ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
about
The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrilsNew Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid MembranesPushing the detection limit of infrared spectroscopy for structural analysis of dilute protein samples.Mid-infrared spectroscopy for protein analysis: potential and challenges.Are current atomistic force fields accurate enough to study proteins in crowded environments?Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Nanoscale spatially resolved infrared spectra from single microdroplets.Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid foldThe OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systemsTwo distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes.Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.Nanoscale studies link amyloid maturity with polyglutamine diseases onset.Amyloid-β 1-24 C-terminal truncated fragment promotes amyloid-β 1-42 aggregate formation in the healthy brain.AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Role of water in chromosome spreading and swelling induced by acetic acid treatment: a FTIR spectroscopy study.Thermal-triggerd proteinquake leads to disassembly of DegP hexamer as an imperative activation step.Proteomics applications in prion biology and structure.Effects of small-molecule amyloid modulators on a Drosophila model of Parkinson's disease.Optimization and partial characterization of intracellular anticandidal protein from Aspergillus giganteus MTCC 8408 using taguchi DOE.Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide.Hydrogel coated mesh decreases tissue reaction resulting from polypropylene mesh implant: implication in hernia repair.Self-assembly of 33-mer gliadin peptide oligomers.Combined experimental and simulation studies suggest a revised mode of action of the anti-Alzheimer disease drug NQ-Trp.Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.Characterization of Amyloid Cores in Prion Domains.How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.A modular self-assembly approach to functionalised β-sheet peptide hydrogel biomaterials.Simultaneous acquisition of infrared, fluorescence and light scattering spectra of proteins: direct evidence for pre-fibrillar species in amyloid fibril formation.Probing the role of aromatic residues in the self-assembly of Aβ(16-22) in fluorinated alcohols and their aqueous mixtures.Multistep Conformation Selection in Amyloid Assembly.Detection of Aβ plaque-associated astrogliosis in Alzheimer's disease brain by spectroscopic imaging and immunohistochemistry.Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy.Simultaneous IR-Spectroscopic Observation of α-Synuclein, Lipids, and Solvent Reveals an Alternative Membrane-Induced Oligomerization Pathway.Controlled Exposure of Bioactive Growth Factor in 3D Amyloid Hydrogel for Stem Cells Differentiation.Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTR105-115 Mutant.
P2860
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P2860
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@ast
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@en
type
label
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@ast
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@en
prefLabel
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@ast
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@en
P2093
P3181
P1476
ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.
@en
P2093
Erik Goormaghtigh
Jean-Marie Ruysschaert
Rabia Sarroukh
Vincent Raussens
P304
P3181
P356
10.1016/J.BBAMEM.2013.04.012
P407
P577
2013-06-05T00:00:00Z