Works matching DE "AMYLOID"
Results: 5000
Synaptic protein CSF levels relate to memory scores in individuals without dementia.
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- Alzheimer's Research & Therapy, 2025, v. 17, n. 1, p. 1, doi. 10.1186/s13195-025-01703-z
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Nonspecific Interaction of Immunoglobulins (IgG) with Human Beta-2 Microglobulin Fibrils.
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- Journal of Evolutionary Biochemistry & Physiology, 2025, v. 61, n. 1, p. 153, doi. 10.1134/S0022093025010120
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The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis.
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- Biological Trace Element Research, 2025, v. 203, n. 3, p. 1251, doi. 10.1007/s12011-024-04245-x
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Classification of amyloidosis and protein misfolding disorders in animals 2024: A review on pathology and diagnosis.
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- Veterinary Pathology, 2025, v. 62, n. 2, p. 117, doi. 10.1177/03009858241283750
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Deletion of Murine APP Aggravates Tau and Amyloid Pathologies in the 5xFADXTg30 Alzheimer's Disease Model.
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- Biomolecules (2218-273X), 2025, v. 15, n. 2, p. 159, doi. 10.3390/biom15020159
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Retraction Note: K284-6111 prevents the amyloid beta-induced neuroinflammation and impairment of recognition memory through inhibition of NF-κB-mediated CHI3L1 expression.
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- 2025
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- Correction Notice
On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.
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- International Journal of Molecular Sciences, 2025, v. 26, n. 4, p. 1637, doi. 10.3390/ijms26041637
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Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.
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- International Journal of Molecular Sciences, 2025, v. 26, n. 4, p. 1512, doi. 10.3390/ijms26041512
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Treating Hereditary TTR Amyloid Polyneuropathy with Patisiran.
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- Neurology Alert, 2025, v. 44, n. 7, p. 1
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- Article
Selective suppression of oligodendrocyte-derived amyloid beta rescues neuronal dysfunction in Alzheimer's disease.
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- PLoS Biology, 2024, v. 22, n. 7, p. 1, doi. 10.1371/journal.pbio.3002727
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RELATIONSHIP BETWEEN ACUTE PHASE PROTEINS AND SUBSEQUENT FERTILITY OF DAIRY COWS AFTER POSTPARTUM UTERINE INFLAMMATION AND HEALTHY COWS.
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- Veterinarija ir Zootechnika, 2015, v. 70, n. 92, p. 6
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Calcitonin Gene-Related Peptide Upregulates Serum Amyloid A Synthesis through Activation of Interleukin-6.
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- Bioscience, Biotechnology & Biochemistry, 2013, v. 77, n. 10, p. 2151, doi. 10.1271/bbb.130450
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Stimulation of the Amyloidogenic Pathway by Cytoplasmic Superoxide Radicals in an Alzheimer's Disease Mouse Model.
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- Bioscience, Biotechnology & Biochemistry, 2012, v. 76, n. 6, p. 1098, doi. 10.1271/bbb.110934
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Inhibition of Aggregation of Amyloid &bgr;42 by Arginine-Containing Small Compounds.
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- Bioscience, Biotechnology & Biochemistry, 2012, v. 76, n. 4, p. 762, doi. 10.1271/bbb.110879
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Identification of Novel Short Peptide Inhibitors of Soluble 37/48 kDa Oligomers of Amyloid β42.
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- Bioscience, Biotechnology & Biochemistry, 2011, v. 75, n. 8, p. 1496, doi. 10.1271/bbb.110198
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Silymarin Attenuated the Amyloid β Plaque Burden and Imprové4 Behavioral Abnormalities in an Alzheimer's Disease Mouse Model.
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- Bioscience, Biotechnology & Biochemistry, 2010, v. 74, n. 11, p. 2299, doi. 10.1271/bbb.100524
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Selection of Peptide Inhibitors of Soluble Aβ<sub>1-42</sub> Oligomer Formation by Phage Display.
