About: Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis

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About: Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1996 (uk) im Mai 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 1996 (ast) scientific article published on 01 May 1996 (en)
publication date	wds:Q71077761-F49DF8FC-4C18-4D69-A26D-BB4B1F0E835A
publication date	1996-05-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q71077761-48E6E9C5-A702-43B2-BC69-30E491E9C1D7 wds:Q71077761-56CCA397-196A-45CF-96A2-E5801573C29E wds:Q71077761-9E43909A-69A5-4FF4-9893-BE3FB0764D47 wds:Q71077761-E7A64B66-FFA5-4058-931E-DE479A46EC8C
author name string	Mason RP Kelly JF Mason PE Estermyer JD
rdfs:label	Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (en) Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (nl)
skos:prefLabel	Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (en) Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (nl)
name	Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (en) Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (nl)
title	wds:Q71077761-A2CBF3CF-A356-4AA1-8FB8-5A154D441762
title	Alzheimer's disease amyloid beta peptide 25-35 is localized in the membrane hydrocarbon core: x-ray diffraction analysis (en)
page(s)	wds:Q71077761-FA7E14EE-4884-4D8B-8E16-0D3388FC229E
page(s)	78-82
instance of	wds:Q71077761-A53103F0-7DF8-466F-89FC-234B868D64E4
instance of	scholarly article
main subject	wds:Q71077761-9E645264-E314-4648-87E8-655C866606E4 wds:Q71077761-A205F6B8-F872-417F-A5E0-AAA8D65FC475
main subject	Alzheimer's disease X-ray diffraction
PubMed ID	wds:Q71077761-07288DBD-008B-4DCD-90B8-A6AC59BECA6C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8630078
PubMed ID	8630078
published in	wds:Q71077761-BCA5EA44-5AD3-4734-8868-B76006FE9862
published in	Biochemical and Biophysical Research Communications
issue	wds:Q71077761-1E12E88D-A106-43FB-B7CA-ED29CF706590
volume	wds:Q71077761-B7835AEC-EEDD-48AF-949D-070DB8EF46F3
issue	1
volume	222
DOI	wds:Q71077761-0EDF04F7-523F-4539-BCB6-D155FAFBE5B5
DOI	http://dx.doi.org/10.1006/BBRC.1996.0699
DOI	10.1006/BBRC.1996.0699
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71077761
is cites work of	The modulating effect of mechanical changes in lipid bilayers caused by apoE-containing lipoproteins on Aβ induced membrane disruption Elevated oxidative stress in models of normal brain aging and Alzheimer's disease Amyloid beta-protein interactions with membranes and cholesterol: causes or casualties of Alzheimer's disease Distribution and fluidizing action of soluble and aggregated amyloid beta-peptide in rat synaptic plasma membranes. Coenzyme Q10 protects human endothelial cells from β-amyloid uptake and oxidative stress-induced injury Regional membrane phospholipid alterations in Alzheimer's disease. A novel action of alzheimer's amyloid beta-protein (Abeta): oligomeric Abeta promotes lipid release. Embedding Aβ42 in heterogeneous membranes depends on cholesterol asymmetries Abeta25-35 induces rapid lysis of red blood cells: contrast with Abeta1-42 and examination of underlying mechanisms Cholesterol as a causative factor in Alzheimer's disease: a debatable hypothesis Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL Amyloid beta-peptide induces cholinergic dysfunction and cognitive deficits: a minireview Reduced membrane lipids in the cortex of Alzheimer's disease transgenic mice Architecture of the Alzheimer's A beta P ion channel pore Designed amyloid beta peptide fibril - a tool for high-throughput screening of fibril inhibitors Membrane destabilization induced by β-amyloid peptide 29-42: Importance of the amino-terminus Assemblies of Alzheimer's peptides A beta 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction. Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption Beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents Amyloid beta peptide membrane perturbation is the basis for its biological effects Autoinsertion of soluble oligomers of Alzheimer's Abeta(1-42) peptide into cholesterol-containing membranes is accompanied by relocation of the sterol towards the bilayer surface. Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay. Lipids in Amyloid-β Processing, Aggregation, and Toxicity The interaction between amyloid-β peptides and anionic lipid membranes containing cholesterol and melatonin Biochemical identification of a linear cholesterol-binding domain within Alzheimer's β amyloid peptide Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition. X-Ray fiber and powder diffraction of PrP prion peptides. Structure of amyloid β in lipid environment and cholesterol-dependent membrane pore formation The influence of phospholipid membranes on bovine calcitonin secondary structure and amyloid formation The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol. Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets. De novo aggregation of Alzheimer's Aβ25-35 peptides in a lipid bilayer Membrane-Modulating Drugs can Affect the Size of Amyloid-β Aggregates in Anionic Membranes
is cites work of	wds:Q28543468-1C9AA219-D0D2-487E-B637-07BA40633250 wds:Q34175164-F677F9E0-0027-4971-804E-937571AD57C1 wds:Q35089446-2B14E861-93CA-47A3-996B-5566AF904001 wds:Q33790830-4F5D6F29-514A-40A1-8425-76D66A1A9D04 wds:Q40217129-8C4C6F02-73D3-400F-8E67-717A524644F1 wds:Q34180669-2653B274-D05F-4F9D-9946-480DE6605B19 wds:Q37066023-A4650E9F-663D-45EB-82EC-E4EB787B7502 wds:Q48524004-E38AE286-570D-4453-9120-0361E1794ACA wds:Q30777774-FD0E5B37-6E9A-4C1E-9F0C-E29834079B1C wds:Q37722680-5DB08371-F344-4AB4-B426-1BFE1409D983 wds:Q61587511-942F2409-073B-4E0C-884C-A822269D84AD wds:Q34750579-43C6E230-4530-4FF3-A005-6E0754386CF9 wds:Q37117427-C31B50CE-CBB1-42E0-8892-258DF70D7C1B wds:Q39369410-C1EC970C-8700-44B1-93FE-36060966E74A wds:Q33260929-86A6267D-23A2-4F75-BDAD-2CF97A4ED6D4 wds:Q36476839-5C634C26-CE09-463E-BEBB-216257B0DF71 wds:Q33781604-E9EB5AD6-7555-4815-BAFF-1F9148F83E15 wds:Q44795710-5C80B0EA-DD17-452B-9BF2-4ED642064061 wds:Q41666582-F32C8DDC-6932-4DA6-BCD2-B1F18C06AE95 wds:Q64061138-1E753C50-E701-4A68-B4DD-13B1DA6D88F4

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