Observation of spatial propagation of amyloid assembly from single nuclei
about
The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityPhase transitions and size scaling of membrane-less organellesMicro total analysis systems: fundamental advances and applications in the laboratory, clinic, and field.Nanoscale spatially resolved infrared spectra from single microdroplets.Connecting macroscopic observables and microscopic assembly events in amyloid formation using coarse grained simulationsKinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.Single-particle characterization of Aβ oligomers in solution.SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.Resolution of oligomeric species during the aggregation of Aβ1-40 using (19)F NMR.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Microfluidics: reframing biological enquiry.The Amyloid Phenomenon and Its Links with Human Disease.Competition between primary nucleation and autocatalysis in amyloid fibril self-assembly.Pseudo-one-dimensional nucleation in dilute polymer solutionsElucidating the locking mechanism of peptides onto growing amyloid fibrils through transition path sampling.Unlocking the atomic-level details of amyloid fibril growth through advanced biomolecular simulations.Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp70 chaperone.An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation.Absolute Quantification of Amyloid Propagons by Digital Microfluidics.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Theory of amyloid fibril nucleation from folded proteins.Microfluidic devices fabricated using fast wafer-scale LED-lithography patterning.In vivo cortical spreading pattern of tau and amyloid in the Alzheimer disease spectrum.Fluctuations in the Kinetics of Linear Protein Self-Assembly.Stochastic lag time in nucleated linear self-assembly.Insights into the variability of nucleated amyloid polymerization by a minimalistic model of stochastic protein assembly.Asymptotic solutions of the Oosawa model for the length distribution of biofilaments.Oil Palm Phenolics Inhibit the In Vitro Aggregation of β-Amyloid Peptide into Oligomeric Complexes.Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space.Scaling and dimensionality in the chemical kinetics of protein filament formationExtrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in SolutionSpatial Propagation of Protein PolymerizationInherent Variability in the Kinetics of Autocatalytic Protein Self-AssemblyShear-Induced Amyloid Formation in the Brain: III. The Roles of Shear Energy and Seeding in a Proposed Shear Model
P2860
Q24298721-660B184C-98FF-437F-AA44-025FAC2474A0Q26852037-F31081B0-9BE0-4B88-B978-A6EC4E4E481FQ30444364-A81D934F-9033-4E4C-AA5F-97C4942EDBA4Q34403699-83FBAE6E-C4A5-415F-8084-8FC35CF10E43Q34446601-078E7CF1-55AC-4546-9F4D-3E8F0B47447AQ34499321-02311347-303E-4DEC-AFC3-19AD41ACF430Q36163564-8CE2663E-8DDC-4E0E-809C-1193DE725FD6Q36234963-FC2975A4-DBD7-41FB-B326-8282B9AAE621Q36499643-F2D99E7C-F24E-4303-92A8-4D5281AB4E90Q36772928-8420B0C1-4A18-4301-B1F9-E7A1263A3246Q38240692-B328D698-800B-4B64-B418-5E47C67411E1Q38571113-A6D0AE1D-8882-4117-BD01-951B69EBE391Q39071444-8E57F1CE-3B32-41E7-9B31-93819DD65956Q41480687-E4657170-D516-4104-9D18-2686DEE9A2AFQ41502023-C121FE20-7115-42DA-B943-B33BD08522BFQ42020233-6CBEF464-BF45-4838-BD20-6D33909EDE07Q42037579-BEAA7665-BB8C-46B8-A91A-5DBDDE4CD388Q42233230-1AFD60A4-3F59-4B72-A8BF-6C63298C255DQ47141146-FA6BAAD7-5995-4A5D-B6DD-1286DDF8E3B0Q47152913-4116FB49-847B-4780-8FDE-7833CCCA8164Q47722422-C193F4EA-7030-4320-ACDA-6831D80CDCBCQ47764012-B92DCD59-9887-445D-A5C6-8E7C4CA7E8A4Q48133172-A53256F8-1B12-4E6C-A447-6FB70D4AA52CQ48665805-0BA92271-7F92-4E2E-8896-CCFCA76B6CD7Q50614621-6E04C5B2-CF57-4DAF-B4AA-83E909E78BB1Q50622723-B88FE8EF-38ED-4945-BBC3-3671ACD60E6EQ50650754-64CF4CB5-1104-4E74-A4D4-01F7345C75EBQ51083983-3743F0A5-9B51-4974-86C0-F988BAF2781BQ53073171-A0B7F424-0458-41C8-8D83-09A6671EDA40Q53355595-97818CAB-8A15-4DA9-9B87-549B642E5FE5Q57369244-EB5A04AD-753A-4B06-A1C0-DF0D871B9946Q57986194-F475C772-3D3C-4527-B419-0194E99A35AFQ57986454-E6C002D1-8007-4AC0-BEAF-7E17C4151FAEQ58028801-E618ABB8-1203-4F2E-97D3-9AAB3147036EQ58797396-0DBB25AA-A61F-4294-8FD4-5D152D598849
P2860
Observation of spatial propagation of amyloid assembly from single nuclei
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
name
Observation of spatial propagation of amyloid assembly from single nuclei
@ast
Observation of spatial propagation of amyloid assembly from single nuclei
@en
type
label
Observation of spatial propagation of amyloid assembly from single nuclei
@ast
Observation of spatial propagation of amyloid assembly from single nuclei
@en
prefLabel
Observation of spatial propagation of amyloid assembly from single nuclei
@ast
Observation of spatial propagation of amyloid assembly from single nuclei
@en
P2093
P2860
P356
P1476
Observation of spatial propagation of amyloid assembly from single nuclei
@en
P2093
Adam R Abate
David A Weitz
Duncan A White
Erwin J De Genst
Jeremy J Agresti
Samuel I A Cohen
Tuomas P J Knowles
P2860
P304
14746-14751
P356
10.1073/PNAS.1105555108
P407
P577
2011-08-26T00:00:00Z