about
Probing protein aggregation using discrete molecular dynamicsAGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.Nuclear medicine studies in the dialysis patient.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.Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architectureEndocytosed 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.Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.A case of femoral compressive neuropathy in AL amyloidosis.Clinical Utility of Urinary β2-Microglobulin in Detection of Early Nephropathy in African Diabetes Mellitus Patients.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Systemic amyloidoses.Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry.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.HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.The GOR Method of Protein Secondary Structure Prediction and Its Application as a Protein Aggregation Prediction Tool.Sequence and expression analysis of the beta-2-microglobulin gene in dialysis patients.The Rise of Expanded Hemodialysis.Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
beta2-microglobulin-derived amyloidosis: an update.
@ast
beta2-microglobulin-derived amyloidosis: an update.
@en
beta2-microglobulin-derived amyloidosis: an update.
@nl
type
label
beta2-microglobulin-derived amyloidosis: an update.
@ast
beta2-microglobulin-derived amyloidosis: an update.
@en
beta2-microglobulin-derived amyloidosis: an update.
@nl
prefLabel
beta2-microglobulin-derived amyloidosis: an update.
@ast
beta2-microglobulin-derived amyloidosis: an update.
@en
beta2-microglobulin-derived amyloidosis: an update.
@nl
P1476
beta2-microglobulin-derived amyloidosis: an update.
@en
P2093
P304
P356
10.1046/J.1523-1755.2001.59780164.X
P577
2001-02-01T00:00:00Z