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- Bioscience, Biotechnology & Biochemistry, 2010, v. 74, n. 11, p. 2214, doi. 10.1271/bbb.100388
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Induction of Serum Amyloid A Genes Is Associated with Growth and Apoptosis of HC11 Mammary Epithelial Cells.
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- Bioscience, Biotechnology & Biochemistry, 2008, v. 72, n. 1, p. 70, doi. 10.1271/bbb.70374
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Systematic Analysis of Aggregates from 38 Kinds of Non Disease-Related Proteins: Identifying the Intrinsic Propensity of Polypeptides to Form Amyloid Fibrils.
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- Bioscience, Biotechnology & Biochemistry, 2007, v. 71, n. 5, p. 1313, doi. 10.1271/bbb.60718
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(2142) Proposal to conserve the name Peziza ammophila Durieu & Lev. 1848 against P. ammophila Saut. 1841 (Ascomycota: Pezizaceae).
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- Taxon, 2013, v. 62, n. 3, p. 628, doi. 10.12705/623.19
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Preventing Neurodegeneration.
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- Innovation, 2004, v. 4, n. 2, p. 52
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Characterizing the Oligomers Distribution along the Aggregation Pathway of Amyloid Aβ1‐40 by NMR.
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- Chemistry - A European Journal, 2024, v. 30, n. 38, p. 1, doi. 10.1002/chem.202400594
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Amphiphilic Molecules Exhibiting Zwitterionic Excited‐State Intramolecular Proton Transfer and Near‐Infrared Emission for the Detection of Amyloid β Aggregates in Alzheimer's Disease.
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- Chemistry - A European Journal, 2023, v. 29, n. 64, p. 1, doi. 10.1002/chem.202302408
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Beta Amyloid Oligomers with Higher Cytotoxicity have Higher Sidechain Dynamics.
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- Chemistry - A European Journal, 2023, v. 29, n. 58, p. 1, doi. 10.1002/chem.202301879
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Inhibition of Amyloid β Aggregation and Cytotoxicity by Berbamine Hydrochloride.
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- Chemistry - A European Journal, 2023, v. 29, n. 56, p. 1, doi. 10.1002/chem.202301865
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Real‐Time Observation for Dynamic Oscillation during Self‐Assembly and Clearance of Aβ42.
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- Chemistry - A European Journal, 2023, v. 29, n. 35, p. 1, doi. 10.1002/chem.202300142
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Cucurbit[7]uril Inhibits Islet Amyloid Polypeptide Aggregation by Targeting N Terminus Hot Segments and Attenuates Cytotoxicity.
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- Chemistry - A European Journal, 2022, v. 28, n. 38, p. 1, doi. 10.1002/chem.202201698
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Versatile Near‐Infrared Super‐Resolution Imaging of Amyloid Fibrils with the Fluorogenic Probe CRANAD‐2.
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- Chemistry - A European Journal, 2022, v. 28, n. 19, p. 1, doi. 10.1002/chem.202200026
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Unimolecular Chemiexcited Oxygenation of Pathogenic Amyloids.
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- Angewandte Chemie, 2024, v. 136, n. 31, p. 1, doi. 10.1002/ange.202405605
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Exploring Peptido‐Nanocomposites in the Context of Amyloid Diseases.
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- Angewandte Chemie, 2024, v. 136, n. 9, p. 1, doi. 10.1002/ange.202309958
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Chemical Imaging of RNA‐Tau Amyloid Fibrils at the Nanoscale Using Tip‐Enhanced Raman Spectroscopy.
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- Angewandte Chemie, 2023, v. 135, n. 50, p. 1, doi. 10.1002/ange.202314369
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Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP.
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- Angewandte Chemie, 2023, v. 135, n. 50, p. 1, doi. 10.1002/ange.202310230
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Creating an Amyloid 'Kaleidoscope' Using Short Iodinated Peptides.
