ArticleBiophysical journal2010
Copper uptake induces self-assembly of 18.5 kDa myelin basic protein (MBP).
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Decreased metallothionein-3 expression in the human spinal cord is a common feature of amyotrophic lateral sclerosis and multiple sclerosis.Scientific reports · 2026Article
- Mammalian copper homeostasis: physiological roles and molecular mechanisms.Physiological reviews · 2025Review
- Aqueous Ionic Liquid Mixtures as Minimal Models of Lipid Bilayer Membranes.ACS biomaterials science & engineering · 2024Article
- Bifidobacterium breve Probiotic Compared to Lactobacillus casei Causes a Better Reduction in Demyelination and Oxidative Stress in Cuprizone-Induced Demyelination Model of Rat.Molecular neurobiology · 2024Article
- Folding and self-assembly of short intrinsically disordered peptides and protein regions.Nanoscale advances · 2021Review
- Article
- Differential effects of zinc binding on structured and disordered regions in the multidomain STIL protein.Chemical science · 2016Article
- Conformational Stability and Pathogenic Misfolding of the Integral Membrane Protein PMP22.Journal of the American Chemical Society · 2015Article
- Solving the Measurement Problem and then Steppin' Out over the Line Riding the Rarest Italian: Crossing the Streams to Retrieve Stable Bioactivity in Majorana Bound States of Dialy zed Human Platelet Lysates.The open neurology journal · 2015Article
- Myelin architecture: zippering membranes tightly together.Cellular and molecular life sciences : CMLS · 2014Review
- Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms.Journal of neurochemistry · 2013Review
- Characterization of the solution structure of human serum albumin loaded with a metal porphyrin and fatty acids.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Myelin basic protein (MBP) is predominantly found in the membranes of the myelin sheath of the central nervous system and is involved in important protein-protein and protein-lipid interactions in vivo and in vitro. Furthermore, divalent transition metal ions, especially Zn(2+) and Cu(2+), seem to directly affect the MBP-mediated formation and stabilization of the myelin sheath of the central nervous system. MBP belongs to the realm of intrinsically disordered proteins, and only fragmentary information is available regarding its partial structure(s) or supramolecular arrangements. Here, using standard continuous wave and modern pulse electron paramagnetic resonance methods, as well as dynamic light scattering, we demonstrate the uptake and specific coordination of two Cu(2+) atoms or one Zn(2+) atom per MBP molecule in solution. In the presence of phosphates, further addition of divalent metal ions above a characteristic threshold of four Cu(2+) atoms or two Zn(2+) atoms per MBP molecule leads to the formation of large MBP aggregates within the protein solution. In vivo, MBP-MBP interactions may thus be mediated by divalent cations.
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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.