ReviewBiochimica et biophysica acta2005
Towards an understanding of the structural molecular mechanism of beta(2)-microglobulin amyloid formation in vitro.
Review in Biochimica et biophysica acta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
The trial behind it
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Who cites it
22 citing papers in PubMed, 59 citations in OpenAlex.
- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins.ACS chemical neuroscience · 2024Article
- Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation.International journal of molecular sciences · 2018Review
- TiO2 Nanoparticles as Potential Promoting Agents of Fibrillation of α-Synuclein, a Parkinson's Disease-Related Protein.Iranian journal of biotechnology · 2017Article
- Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation.Journal of molecular biology · 2016Article
- Article
- Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis.Protein science : a publication of the Protein Society · 2013Article
- Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.Biophysical reviews · 2013Review
- A generic crystallization-like model that describes the kinetics of amyloid fibril formation.The Journal of biological chemistry · 2012Article
- Top-down study of β2-microglobulin deamidation.Analytical chemistry · 2012Article
- Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.The journal of physical chemistry. B · 2012Article
- Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Journal of the American Chemical Society · 2010Article
- Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Journal of the American Chemical Society · 2009Article
- Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape.FEBS letters · 2009Review
- Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.Journal of molecular biology · 2009Article
- Existence of different structural intermediates on the fibrillation pathway of human serum albumin.Biophysical journal · 2009Article
- Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.Journal of molecular biology · 2008Article
- Production and characterization of RNA aptamers specific for amyloid fibril epitopes.The Journal of biological chemistry · 2007Article
- Nucleation of protein fibrillation by nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Deriving a complete understanding of protein self-association into amyloid fibrils across multiple distance and time scales is an enormous challenge. At small length scales, a detailed description of the partially folded protein ensemble that participates in self-assembly remains obscure. At larger length scales, amyloid fibrils are often heterogeneous, can form along multiple pathways, and are further complicated by phenomena such as phase-separation. Over the last 5 years, we have used an array of biophysical approaches in order to elucidate the structural and molecular mechanism of amyloid fibril formation, focusing on the all beta-sheet protein, beta(2)-microglubulin (beta(2)m). This protein forms amyloid deposits in the human disease 'dialysis-related amyloidosis' (DRA). We have shown that under acidic conditions beta(2)m rapidly associates in vitro to form amyloid-like fibrils that have different morphological properties, but which contain an underpinning cross-beta structure. In this review, we discuss our current knowledge of the structure of these fibrils, as well as the structural, kinetic and thermodynamic relationship between fibrils with different morphologies. The results provide some of the first insights into the shape of the self-assembly free-energy landscape for this protein and highlight the parallel nature of the assembly process. We include a detailed description of the structure and dynamics of partially folded and acid unfolded species of beta(2)m using NMR, and highlight regions thought to be important in early self-association events. Finally, we discuss briefly how knowledge of assembly mechanisms in vitro can be used to inform the design of therapeutic strategies for this, and other amyloid disorders, and we speculate on how the increasing power of biophysical approaches may lead to a fuller description of protein self-assembly into amyloid in the future.
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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.