecular biology · 2014Article
- Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.Biochemistry · 2014Article
- Molecular origin of pH-dependent fibril formation of a functional amyloid.Chembiochem : a European journal of chemical biology · 2014Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Pmel17 is a human amyloid involved in melanin synthesis. A fragment of Pmel17, the repeat domain (RPT) rich in glutamic acids, forms amyloid only at mildly acidic pH. Unlike pathological amyloids, these fibrils dissolve at neutral pH, supporting a reversible aggregation-disaggregation process. Here, we study RPT dissolution using atomic force microscopy and solution-state nuclear magnetic resonance spectroscopy. Our results reveal asymmetric fibril disassembly proceeding in the absence of intermediates. We suggest that fibril unfolding involves multiple deprotonation events resulting in electrostatic charge repulsion and filament dissolution.
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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.