ArticleChembiochem : a European journal of chemical biology2014
Molecular origin of pH-dependent fibril formation of a functional amyloid.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Amyloid formation of alternatively spliced variants of α-synuclein.Protein science : a publication of the Protein Society · 2025Article
- 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
- Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL.Scientific reports · 2021Article
- Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17.The Journal of biological chemistry · 2020Article
- pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Repeat domain-associated O-glycans govern PMEL fibrillar sheet architecture.Scientific reports · 2019Article
- Intramelanocytic Acidification Plays a Role in the Antimelanogenic and Antioxidative Properties of Vitamin C and Its Derivatives.Oxidative medicine and cellular longevity · 2019Article
- Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17.Journal of molecular biology · 2018Review
- Raman fingerprints of amyloid structures.Chemical communications (Cambridge, England) · 2018Article
- A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.The Journal of biological chemistry · 2017Article
- 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
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3 authors.
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Abstract
Fibrils derived from Pmel17 are functional amyloids upon which melanin is deposited. Fibrils of the repeat domain (RPT) of Pmel17 form under strict melanosomal pH (4.5-5.5) and completely dissolve at pH≥6. To determine which Glu residue is responsible for this reversibility, aggregation of single, double, and quadruple Ala and Gln mutants were examined by intrinsic Trp fluorescence, circular dichroism spectroscopy, and transmission electron microscopy. Charge neutralization of E404, E422, E425, or E430, which are located in the putative amyloid-forming region, modulated aggregation kinetics. Remarkably, the removal of a single negative charge at E422, one of 16 carboxylic acids, shifted the pH dependence by a full pH unit. Mutation at E404, E425, or E430 had little to no effect. We suggest that protonation at E422 is essential for initiating amyloid formation and that the other Glu residues play an allosteric role in fibril stability.
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