ArticleProtein science : a publication of the Protein Society2002
Topological investigation of amyloid fibrils obtained from beta2-microglobulin.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 53 citations in OpenAlex.
- Predicting stable binding modes from simulated dimers of the D76N mutant ofComputational and structural biotechnology journal · 2021Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes.The Journal of biological chemistry · 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
- Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Biophysical journal · 2011Article
- Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Journal of the American Chemical Society · 2010Article
- Mass spectrometry and the amyloid problem--how far can we go in the gas phase?Journal of the American Society for Mass Spectrometry · 2010Article
- Structure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations.Biophysical journal · 2007Article
- Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry.Journal of molecular biology · 2006Article
- Investigating the structural properties of amyloid-like fibrils formed in vitro from beta2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry.Rapid communications in mass spectrometry : RCM · 2006Article
- Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Protein science : a publication of the Protein Society · 2006Article
- Towards an understanding of the structural molecular mechanism of beta(2)-microglobulin amyloid formation in vitro.Biochimica et biophysica acta · 2005Review
- Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.Protein science : a publication of the Protein Society · 2005Article
- Ribosomal protein L7a binds RNA through two distinct RNA-binding domains.The Biochemical journal · 2005Article
- LC-mass spectrometry analysis of N- and C-terminal boundary sequences of polypeptide fragments by limited proteolysis.Journal of the American Society for Mass Spectrometry · 2005Article
- Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Beta edge strands in protein structure prediction and aggregation.Protein science : a publication of the Protein Society · 2003Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils of patients treated with regular hemodialysis essentially consists of beta2-microglobulin (beta2-m) and its truncated species DeltaN6beta2-m lacking six residues at the amino terminus. The truncated fragment has a more flexible three-dimensional structure and constitutes an excellent candidate for the analysis of a protein in the amyloidogenic conformation. The surface topology of synthetic fibrils obtained from intact beta2-m and truncated DeltaN6beta2-m was investigated by the limited proteolysis/mass spectrometry approach that appeared particularly suited to gain insights into the structure of beta2-m within the fibrillar polymer. The distribution of prefential proteolytic sites observed in both fibrils revealed that the central region of the protein, which had been easily cleaved in the full-length globular beta2-m, was fully protected in the fibrillar form. In addition, the amino- and carboxy-terminal regions of beta2-m became exposed to the solvent in the fibrils, whereas they were masked completely in the native protein. These data indicate that beta2-m molecules in the fibrils consist of an unaccessible core comprising residues 20-87 with the strands I and VIII being not constrained in the fibrillar polymer and exposed to the proteases. Moreover, proteolytic cleavages observed in vitro at Lys 6 and Lys 19 reproduce specific cleavages that have to occur in vivo to generate the truncated forms of beta2-m occurring in natural fibrils. On the basis of these data, a possible mechanism for fibril formation from native beta2-m is discussed and an explanation for the occurrence of truncated protein species in natural fibrils is given.
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