Conformational Conversion during Amyloid Formation at Atomic Resolution - sprookjes - yvandenbroek - TriplyDB

Conformational Conversion during Amyloid Formation at Atomic Resolution

Conformational Conversion during Amyloid Formation at Atomic Resolution

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Mechanisms of amyloid formation revealed by solution NMR Assessing the causes and consequences of co-polymerization in amyloid formation C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure Global structural motions from the strain of a single hydrogen bond Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis Dialysis-related amyloidosis: challenges and solutions Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.Systemic amyloidosis: lessons from β2-microglobulin.Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1 A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Energy landscapes of functional proteins are inherently risky.Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.Thermodynamics of protein destabilization in live cells Energetics and mechanism of the normal-to-amyloidogenic isomerization of β2-microglobulin: on-the-fly string method calculations Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid Transiently populated intermediate functions as a branching point of the FF domain folding pathway Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors Comparing the energy landscapes for native folding and aggregation of PrP.Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Fast real-time NMR methods for characterizing short-lived molecular states.Misfolding of amyloidogenic proteins and their interactions with membranes.Distinguishing closely related amyloid precursors using an RNA aptamer.Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.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.Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation Phosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture.How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity.A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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J.MOLCEL.2010.11.028

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Conformational Conversion during Amyloid Formation at Atomic Resolution

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Arnout P Kalverda

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Gary S Thompson

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Steve W Homans

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Timo Eichner

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Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.

Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties

beta2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation

Essential role of proline isomerization in stefin B tetramer formation

A regulatable switch mediates self-association in an immunoglobulin fold

Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation

Three-dimensional structure of beta 2-microglobulin

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

A primer of amyloid nomenclature

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2058810

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10.1016/J.MOLCEL.2010.11.028

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