Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth
about
A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured stateA computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formationPolyanionic candidate microbicides accelerate the formation of semen-derived amyloid fibrils to enhance HIV-1 infectionAmyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation.Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site.Heterologous amyloid seeding: revisiting the role of acetylcholinesterase in Alzheimer's disease.Heparan sulfate accumulation with Abeta deposits in Alzheimer's disease and Tg2576 mice is contributed by glial cells.Targeting Abeta and tau in Alzheimer's disease, an early interim reportHeparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Effects of heparin and enoxaparin on APP processing and Aβ production in primary cortical neurons from Tg2576 mice.Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid AShort-chain aliphatic polysulfonates inhibit the entry of Plasmodium into red blood cellsMidkine as a factor to counteract the deposition of amyloid β-peptide plaques: in vitro analysis and examination in knockout mice.Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversionPhysiopathological modulators of amyloid aggregation and novel pharmacological approaches in Alzheimer's disease.Heparin nanoparticles for β amyloid binding and mitigation of β amyloid associated cytotoxicity.Inhibition of amyloid A amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2-deoxy-alpha- and beta-d-glucose: implications for the treatment of various amyloidoses.Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit.Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation.Polyanions and the proteome.Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Cellular interaction and cytotoxicity of the iowa mutation of apolipoprotein A-I (ApoA-IIowa) amyloid mediated by sulfate moieties of heparan sulfate.Molecular interactions in the formation and deposition of beta2-microglobulin-related amyloid fibrils.Disease modifying therapy for AD?Small molecule inhibitors of Abeta assembly.Heparan sulphate biosynthesis and disease.Heparin accelerates gelsolin amyloidogenesis.Amyloid-β Precursor Protein Modulates the Sorting of Testican-1 and Contributes to Its Accumulation in Brain Tissue and Cerebrospinal Fluid from Patients with Alzheimer Disease.Amyloid-beta interactions with chondroitin sulfate-derived monosaccharides and disaccharides. implications for drug development.The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Protein/Peptide Aggregation and Amyloidosis on Biointerfaces.Nanotechnology based theranostic approaches in Alzheimer's disease management: Current status and future perspective.Double-stranded DNA stereoselectively promotes aggregation of amyloid-like fibrils and generates peptide/DNA matrices.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity.Sulfated glycosaminoglycans in protein aggregation diseases.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.
P2860
Q28346218-9E5B54AB-E254-47AB-B03B-2F526D4A38CFQ28474733-46101146-FA91-47DB-9CA4-E7B5E24E5A9AQ28489042-BBEE775F-47C1-4C64-862D-D4B37BC03051Q30167545-D7F40D0B-3645-42AB-8978-EA2BE0B177C4Q31807323-F37F5B9F-2205-4954-A4A5-E748487A8EEAQ33181061-0E90C688-24AF-49D5-BD6E-4E3CFAB0A046Q33291757-DE5B5A02-68C5-4945-90AA-FBB35D966975Q33795144-CA14B2F2-64EF-4129-ACE0-320CFF32E423Q33829008-5ACADB70-899A-4B09-848D-B1A2BDE6BBE9Q33968252-CFF63AE8-1711-4CEE-8C5D-24E2B03F7AFCQ33988177-944A1DA0-B7A4-4591-B772-326A0FDBA3B9Q33993673-BE4E34C4-F413-4457-A667-4EE121114019Q34111618-40C771AB-24E7-4281-9A95-222109605AEFQ34506576-46CE5A83-BF78-4FEA-9493-67F2DFB04A3AQ34561167-6F03F6D2-CFB3-47A9-AB0F-ED7DB6C5FFA8Q34721350-0B0D339C-EDDD-4AA3-B50A-9DE588F26EB3Q35040469-BC237114-9B20-4444-A714-25A90540FAE1Q35098443-4D53DD1F-C446-4BF7-898B-56C7048A12C6Q35215412-544D2256-AC98-45C3-A728-573B6718D451Q35709805-25742B09-C864-4780-8925-D81E95F7ACDDQ35773099-75C30067-0C07-4B88-8CB9-5E07FEF9EE0AQ35881767-032CEF49-1A21-4351-9E55-1BD8A5077793Q36115813-1E9EC24F-930A-4FFC-91BA-BAA74B3A9CF0Q36217094-87F69C92-A9D1-4C27-9F25-B5102CE0C1ABQ36640414-6F466D7C-0C20-47A1-9E09-3D482704A9F6Q36911406-E31D1D09-E769-4F81-9AFF-40675811830AQ37119533-DDD5C131-770D-4608-B030-93FCFA866C09Q37132636-979E4412-1020-4206-8B1F-23632F35FD1BQ37241399-9900EBD7-766B-4611-9BCE-B0139DAB41E7Q38306026-154C315A-80ED-444C-B2A2-5C253CA60BA7Q38343014-FAA70B42-6660-443C-87A0-5FECF301AF83Q38635739-25857E43-2127-4A8D-A3A0-D570D01326F9Q38647304-D77D1FE6-2985-4CC5-8A14-5563481B6B30Q38686370-9D6FB064-6858-4EE9-AF65-163F4B16CCD4Q38950497-7307B072-1376-4499-A143-D84B507D48CEQ39126169-18CC0E89-6449-4E65-A1F2-6F4ECD70A07BQ39176222-A36A3DBF-6BCC-4759-AC41-8AE763A8B78EQ39236820-4808F943-5A1D-4F80-8681-A7D9C5E897A6Q39322110-34E8D2D7-0D6B-478D-BCFA-F640AFC82022Q39385143-CA2784FD-0799-4ADF-B90D-1B3CB00AC6DB
P2860
Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth
description
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Dezember 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/12/01)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/12/01)
@nl
наукова стаття, опублікована в грудні 1999
@uk
مقالة علمية (نشرت في ديسمبر 1999)
@ar
name
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@ast
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@en
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@nl
type
label
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@ast
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@en
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@nl
prefLabel
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@ast
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@en
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@nl
P2093
P3181
P1433
P1476
Interactions of Alzheimer amyl ...... n fibril nucleation and growth
@en
P2093
J. McLaurin
P. E. Fraser
T. Franklin
P304
P3181
P356
10.1046/J.1432-1327.1999.00957.X
P407
P577
1999-12-01T00:00:00Z