Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR.
about
A unified conformational selection and induced fit approach to protein-peptide dockingA novel "molecular tweezer" inhibitor of α-synuclein neurotoxicity in vitro and in vivo.Fibrils and nanotubes assembled from a modified amyloid-β peptide fragment differ in the packing of the same β-sheet building blocks.Recent advances in the genetics of Parkinson's disease.Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Solid-state NMR studies of amyloid fibril structureIntracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation.Modulating the Amyloidogenesis of α-Synucleinalpha-Synuclein: a therapeutic target for Parkinson's disease?Cell death pathways in Parkinson's disease: proximal triggers, distal effectors, and final steps.The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies.A deadly spread: cellular mechanisms of α-synuclein transfer.Observation of molecular inhibition and binding structures of amyloid peptides.Investigational α-synuclein aggregation inhibitors: hope for Parkinson's disease.Peptide N-Amination Supports β-Sheet Conformations.Amyloidogenic sequences in native protein structures.Chaperone-like N-methyl peptide inhibitors of polyglutamine aggregationBinding Interactions of Agents That Alter α-Synuclein Aggregation.Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein.Influence of EGCG on α-synuclein (αS) aggregation and identification of their possible binding mode: A computational study using molecular dynamics simulation.Toward peptide-based inhibitors as therapies for Parkinson's disease.Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.Inhibition of amyloid aggregation by formation of helical assemblies.Amyloid Beta Aggregation in the Presence of Temperature-Sensitive PolymersNeurodegenerative Diseases: Regenerative Mechanisms and Novel Therapeutic Approaches
P2860
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P2860
Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@en
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@nl
type
label
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@en
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@nl
prefLabel
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@en
Design of an N-methylated pept ...... ion guided by solid-state NMR.
@nl
P2860
P50
P356
P1476
Design of an N-methylated pept ...... tion guided by solid-state NMR
@en
P2093
David A Middleton
P2860
P304
P356
10.1021/JA075356Q
P407
P577
2008-05-30T00:00:00Z