ArticleThe Journal of biological chemistry2008
A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 63 citations in OpenAlex.
- Effect of RNA on the supramolecular architecture of α-synuclein fibrils.Biophysical journal · 2025Article
- Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- Extracellular matrix components modulate different stages in βThe Journal of biological chemistry · 2019Article
- Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- The structure of a βNature communications · 2018Article
- Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.International journal of molecular sciences · 2017Article
- Stepwise unfolding of human βEuropean biophysics journal : EBJ · 2017Article
- pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes.The Journal of biological chemistry · 2014Article
- β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH.PloS one · 2014Article
- Article
- Structural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growth.The Journal of chemical physics · 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
- The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Rapid communications in mass spectrometry : RCM · 2012Article
- The interconversion between a flexible β-sheet and a fibril β-arrangement constitutes the main conformational event during misfolding of PSD95-PDZ3 domain.Biophysical journal · 2012Article
- Understanding the complex mechanisms of β2-microglobulin amyloid assembly.The FEBS journal · 2011Review
- Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases. Fibrillar aggregates with amyloid-like properties can also be generated in vitro from pure proteins and peptides, including those not known to be associated with amyloidosis. Whereas biophysical studies of amyloid-like fibrils formed in vitro have provided important insights into the molecular mechanisms of amyloid generation and the structural properties of the fibrils formed, amyloidogenic proteins are typically exposed to mild or more extreme denaturing conditions to induce rapid fibril formation in vitro. Whether the structure of the resulting assemblies is representative of their natural in vivo counterparts, thus, remains a fundamental unresolved issue. Here we show using Fourier transform infrared spectroscopy that amyloid-like fibrils formed in vitro from natively folded or unfolded beta(2)-microglobulin (the protein associated with dialysis-related amyloidosis) adopt an identical beta-sheet architecture. The same beta-strand signature is observed whether fibril formation in vitro occurs spontaneously or from seeded reactions. Comparison of these spectra with those of amyloid fibrils extracted from patients with dialysis-related amyloidosis revealed an identical amide I' absorbance maximum, suggestive of a characteristic and conserved amyloid fold. Our results endorse the relevance of biophysical studies for the investigation of the molecular mechanisms of beta(2)-microglobulin fibrillogenesis, knowledge about which may inform understanding of the pathobiology of this protein.
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