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- Angewandte Chemie, 2023, v. 135, n. 42, p. 1, doi. 10.1002/ange.202310737
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Titelbild: Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten (Angew. Chem. 19/2023).
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- Angewandte Chemie, 2023, v. 135, n. 19, p. 1, doi. 10.1002/ange.202304138
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Amyloid Against Amyloid: Dimeric Amyloid Fragment Ameliorates Cognitive Impairments by Direct Clearance of Oligomers and Plaques.
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- Angewandte Chemie, 2023, v. 135, n. 7, p. 1, doi. 10.1002/ange.202210209
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Cross β Amyloid Nanotubes Demonstrate Promiscuous Catalysis in a Chemical Reaction Network via Co‐option.
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- Angewandte Chemie, 2022, v. 134, n. 48, p. 1, doi. 10.1002/ange.202210972
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pH Dependence of Amyloid‐β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes.
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- Angewandte Chemie, 2022, v. 134, n. 48, p. 1, doi. 10.1002/ange.202210675
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3D Blockage Mapping for Identifying Familial Point Mutations in Single Amyloid‐β Peptides with a Nanopore.
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- Angewandte Chemie, 2022, v. 134, n. 44, p. 1, doi. 10.1002/ange.202209970
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Fluorescent Microswimmers Based on Cross‐β Amyloid Nanotubes and Divergent Cascade Networks.
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- Angewandte Chemie, 2022, v. 134, n. 29, p. 1, doi. 10.1002/ange.202201547
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Site‐Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation.
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- Angewandte Chemie, 2022, v. 134, n. 16, p. 1, doi. 10.1002/ange.202115336
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A Fluorescent Sensor for Quantitative Super‐Resolution Imaging of Amyloid Fibril Assembly**.
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- Angewandte Chemie, 2022, v. 134, n. 10, p. 1, doi. 10.1002/ange.202112832
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Inhibitor‐Mediated Structural Transition in a Minimal Amyloid Model.
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- Angewandte Chemie, 2022, v. 134, n. 3, p. 1, doi. 10.1002/ange.202113845
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Chiral Selectivity of Secondary Nucleation in Amyloid Fibril Propagation.
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- Angewandte Chemie, 2021, v. 133, n. 45, p. 24210, doi. 10.1002/ange.202108648
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Nanoscale Hyperspectral Imaging of Amyloid Secondary Structures in Liquid.
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- Angewandte Chemie, 2021, v. 133, n. 9, p. 4595, doi. 10.1002/ange.202010331
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Protofibril–Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation.
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- Angewandte Chemie, 2021, v. 133, n. 6, p. 3053, doi. 10.1002/ange.202010098
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Complex Cascade Reaction Networks via Cross β Amyloid Nanotubes.
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- Angewandte Chemie, 2021, v. 133, n. 1, p. 204, doi. 10.1002/ange.202011454
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Nanochaperone‐Based Strategies to Control Protein Aggregation Linked to Conformational Diseases.
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- Angewandte Chemie, 2021, v. 133, n. 1, p. 41, doi. 10.1002/ange.202007924
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Rhizolutin, a Novel 7/10/6‐Tricyclic Dilactone, Dissociates Misfolded Protein Aggregates and Reduces Apoptosis/Inflammation Associated with Alzheimer's Disease.
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- Angewandte Chemie, 2020, v. 132, n. 51, p. 23194, doi. 10.1002/ange.202009294
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Non‐Equilibrium Polymerization of Cross‐β Amyloid Peptides for Temporal Control of Electronic Properties.
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- Angewandte Chemie, 2020, v. 132, n. 32, p. 13608, doi. 10.1002/ange.202003721
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Discovery of Chemicals to Either Clear or Indicate Amyloid Aggregates by Targeting Memory‐Impairing Anti‐Parallel Aβ Dimers.
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- Angewandte Chemie, 2020, v. 132, n. 28, p. 11588, doi. 10.1002/ange.202002574
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