pH-dependent structural transitions of Alzheimer amyloid peptides.
about
An atomic model for the pleated beta-sheet structure of abeta amyloid protofilamentsConversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteinsNovel therapeutics for Alzheimer's disease: an updateMelatonin and Other Tryptophan Metabolites Produced by Yeasts: Implications in Cardiovascular and Neurodegenerative DiseasesSecondary Structure of Huntingtin Amino-Terminal RegionBeta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residuesSupramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent.Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble saltsAmyloid fibril formation by an SH3 domain.The divergence, actions, roles, and relatives of sodium-coupled bicarbonate transportersConcentration effect on the aggregation of a self-assembling oligopeptide.Comparison of the structures of beta amyloid peptide (25-35) and substance P in trifluoroethanol/water solution.Amyloid structure and assembly: insights from scanning transmission electron microscopy.Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils.Recent Advances of Activatable Molecular Probes Based on Semiconducting Polymer Nanoparticles in Sensing and Imaging.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths.The protofilament structure of insulin amyloid fibrils.In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopyPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.The functions of the amyloid precursor protein gene.Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsStructure of core domain of fibril-forming PHF/Tau fragments.Anti-amyloidogenic and anti-apoptotic role of melatonin in Alzheimer diseaseSurface effects mediate self-assembly of amyloid-β peptides.Physiopathological modulators of amyloid aggregation and novel pharmacological approaches in Alzheimer's disease.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational studyGas-phase structure of amyloid-β (12-28) peptide investigated by infrared spectroscopy, electron capture dissociation and ion mobility mass spectrometry.Frontiers in Alzheimer's disease therapeutics.Genetics, lifestyle and the roles of amyloid beta and oxidative stress in Alzheimer's disease.Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.Linking folding with aggregation in Alzheimer's beta-amyloid peptidesAnalysis of the interaction between heparin and follistatin and heparin and follistatin-ligand complexes using surface plasmon resonance.Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.Prophylactic melatonin significantly reduces Alzheimer's neuropathology and associated cognitive deficits independent of antioxidant pathways in AβPP(swe)/PS1 mice.Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro.Scanning tunnelling microscopy studies of beta-amyloid fibril structure and assembly.
P2860
Q24170232-0F78A281-F3DC-4E24-8466-18D14A4686C7Q24564014-659C2D20-116B-4233-8F19-E3463FB8081FQ24620383-E033C194-41C5-4803-B933-C8F74AC31FDEQ26772733-10AC546A-0AF0-403F-8D4A-072C479F812AQ27657408-375AB370-B639-4DC8-828D-84992B757F59Q27676093-4DAABE86-2FEC-4523-A3B5-86243A949081Q28386697-C3F59241-8633-4589-8074-F2CA2CCC6DC2Q28386755-37F6C78E-F212-4930-9C6E-1416A116187BQ28387541-F8A9B32F-5A06-4A8B-A3F1-EDB14EACA85AQ30176202-57B00C91-5FBF-4437-B05D-A50733F1EA93Q30440948-830A93D3-8A1A-4C6B-ADF1-35321D9186C6Q30503518-E1BFB741-881D-4C14-A21F-2B4197E5DCDAQ30584433-C6E28637-E282-4EDE-A3A6-8E402668CC16Q33702933-BAAD6332-7F0A-4DA1-A50A-6869F5547162Q33793290-C0A5BEB2-2443-4B97-B5E8-53941B4C1C5CQ33806298-DACFABE6-5556-47AE-B360-8B2A62BECE25Q33893017-63406AE2-B9EC-4ED3-BEE4-F2172FC73A03Q34018579-04BD813C-D972-41C7-B574-F6BB56F43481Q34034361-DEE40724-E075-4BDF-AE95-65E6C7344DD7Q34040648-293AC37A-2C32-4A49-A515-9489F162FACDQ34059772-99268BFE-63AC-49FF-9720-E5AA37016030Q34092116-AFF899BE-D8A7-4100-AB55-60D7FF4F3E74Q34167200-7C4A53E3-836E-4784-B7C9-13D9AF79757FQ34173160-310E59B5-9471-4C76-957C-53C4BE79B7C5Q34184303-ED5BA92B-093C-43EE-9804-2584FCB9912EQ34354306-9C8DAEBC-E979-44AA-AE5D-BDB855767BDEQ34402167-8D6168C7-AE46-4DE3-95AD-487C9F9154BFQ34419863-42BB90BE-A516-44BC-99D6-328211C38DCEQ34721350-BCC9193B-85F2-4AAE-B8D0-1DAAA6ABF5CEQ34923134-491ED281-5A85-48B3-A071-B09FF409C2E4Q34991319-20CFD0DF-3E5E-45C8-A543-4C0CC0A82C6AQ35086876-652091D2-6511-45A9-89BA-3BBB9AB4E3B8Q35607880-E206675F-B4A5-4F94-892B-91AD3EB87B8AQ36022813-DF29D622-817E-43E7-8F12-27ECEDF18754Q36089177-D68889C0-69AA-43B1-BFA5-32A603749BF9Q36311737-C5643CD4-5CBB-410C-925D-C22725C0FB04Q36321873-E651F04F-9CCA-4EFD-A48F-CFE5C43B2442Q36433222-E0E9D209-0149-4CB5-AA0F-F097608300AFQ36606154-7DA722DC-28A9-40E5-822D-8B08F5A96C78Q36693415-2274573A-E7BC-46D7-A04B-F51D046B2F6C
P2860
pH-dependent structural transitions of Alzheimer amyloid peptides.
description
1991 nî lūn-bûn
@nan
1991 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
pH-dependent structural transitions of Alzheimer amyloid peptides.
@ast
pH-dependent structural transitions of Alzheimer amyloid peptides.
@en
pH-dependent structural transitions of Alzheimer amyloid peptides.
@nl
type
label
pH-dependent structural transitions of Alzheimer amyloid peptides.
@ast
pH-dependent structural transitions of Alzheimer amyloid peptides.
@en
pH-dependent structural transitions of Alzheimer amyloid peptides.
@nl
prefLabel
pH-dependent structural transitions of Alzheimer amyloid peptides.
@ast
pH-dependent structural transitions of Alzheimer amyloid peptides.
@en
pH-dependent structural transitions of Alzheimer amyloid peptides.
@nl
P2093
P2860
P1433
P1476
pH-dependent structural transitions of Alzheimer amyloid peptides.
@en
P2093
D A Kirschner
J T Nguyen
P E Fraser
W K Surewicz
P2860
P304
P356
10.1016/S0006-3495(91)82154-3
P407
P577
1991-11-01T00:00:00Z