ArticleJournal of molecular biology2009
Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 76 citations in OpenAlex.
- Deciphering Amyloid Fibril Formation through Protein Concentration by Optical Trapping.JACS Au · 2025Article
- The Catalyzing Effect of Aggregates on the Fibrillation Pathway of Human Insulin: A Spectroscopic Investigation During the Lag Phase.International journal of molecular sciences · 2025Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Article
- The Early Phase of β2m Aggregation: An Integrative Computational Study Framed on the D76N Mutant and the ΔN6 Variant.Biomolecules · 2019Article
- Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.Nature communications · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- The structure of a βNature communications · 2018Article
- Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.The Journal of biological chemistry · 2016Article
- MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images.Scientific reports · 2016Article
- A covalent homodimer probing early oligomers along amyloid aggregation.Scientific reports · 2015Article
- Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Energy landscapes of functional proteins are inherently risky.Nature chemical biology · 2014Article
- 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
- β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH.PloS one · 2014Article
- Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Journal of the American Chemical Society · 2013Article
- An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior.Biophysical journal · 2013Article
- Aggregation modulators interfere with membrane interactions of β2-microglobulin fibrils.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is known about the assembly contacts that define the fibril architecture. Here we present a set of three-dimensional structures of amyloid fibrils formed from full-length beta(2)-microglobulin, a 99-residue protein involved in clinical amyloidosis. Our cryo-electron microscopy maps reveal a hierarchical fibril structure built from tetrameric units of globular density, with at least three different subunit interfaces in this homopolymeric assembly. These findings suggest a more complex superstructure for amyloid than hitherto suspected and prompt a re-evaluation of the defining features of the amyloid fold.
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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.