ArticleJournal of the American Chemical Society2010
Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
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- Tau Interacts with the C-Terminal Region of α-Synuclein, Promoting Formation of Toxic Aggregates with Distinct Molecular Conformations.Biochemistry · 2019Article
- Extracellular matrix components modulate different stages in βThe Journal of biological chemistry · 2019Article
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- Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Nature communications · 2018Article
- Aggregation and Fibril Structure of AβBiochemistry · 2017Article
- Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.Biochemistry · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Biochemistry · 2016Article
- Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.Biochemistry · 2016Article
- High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Journal of the American Chemical Society · 2015Article
- pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.PloS one · 2015Article
- Physical and structural basis for polymorphism in amyloid fibrils.Protein science : a publication of the Protein Society · 2014Review
- Distinguishing closely related amyloid precursors using an RNA aptamer.The Journal of biological chemistry · 2014Article
- Solid-state NMR studies of metal-free SOD1 fibrillar structures.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
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5 authors.
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Abstract
Beta(2)-microglobulin (beta(2)m) is the major structural component of amyloid fibrils deposited in a condition known as dialysis-related amyloidosis. Despite numerous studies that have elucidated important aspects of the fibril formation process in vitro, and a magic angle spinning (MAS) NMR study of the fibrils formed by a small peptide fragment, structural details of beta(2)m fibrils formed by the full-length 99-residue protein are largely unknown. Here, we present a site-specific MAS NMR analysis of fibrils formed by the full-length beta(2)m protein and compare spectra of fibrils prepared under two different conditions. Specifically, long straight (LS) fibrils are formed at pH 2.5, while a very different morphology denoted as worm-like (WL) fibrils is observed in preparations at pH 3.6. High-resolution MAS NMR spectra have allowed us to obtain (13)C and (15)N resonance assignments for 64 residues of beta(2)m in LS fibrils, including part of the highly mobile N-terminus. Approximately 25 residues did not yield observable signals. Chemical shift analysis of the sequentially assigned residues indicates that these fibrils contain an extensive beta-sheet core organized in a non-native manner, with a trans-P32 conformation. In contrast, WL fibrils exhibit more extensive dynamics and appear to have a smaller beta-sheet core than LS fibrils, although both cores seem to share some common elements. Our results suggest that the distinct macroscopic morphological features observed for the two types of fibrils result from variations in structure and dynamics at the molecular level.
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