about
A flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceTowards a Pharmacophore for AmyloidAnti-prion activity of an RNA aptamer and its structural basisProgrammable biofilm-based materials from engineered curli nanofibresBiochemical properties of highly neuroinvasive prion strainsMAS NMR of HIV-1 protein assemblies.Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide4D solid-state NMR for protein structure determination.The structural basis for optimal performance of oligothiophene-based fluorescent amyloid ligands: conformational flexibility is essential for spectral assignment of a diversity of protein aggregates.Distinct Spacing Between Anionic Groups: An Essential Chemical Determinant for Achieving Thiophene-Based Ligands to Distinguish β-Amyloid or Tau Polymorphic AggregatesStructure-based drug design identifies polythiophenes as antiprion compounds.Looked at life from both sides nowNanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy.Pentameric thiophene-based ligands that spectrally discriminate amyloid-β and tau aggregates display distinct solvatochromism and viscosity-induced spectral shifts.Congo Red Interactions with Curli-Producing E. coli and Native Curli Amyloid Fibers.Disordered binding of small molecules to Aβ(12-28).Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.High-resolution analytical imaging and electron holography of magnetite particles in amyloid cores of Alzheimer's disease.Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?The HET-S/s Prion Motif in the Control of Programmed Cell Death.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Characterization of fibril dynamics on three timescales by solid-state NMR.Investigation of the structural preference and flexibility of the loop residues in amyloid fibrils of the HET-s prion.Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant Aβ Amyloid Fibrils and Alzheimer's Disease Brain-Derived Aβ.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Multimodal fluorescence microscopy of prion strain specific PrP deposits stained by thiophene-based amyloid ligands.Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils.Hierarchical organization from self-assembling disulfide macrocycles.The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218-289): a solid-state NMR study.Temperature dependence of Congo red binding to amyloid β12-28.Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging.1H-Detected REDOR with Fast Magic-Angle Spinning of a Deuterated Protein.Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.Binding of ACE-inhibitors to in vitro and patient-derived amyloid-β fibril models.Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory.X-Ray Structural Study of Amyloid-Like Fibrils of Tau Peptides Bound to Small-Molecule Ligands.Nucleation of Amyloid Oligomers by RepA-WH1-Prionoid-Functionalized Gold Nanorods.
P2860
Q26997922-DAA23EE3-6350-49B1-B2C7-20ED3EDF1A24Q27670496-84888B23-C47D-47AB-9776-E059E3CAB63AQ27675235-0FF099F0-2DBD-40F7-875F-4B280EE5FF82Q28248161-931F533F-E02B-4745-9893-7F4DBA3BC8C8Q28480480-70552320-4CD7-4FAA-B9DB-D336AF7D4AB4Q30372916-21512C67-3C19-4B33-85D5-AA0AE67C75F5Q30379691-E27C5AD0-D18F-45EF-85B8-A4EAFC8D8E95Q30414061-24467FFD-97BF-488E-821E-5E4B31FB86C4Q34351807-DF0EE39A-2F3C-4715-A40E-4E7EF3076EFBQ34477979-F8467A78-228E-49AF-96EF-60D181E683F6Q34488418-B28141F5-1F6A-437E-AECA-2886B5B08063Q34829539-E26D037C-19A6-41FC-BE0B-CA0BF3065FC1Q35212582-EC706F6F-2236-4809-AB0B-FFB84145B178Q35222856-46A83F54-3562-4E9D-AEBC-30EDDB97BA4EQ35814646-09A54399-70CE-40CD-8381-4AC593E96015Q35842197-2A911997-C7B1-4B21-BA72-6A80B664C499Q35853749-D5B63775-5ECB-4378-8B51-B6569008600DQ36331907-FBF0F835-A4E0-49EF-85F1-9C3C42A7F2E9Q36845628-1E6D3657-577C-41B0-9FB8-8F0F809844C3Q37019530-0803081C-BE26-4555-8BAC-D87365AC15CFQ38261844-59CAB5C7-CB6C-47D7-87D4-D835739E5E48Q38879717-DDFC4D87-D09F-42E3-A1ED-F162E5FB4D9EQ39017883-DE20AC1E-92D3-4390-98C2-C832DBE15ECAQ39595107-B99898F9-FF6E-4533-8DE9-33ED2BF26F81Q40068029-C4D4A2BC-6111-44DF-BDCA-C40FCB88CD1FQ40815219-DC6A19D1-C6AA-46A8-9146-2606705A7447Q41702344-BD1018DE-CE65-4719-97B2-70FB00483E19Q41921037-5CD65A74-8313-49CF-B4B4-6B828C36907EQ42117131-1E98774D-00EA-4BC8-9757-3AE9E710734CQ44212461-55442D04-EEDC-44CC-AEA4-7E0E57976E93Q46297972-A3E11982-3222-462B-A35D-CF21FAFC61A8Q46510099-B59CDFF2-B5D0-4070-A271-D558043CF7C2Q46920907-4BF32846-28CD-44FA-90FD-3FC4B21583EEQ47384795-CA25ACED-EEB6-4F25-AA9F-9349D6168F42Q47941728-06247991-D16C-498D-9717-3AD6BDEB60ABQ48315178-287133CB-8A2A-48A0-8D2B-2BB18B2CCC47Q49021624-08683B09-BD1D-45C0-8666-BCE4B483CE8AQ50909577-A903FE6D-E45E-4D3E-BC96-29C7DFB8BB29Q51263493-CF726E3D-BB7F-4CA6-8B0B-13477DE6BA86Q51595806-5993AABE-3A89-44A7-BDD7-3232A0704CC6
P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The amyloid-Congo red interface at atomic resolution
@ast
The amyloid-Congo red interface at atomic resolution
@en
The amyloid-Congo red interface at atomic resolution
@nl
type
label
The amyloid-Congo red interface at atomic resolution
@ast
The amyloid-Congo red interface at atomic resolution
@en
The amyloid-Congo red interface at atomic resolution
@nl
prefLabel
The amyloid-Congo red interface at atomic resolution
@ast
The amyloid-Congo red interface at atomic resolution
@en
The amyloid-Congo red interface at atomic resolution
@nl
P2093
P2860
P50
P3181
P356
P1476
The amyloid-Congo red interface at atomic resolution
@en
P2093
Anja Böckmann
Anne K Schütz
Matthias Ernst
P2860
P304
P3181
P356
10.1002/ANIE.201008276
P407
P577
2011-06-20T00:00:00Z