ArticleThe Journal of biological chemistry2010
Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 57 citations in OpenAlex.
- A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022Article
- Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?International journal of biological macromolecules · 2022Article
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Article
- Anti-prion systems in yeast.The Journal of biological chemistry · 2019Review
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- The structure of a βNature communications · 2018Article
- Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017Review
- A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.Journal of the American Chemical Society · 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
- Review
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry.Molecular bioSystems · 2014Article
- Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Biochimica et biophysica acta · 2013Review
- Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors.The Journal of biological chemistry · 2013Article
- Direct three-dimensional visualization of membrane disruption by amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural features and domain organization of huntingtin fibrils.The Journal of biological chemistry · 2012Article
- Domain swapping and amyloid fibril conformation.Prion · 2012Article
- Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Computer modeling of nitroxide spin labels on proteins.Biopolymers · 2012Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
beta(2)-microglobulin (beta(2)m) is a 99-residue protein with an immunoglobulin fold that forms beta-sheet-rich amyloid fibrils in dialysis-related amyloidosis. Here the environment and accessibility of side chains within amyloid fibrils formed in vitro from beta(2)m with a long straight morphology are probed by site-directed spin labeling and accessibility to modification with N-ethyl maleimide using 19 site-specific cysteine variants. Continuous wave electron paramagnetic resonance spectroscopy of these fibrils reveals a core predominantly organized in a parallel, in-register arrangement, by contrast with other beta(2)m aggregates. A continuous array of parallel, in-register beta-strands involving most of the polypeptide sequence is inconsistent with the cryoelectron microscopy structure, which reveals an architecture based on subunit repeats. To reconcile these data, the number of spins in close proximity required to give rise to spin exchange was determined. Systematic studies of a model protein system indicated that juxtaposition of four spin labels is sufficient to generate exchange narrowing. Combined with information about side-chain mobility and accessibility, we propose that the amyloid fibrils of beta(2)m consist of about six beta(2)m monomers organized in stacks with a parallel, in-register array. The results suggest an organization more complex than the accordion-like beta-sandwich structure commonly proposed for amyloid fibrils.
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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.