Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.
about
β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHSimulation 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.Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry.Approach to characterization of the higher order structure of disulfide-containing proteins using hydrogen/deuterium exchange and top-down mass spectrometryProtein surface mapping using diethylpyrocarbonate with mass spectrometric detectionStructural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometryCu(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.Copper binding to beta-2-microglobulin and its pre-amyloid oligomers.beta(2)-microglobulin: from physiology to amyloidosis.Unique effect of Cu(II) in the metal-induced amyloid formation of β-2-microglobulinUnderstanding the complex mechanisms of β2-microglobulin amyloid assembly.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Metal binding sheds light on mechanisms of amyloid assembly.HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.Peculiarities of copper binding to alpha-synuclein.A native to amyloidogenic transition regulated by a backbone trigger.Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.
P2860
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P2860
Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.
description
2004 nî lūn-bûn
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
@zh-hk
2004年論文
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2004年論文
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2004年论文
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2004年论文
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name
Increase in the conformational ...... dialysis-related amyloidosis.
@en
type
label
Increase in the conformational ...... dialysis-related amyloidosis.
@en
prefLabel
Increase in the conformational ...... dialysis-related amyloidosis.
@en
P2093
P2860
P356
P1433
P1476
Increase in the conformational ...... dialysis-related amyloidosis.
@en
P2093
Hidenori Katou
Hironobu Naiki
James Villanueva
József Kardos
Kazuhiro Hasegawa
Masaru Hoshino
P2860
P304
P356
10.1110/PS.03445704
P577
2004-02-06T00:00:00Z