Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
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Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue TargetingMechanisms of amyloid formation revealed by solution NMRβ2-Microglobulin-mediated signaling as a target for cancer therapyOut-of-register -sheets suggest a pathway to toxic amyloid aggregatesThe structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulinsβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHInsights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometryRediscovering Beta-2 Microglobulin As a Biomarker across the Spectrum of Kidney Diseases.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.The orthologue of Sjögren's syndrome nuclear autoantigen 1 (SSNA1) in Trypanosoma brucei is an immunogenic self-assembling molecule.A mechanistic model for amorphous protein aggregation of immunoglobulin-like domains.Calcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.Energy landscapes of functional proteins are inherently risky.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.Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2-microglobulin.Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly.Structural, morphological, and functional diversity of amyloid oligomers.Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.A systematic molecular dynamics approach to the structural characterization of amyloid aggregation propensity of β2-microglobulin mutant D76N.Capillary electrophoresis analysis of different variants of the amyloidogenic protein β2 -microglobulin as a simple tool for misfolding and stability studies.An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins.Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril FormationUnderstanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies.Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation.Impact of advanced dialysis technology on the prevalence of dialysis-related amyloidosis in long-term maintenance dialysis patients.Accumulation of advanced glycation end products and beta 2-microglobulin in fibrotic thickening of the peritoneum in long-term peritoneal dialysis patients.ATP5b and β2-microglobulin are predictive markers for the prognosis of patients with gallbladder cancer.C-terminal unfolding of an amyloidogenicβ2-microglobulin fragment:ΔN6β2-microglobulin
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P2860
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 June 2011
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en-gb
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@nl
type
label
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en-gb
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@nl
prefLabel
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en-gb
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@nl
P2860
P921
P1433
P1476
Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
@en
P2093
Timo Eichner
P2860
P304
P356
10.1111/J.1742-4658.2011.08186.X
P407
P577
2011-06-13T00:00:00Z
2011-10-01T00:00:00Z