Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
about
Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsDeciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopyStepwise dynamics of epitaxially growing single amyloid fibrils.Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46KBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spineα-synuclein reactive antibodies as diagnostic biomarkers in blood sera of Parkinson's disease patients.Mysterious oligomerization of the amyloidogenic proteinsDirect observation of the interconversion of normal and toxic forms of α-synucleinThe role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease.Lewy bodies under atomic force microscope.Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril massDOPAL is transmissible to and oligomerizes alpha-synuclein in human glial cells.Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domainIntrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanoporesNanotools for megaproblems: probing protein misfolding diseases using nanomedicine modus operandiSingle-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanismsEffects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging.Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Protein aggregation processes: In search of the mechanism.Nanoimaging in protein-misfolding and -conformational diseases.AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.Nanoimaging for prion related diseases.Electrocatalysis in proteins, nucleic acids and carbohydrates.α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.Protein fibrillation and nanoparticle interactions: opportunities and challenges.Toward the discovery of effective polycyclic inhibitors of alpha-synuclein amyloid assembly.Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutantsImaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy.Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory.The position of hydrophobic residues tunes peptide self-assembly.Local Mechanical Perturbation Provides an Effective Means to Regulate the Growth and Assembly of Functional Peptide Fibrils.Changes in interfacial properties of alpha-synuclein preceding its aggregation.Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.
P2860
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P2860
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@en
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@nl
type
label
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@en
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@nl
prefLabel
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@en
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@nl
P2093
P1476
Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.
@en
P2093
Dmitry Cherny
Thomas M Jovin
Vinod Subramaniam
P304
P356
10.1016/J.JMB.2004.04.051
P407
P577
2004-06-01T00:00:00Z