The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition - Wikidata - awgldk - TriplyDB

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

http://www.wikidata.org/entity/Q27637822

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D-strand perturbation and amyloid propensity in beta-2 microglobulin Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties A regulatable switch mediates self-association in an immunoglobulin fold Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis Distance-Based Configurational Entropy of Proteins from Molecular Dynamics Simulations Diethylpyrocarbonate labeling for the structural analysis of proteins: label scrambling in solution and how to avoid it.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Molecular basis for the Cu2+ binding-induced destabilization of beta2-microglobulin revealed by molecular dynamics simulation.Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry A specific nanobody prevents amyloidogenesis of D76N β2-microglobulin in vitro and modifies its tissue distribution in vivo.Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry.Mysterious oligomerization of the amyloidogenic proteins Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis.Structural defects and the diagnosis of amyloidogenic propensity Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry 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.A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation.The Implication and Significance of Beta 2 Microglobulin: A Conservative Multifunctional Regulator.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.Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Abeta aggregation and possible implications in Alzheimer's disease pathogenesis Copper binding to beta-2-microglobulin and its pre-amyloid oligomers.beta(2)-microglobulin: from physiology to amyloidosis.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.The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.Structural, morphological, and functional diversity of amyloid oligomers.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Intermolecular alignment in β2-microglobulin amyloid fibrils.β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species.Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation Metal binding sheds light on mechanisms of amyloid assembly.Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.

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The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

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2002 nî lūn-bûn

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The solution structure of huma ...... omes of its amyloid transition

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Protein Science

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The solution structure of huma ...... omes of its amyloid transition

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Alessia Andreola

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Fabio Pettirossi

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Gennaro Esposito

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Giuliana Verdone

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Monica Stoppini

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Palma Mangione

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Paolo Viglino

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Sofia Giorgetti

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Vittorio Bellotti

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P2860

Structure of the human class I histocompatibility antigen, HLA-A2

beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis

The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures

Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution

Three-dimensional structure of beta 2-microglobulin

Analysis of the solution structure of the homeodomain of rat thyroid transcription factor 1 by 1H-NMR spectroscopy and restrained molecular mechanics

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

Torsion angle dynamics for NMR structure calculation with the new program DYANA

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

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10.1110/PS.29002

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3

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2002-03-01T00:00:00Z

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11514571

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11847272

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