The structure of Abeta42 C-terminal fragments probed by a combined experimental and theoretical study.
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Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionAtomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithmsRobotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mappingHuman islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.On the origins of the weak folding cooperativity of a designed ββα ultrafast protein FSD-1.Elucidating the tertiary structure of protein ions in vacuo with site specific photoinitiated radical reactions.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragmentsPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Amyloid-β peptide structure in aqueous solution varies with fragment size.A retrospective analysis of the Alzheimer's disease vaccine progress - The critical need for new development strategies.Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Aβ(39-42) modulates Aβ oligomerization but not fibril formationBinding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studiesMechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachAmyloid beta protein: Abeta40 inhibits Abeta42 oligomerization.Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretaseThe use of mass spectrometry to study amyloid-β peptides.Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Energetic contributions of residues to the formation of early amyloid-β oligomers.Comparison of force fields for Alzheimer's A β42: A case study for intrinsically disordered proteins.Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.Capping of aβ42 oligomers by small molecule inhibitors.A two-step strategy for structure-activity relationship studies of N-methylated aβ42 C-terminal fragments as aβ42 toxicity inhibitorsCharacterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Probing oligomerization of amyloid beta peptide in silico.Binding of fullerenes to amyloid beta fibrils: size matters.Out-of-Register Aβ42 Assemblies as Models for Neurotoxic Oligomers and Fibrils.The mass-mobility correlation redux: the conformational landscape of anhydrous biomolecules.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.Nanogels of dual inhibitor-modified hyaluronic acid function as a potent inhibitor of amyloid β-protein aggregation and cytotoxicity.
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P2860
The structure of Abeta42 C-terminal fragments probed by a combined experimental and theoretical study.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 23 January 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The structure of Abeta42 C-ter ...... imental and theoretical study.
@en
The structure of Abeta42 C-ter ...... imental and theoretical study.
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type
label
The structure of Abeta42 C-ter ...... imental and theoretical study.
@en
The structure of Abeta42 C-ter ...... imental and theoretical study.
@nl
prefLabel
The structure of Abeta42 C-ter ...... imental and theoretical study.
@en
The structure of Abeta42 C-ter ...... imental and theoretical study.
@nl
P2093
P2860
P1476
The structure of Abeta42 C-ter ...... imental and theoretical study.
@en
P2093
Joan-Emma Shea
Margaret M Condron
Megan M Murray
Michael T Bowers
Summer L Bernstein
P2860
P304
P356
10.1016/J.JMB.2009.01.029
P407
P577
2009-01-23T00:00:00Z