about
Sacubitril/valsartan in heart failure: latest evidence and place in therapyNeurochemical profile of dementia pugilisticaSuppression of eIF2α kinases alleviates Alzheimer's disease-related plasticity and memory deficits.Peripherally expressed neprilysin reduces brain amyloid burden: a novel approach for treating Alzheimer's disease.Hypoxia-induced down-regulation of neprilysin by histone modification in mouse primary cortical and hippocampal neurons.Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.Expression and functional profiling of neprilysin, insulin-degrading enzyme, and endothelin-converting enzyme in prospectively studied elderly and Alzheimer's brain.Proteomic identification of galectin-3 binding ligands and characterization of galectin-3 proteolytic cleavage in human prostasomesSomatostatin receptor subtype-4 agonist NNC 26-9100 decreases extracellular and intracellular Aβ₁₋₄₂ trimers.Reduction of amyloid-beta levels in mouse eye tissues by intra-vitreally delivered neprilysinAdvances in the pathogenesis of Alzheimer's disease: a re-evaluation of amyloid cascade hypothesis.Degradation of islet amyloid polypeptide by neprilysin.Evoking plasmin for beta-amyloid clearance.Insulin receptor dysfunction impairs cellular clearance of neurotoxic oligomeric a{beta}Following activation of the amyloid cascade, apolipoprotein E4 drives the in vivo oligomerization of amyloid-β resulting in neurodegeneration.Neprilysin and Aβ Clearance: Impact of the APP Intracellular Domain in NEP Regulation and Implications in Alzheimer's DiseaseChanging the treatment of heart failure with reduced ejection fraction: clinical use of sacubitril-valsartan combinationSink hypothesis and therapeutic strategies for attenuating Abeta levels.Proteolytic degradation of amyloid β-protein.Metallostasis and amyloid β-degrading enzymes.Beta-amyloidolysis and glutathione in Alzheimer's disease.Vitamin E: Curse or Benefit in Alzheimer's Disease? A Systematic Investigation of the Impact of α-, γ- and δ-Tocopherol on Aß Generation and Degradation in Neuroblastoma Cells.Activation of 5-HT(2C) receptor promotes the expression of neprilysin in U251 human glioma cells.Huperzine A alleviates synaptic deficits and modulates amyloidogenic and nonamyloidogenic pathways in APPswe/PS1dE9 transgenic mice.The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a {beta}-secretase-dependent pathwayA Group of Weakly Bound to Neurons Extracellular Metallopeptidases (NEMPs).Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease.APP intracellular domain derived from amyloidogenic β- and γ-secretase cleavage regulates neprilysin expression.The role of zinc in Alzheimer's disease.Co-Administration of TiO2 Nanowired Mesenchymal Stem Cells with Cerebrolysin Potentiates Neprilysin Level and Reduces Brain Pathology in Alzheimer's Disease.Curcumin Ameliorates Memory Decline via Inhibiting BACE1 Expression and β-Amyloid Pathology in 5×FAD Transgenic Mice.Valproic acid reduces neuritic plaque formation and improves learning deficits in APP(Swe) /PS1(A246E) transgenic mice via preventing the prenatal hypoxia-induced down-regulation of neprilysin.Neprilysin in the cerebrospinal fluid and serum of patients infected with HIV1- subtypes C and B.Impaired hepatic amyloid-beta degradation in Alzheimer's disease
P2860
Q28070191-C14F2455-3800-47D1-A68E-C6BD92DA15ACQ28384455-AE2E26BA-B9D5-4909-91D1-EADA0618879AQ30543820-BEF795D7-548A-468E-B0C1-5DE16E0C9395Q33705401-5437C246-BFF0-4E17-86D2-FF21CBFDBE46Q33895062-0CCEEE6E-E52F-4300-931D-3B20B526234FQ33897696-02575119-B7E2-4986-933A-001B2200F537Q34130147-9B284054-3779-4B5B-9021-C9641828EDB2Q34268051-26425603-5EBF-4299-A3D0-E3A6977D3847Q35923336-FB8CDD58-C3B0-400F-818B-818C54685033Q36319298-A648C068-988E-49A5-8C44-D09E8B6216B6Q36478423-8FBB3AAC-111A-40C1-91D5-3A1F444DE5D6Q36862586-2FE21E41-AB63-4675-A4F8-4666F0B876B2Q37234992-4CF3279B-133C-463D-99DB-8D91E06B4F9FQ37253971-90E23010-89FD-4327-8D14-B33E6E404207Q37313065-35D905E6-7FBE-4976-A30F-138F2AD815B4Q37408544-0EA5373F-ED82-45E6-BB1E-AE57FAEE1A49Q37597972-A04DA77D-FCE4-4E1E-A8BF-59F309D55A63Q37844327-5EB3970B-FF39-4A36-B2BC-D98407FF75F1Q38016899-6349D97A-A00D-4D7C-9B3A-C2125F5511CEQ38029514-D1B6DD74-71F8-44D3-BAFD-E7464D52E837Q38104717-C035667A-3799-4BA8-B4C1-C2CBB91AB516Q38866263-A5A50A51-C9CF-47E2-AAC3-887B732149D2Q38934489-1A04AAF8-FFB4-4B80-A9B3-F5FDD6BA4AEFQ39457273-A71B83C2-C01C-45A6-9293-E7A407BBA17DQ39641837-F0FD1E76-667F-45E0-8795-29E3C179452EQ39650176-B28EB160-7A62-4622-B583-3CF3202746CFQ39908636-2DD50AA6-D9F1-4FF4-A5B8-D8D979D86AE6Q41072443-2D0792B5-3AA8-44B7-B93C-7D3C1BE502BFQ41488419-AE2C8B55-C2A8-4166-B919-ECC754C50D82Q47750317-EBCA4B7A-5A3D-433E-A17E-10364BD420C6Q48881749-7945F655-0A3A-452E-928A-6F09401ED7F2Q50706209-28A0631A-1683-4D9A-B654-3A4F1FBAA824Q52730355-3614FBF2-DC34-4D3A-9443-3EB534671A98Q58759988-2958E41D-7865-4157-9EF5-9F735FCD1648
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Neprilysin and amyloid beta peptide degradation.
@en
Neprilysin and amyloid beta peptide degradation.
@nl
type
label
Neprilysin and amyloid beta peptide degradation.
@en
Neprilysin and amyloid beta peptide degradation.
@nl
prefLabel
Neprilysin and amyloid beta peptide degradation.
@en
Neprilysin and amyloid beta peptide degradation.
@nl
P1476
Neprilysin and amyloid beta peptide degradation.
@en
P2093
David W Rodgers
Louis B Hersh
P304
P356
10.2174/156720508783954703
P577
2008-04-01T00:00:00Z