ArticleJournal of the American Chemical Society2014
Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Dental plaque biofilm transforms host-derived βBiofilm · 2025Article
- On-Pathway Oligomer of Human Islet Amyloid Polypeptide Induced and Stabilized by Mechanical Rotation during Magic Angle Spinning Nuclear Magnetic Resonance.The journal of physical chemistry letters · 2023Article
- The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of β-microglobulin.Acta biochimica et biophysica Sinica · 2022Article
- Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules.Journal of the American Chemical Society · 2020Article
- The role of the IThe Journal of biological chemistry · 2020Article
- Article
- The structure of a βNature communications · 2018Article
- Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T.International journal of molecular sciences · 2018Article
- Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Nature communications · 2018Article
- Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.Journal of biomolecular NMR · 2017Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- Aggregation and Fibril Structure of AβBiochemistry · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- Stepwise unfolding of human βEuropean biophysics journal : EBJ · 2017Article
- Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Journal of the American Chemical Society · 2016Article
- Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.Journal of the American Chemical Society · 2016Article
- Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.The Journal of biological chemistry · 2016Article
- Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation.Journal of molecular biology · 2016Article
- Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.Scientific reports · 2015Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Amyloid fibrils formed from initially soluble proteins with diverse sequences are associated with an array of human diseases. In the human disorder, dialysis-related amyloidosis (DRA), fibrils contain two major constituents, full-length human β2-microglobulin (hβ2m) and a truncation variant, ΔN6 which lacks the N-terminal six amino acids. These fibrils are assembled from initially natively folded proteins with an all antiparallel β-stranded structure. Here, backbone conformations of wild-type hβ2m and ΔN6 in their amyloid forms have been determined using a combination of dilute isotopic labeling strategies and multidimensional magic angle spinning (MAS) NMR techniques at high magnetic fields, providing valuable structural information at the atomic-level about the fibril architecture. The secondary structures of both fibril types, determined by the assignment of ~80% of the backbone resonances of these 100- and 94-residue proteins, respectively, reveal substantial backbone rearrangement compared with the location of β-strands in their native immunoglobulin folds. The identification of seven β-strands in hβ2m fibrils indicates that approximately 70 residues are in a β-strand conformation in the fibril core. By contrast, nine β-strands comprise the fibrils formed from ΔN6, indicating a more extensive core. The precise location and length of β-strands in the two fibril forms also differ. The results indicate fibrils of ΔN6 and hβ2m have an extensive core architecture involving the majority of residues in the polypeptide sequence. The common elements of the backbone structure of the two proteins likely facilitates their ability to copolymerize during amyloid fibril assembly.
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