Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor
about
Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assemblyA structural and dynamic investigation of the inhibition of catalase by nitric oxideInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesSecondary Structure of Rat and Human Amylin across Force FieldsMid-infrared spectroscopy for protein analysis: potential and challenges.Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Computing infrared spectra of proteins using the exciton modelWatching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.High-throughput thermal stability analysis of a monoclonal antibody by attenuated total reflection FT-IR spectroscopic imaging.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin.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.2D IR spectroscopy of histidine: probing side-chain structure and dynamics via backbone amide vibrations.Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitorsRole of sequence and structural polymorphism on the mechanical properties of amyloid fibrilsMyeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I.The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systemsHeterodivalent linked macrocyclic β-sheets with enhanced activity against Aβ aggregation: two sites are better than one.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Thermally induced protein unfolding probed by isotope-edited IR spectroscopy.Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.α-helix to β-hairpin transition of human amylin monomer.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Effect of proline mutations on the monomer conformations of amylin.Cyclic N-terminal loop of amylin forms non amyloid fibers.Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamageExperimental implementations of 2D IR spectroscopy through a horizontal pulse shaper design and a focal plane array detector.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption.Simplified and economical 2D IR spectrometer design using a dual acousto-optic modulator.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.Graphene oxide inhibits hIAPP amyloid fibrillation and toxicity in insulin-producing NIT-1 cells.Ultrafast Spectroscopy with Photocurrent Detection: Watching Excitonic Optoelectronic Systems at Work.Neuroprotective peptide-macrocycle conjugates reveal complex structure-activity relationships in their interactions with amyloid β.The molecular rotational motion of liquid ethanol studied by ultrafast time resolved infrared spectroscopy.Inhibition of human amylin fibril formation by insulin-mimetic vanadium complexes.Nanoscale Structure and Spectroscopic Probing of Aβ1-40 Fibril Bundle FormationImplications of peptide assemblies in amyloid diseases.Line shape analysis of two-dimensional infrared spectra
P2860
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P2860
Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@en
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@nl
type
label
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@en
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@nl
prefLabel
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@en
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@nl
P2093
P2860
P356
P1433
P1476
Two-dimensional infrared spect ...... of an amyloid fibril inhibitor
@en
P2093
Ann Marie Woys
Chi-cheng Chiu
Juan J de Pablo
Martin T Zanni
Peter Marek
Sadanand Singh
P2860
P2888
P304
P356
10.1038/NCHEM.1293
P577
2012-03-11T00:00:00Z