K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.
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Potential role of atomic force microscopy in systems biologyFamilial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndromeAntimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesActivity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresStructural convergence among diverse, toxic beta-sheet ion channels.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Polymorphic C-terminal beta-sheet interactions determine the formation of fibril or amyloid beta-derived diffusible ligand-like globulomer for the Alzheimer Abeta42 dodecamer.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Antimicrobial properties of amyloid peptides.X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-MicroglobulinProbing ion channel activity of human islet amyloid polypeptide (amylin).The higher level of complexity of K-Ras4B activation at the membrane.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Mechanism of membrane permeation induced by synthetic β-hairpin peptides.Non-selective ion channel activity of polymorphic human islet amyloid polypeptide (amylin) double channels.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation
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K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on October 2009
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vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
K3 fragment of amyloidogenic beta
@nl
K3 fragment of amyloidogenic b ...... dialysis related amyloidosis.
@en
type
label
K3 fragment of amyloidogenic beta
@nl
K3 fragment of amyloidogenic b ...... dialysis related amyloidosis.
@en
prefLabel
K3 fragment of amyloidogenic beta
@nl
K3 fragment of amyloidogenic b ...... dialysis related amyloidosis.
@en
P2093
P2860
P50
P356
P1476
K3 fragment of amyloidogenic b ...... dialysis related amyloidosis.
@en
P2093
Hyunbum Jang
Mirela Mustata
Ratnesh Lal
P2860
P304
14938-14945
P356
10.1021/JA9049299
P407
P577
2009-10-01T00:00:00Z