Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin.
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Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease.Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils.Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanolProper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains.Destruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometryHuman cyclophilin 40 unravels neurotoxic amyloids.EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.Amyloid structure: conformational diversity and consequences.3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR.Endocytosed 2-Microglobulin Amyloid Fibrils Induce Necrosis and Apoptosis of Rabbit Synovial Fibroblasts by Disrupting Endosomal/Lysosomal Membranes: A Novel Mechanism on the Cytotoxicity of Amyloid Fibrils.Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation.The beta-strand-loop-beta-strand conformation is marginally populated in beta2-microglobulin (20-41) peptide in solution as revealed by replica exchange molecular dynamics simulations.An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilMultifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro.The extracellular chaperone haptoglobin prevents serum fatty acid-promoted amyloid fibril formation of β2-microglobulin, resistance to lysosomal degradation, and cytotoxicityAbeta aggregation and possible implications in Alzheimer's disease pathogenesisC9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins.Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscapeSecondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy.High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag time.Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin.A residue-specific shift in stability and amyloidogenicity of antibody variable domains.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril FormationNMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.The amyloid fibrils of the constant domain of immunoglobulin light chain.Improved selectivity for Pb(II) by sulfur, selenium and tellurium analogues of 1,8-anthraquinone-18-crown-5: synthesis, spectroscopy, X-ray crystallography and computational studies.Expression in E. coli and purification of the fibrillogenic fusion proteins TTR-sfGFP and β2M-sfGFP.Heparin-induced amyloid fibrillation of β2 -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram.Flow-induced alignment of amyloid protofilaments revealed by linear dichroism.Mouse model to study human A β2M amyloidosis: generation of a transgenic mouse with excessive expression of human β2-microglobulinFunctional Amyloids in Bacteria
P2860
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P2860
Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@en
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@nl
type
label
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@en
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@nl
prefLabel
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@en
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@nl
P2093
P2860
P356
P1476
Amyloid fibril formation in th ...... mation of beta2-microglobulin.
@en
P2093
Hironobu Naiki
Kazuhiro Hasegawa
Takashi Higurashi
Takeshi Chiba
P2860
P304
47016-47024
P356
10.1074/JBC.M304473200
P407
P577
2003-09-04T00:00:00Z