Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
about
Alpha1-antichymotrypsin/Alzheimer's peptide Abeta(1-42) complex perturbs lipid metabolism and activates transcription factors PPARgamma and NFkappaB in human neuroblastoma (Kelly) cellsThe coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathwayAssociation of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor proteinMolecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer diseaseLysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin Sbeta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer diseaseA capillary electrophoresis method for evaluation of Abeta proteolysis in vitroBiological markers of amyloid beta-related mechanisms in Alzheimer's diseaseCurcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st centurySoluble oligomers of the amyloid beta-protein impair synaptic plasticity and behaviorProtein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseasesAggregation and disaggregation of senile plaques in Alzheimer diseaseBACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor proteinOverview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal CompoundsTargeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The role of APP and BACE1 trafficking in APP processing and amyloid-β generationDementia of the eye: the role of amyloid beta in retinal degenerationPlatelets and Alzheimer's disease: Potential of APP as a biomarkerEarly etiology of Alzheimer's disease: tipping the balance toward autophagy or endosomal dysfunction?Tailoring the antibody response to aggregated Aß using novel Alzheimer-vaccinesMolecular basis for passive immunotherapy of Alzheimer's diseaseCrystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose OctasulfateAPP processing in Alzheimer's diseaseRegulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding proteinProtection against beta-amyloid-induced apoptosis by peptides interacting with beta-amyloidAlzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzymeTrafficking and proteolytic processing of APPIncreased beta-amyloid levels in the choroid plexus following lead exposure and the involvement of low-density lipoprotein receptor protein-1CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammationPreferential interactions between ApoE-containing lipoproteins and Aβ revealed by a detection method that combines size exclusion chromatography with non-reducing gel-shiftNumerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesDiffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxinsAlzheimer's associated β-amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytes.The sour side of neurodegenerative disorders: the effects of protein glycation.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Human antibodies reactive with beta-amyloid protein in Alzheimer's diseaseStem cell derived basal forebrain cholinergic neurons from Alzheimer's disease patients are more susceptible to cell death.Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.Selection of peptides binding to the amyloid b-protein reveals potential inhibitors of amyloid formation.
P2860
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P2860
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
description
1992 nî lūn-bûn
@nan
1992 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@ast
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@en
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@nl
type
label
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@ast
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@en
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@nl
prefLabel
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@ast
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@en
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@nl
P2093
P356
P1433
P1476
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.
@en
P2093
Schlossmacher M
Swindlehurst C
Vigo-Pelfrey C
P2888
P304
P356
10.1038/359325A0
P407
P577
1992-09-01T00:00:00Z
P6179
1020938642