Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments
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On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesMembrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid BilayersMechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Misfolding of amyloidogenic proteins and their interactions with membranes.Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.Modeling the Aggregation Propensity and Toxicity of Amyloid-β Variants.Formation of lamellar micelle-like oligomers and membrane disruption revealed by the study of short peptide hIAPP18-27.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Effect of lipid shape on toroidal pore formation and peptide orientation in lipid bilayers.Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.Structural analysis of oligomeric and protofibrillar Aβ amyloid pair structures considering F20L mutation effects using molecular dynamics simulations.End Capping Alters the Structural Characteristics and Mechanical Properties of Transthyretin (105-115) Amyloid Protofibrils.Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide.Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.The mechanical response of hIAPP nanowires based on different bending direction simulations.A time-resolved study on the interaction of oppositely charged bicelles--implications on the charged lipid exchange kinetics.Effects of End-Terminal Capping on Transthyretin (105–115) Amyloid Protofibrils Using Steered Molecular Dynamics
P2860
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P2860
Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments
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2013 nî lūn-bûn
@nan
2013年の論文
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2013年論文
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2013年論文
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2013年論文
@zh-hk
2013年論文
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2013年論文
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2013年论文
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2013年论文
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2013年论文
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name
Membrane disordering is not su ...... udies of IAPP(20-29) fragments
@en
type
label
Membrane disordering is not su ...... udies of IAPP(20-29) fragments
@en
prefLabel
Membrane disordering is not su ...... udies of IAPP(20-29) fragments
@en
P2093
P2860
P356
P1476
Membrane disordering is not su ...... udies of IAPP(20-29) fragments
@en
P2093
Deborah L Heyl
Jeffrey R Brender
Joshua M Osborne
Ranadheer R Pesaru
Samuel A Kotler
Shyamprasad Samisetti
P2860
P304
P356
10.1039/C3CP44696D
P407
P577
2013-03-15T00:00:00Z