BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo - Wikidata - wikimedia - TriplyDB

BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo

BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo

http://www.wikidata.org/entity/Q36321125

about

Neurotrophic factors in Alzheimer’s disease: role of axonal transport Retromer deficiency observed in Alzheimer's disease causes hippocampal dysfunction, neurodegeneration, and Abeta accumulation The role of APP and BACE1 trafficking in APP processing and amyloid-β generation Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells Synaptic transmission block by presynaptic injection of oligomeric amyloid beta BACE1 expression and activity: relevance in Alzheimer's disease Alzheimer disease Abeta production in the absence of S-palmitoylation-dependent targeting of BACE1 to lipid rafts Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1 Depletion of GGA1 and GGA3 mediates postinjury elevation of BACE1 Axonal transport and neurodegenerative disease: can we see the elephant?BACE1, a major determinant of selective vulnerability of the brain to amyloid-beta amyloidogenesis, is essential for cognitive, emotional, and synaptic functions.Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis.Amyloid precursor protein-induced axonopathies are independent of amyloid-beta peptides.Presenilin controls kinesin-1 and dynein function during APP-vesicle transport in vivo Proteomic analysis of the amyloid precursor protein fragment C99: expression in yeast.ADAM10 missense mutations potentiate β-amyloid accumulation by impairing prodomain chaperone function Mutant amyloid precursor protein differentially alters adipose biology under obesogenic and non-obesogenic conditions.Neuritic deposits of amyloid-beta peptide in a subpopulation of central nervous system-derived neuronal cells.Intraneuronal APP, not free Aβ peptides in 3xTg-AD mice: implications for tau versus Aβ-mediated Alzheimer neurodegeneration.Cdk5 protein inhibition and Aβ42 increase BACE1 protein level in primary neurons by a post-transcriptional mechanism: implications of CDK5 as a therapeutic target for Alzheimer disease.Transcriptomic Changes Due to Cytoplasmic TDP-43 Expression Reveal Dysregulation of Histone Transcripts and Nuclear Chromatin.Axonal Terminals Exposed to Amyloid-β May Not Lead to Pre-Synaptic Axonal Damage.BACE2 expression increases in human neurodegenerative disease.Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer's disease.Metabolic Characterization of Intact Cells Reveals Intracellular Amyloid Beta but Not Its Precursor Protein to Reduce Mitochondrial Respiration.Inflammatory Eicosanoids Increase Amyloid Precursor Protein Expression via Activation of Multiple Neuronal Receptors.Retention in endoplasmic reticulum 1 (RER1) modulates amyloid-β (Aβ) production by altering trafficking of γ-secretase and amyloid precursor protein (APP).Mechanism of cerebral beta-amyloid angiopathy: murine and cellular models.Amyloid plaque pathogenesis in 5XFAD mouse spinal cord: retrograde transneuronal modulation after peripheral nerve injury Sorting through the cell biology of Alzheimer's disease: intracellular pathways to pathogenesis.Amyloid precursor protein and BACE function as oligomers.Partial BACE1 reduction in a Down syndrome mouse model blocks Alzheimer-related endosomal anomalies and cholinergic neurodegeneration: role of APP-CTF.Effects of TNFalpha-converting enzyme inhibition on amyloid beta production and APP processing in vitro and in vivo.Apolipoprotein E highly correlates with AbetaPP- and tau-related markers in human cerebrospinal fluid.Neuronal protein trafficking associated with Alzheimer disease: from APP and BACE1 to glutamate receptors Increased expression of reticulon 3 in neurons leads to reduced axonal transport of β site amyloid precursor protein-cleaving enzyme 1.BACE1 regulates voltage-gated sodium channels and neuronal activity.Disrupted-in-Schizophrenia-1 Attenuates Amyloid-β Generation and Cognitive Deficits in APP/PS1 Transgenic Mice by Reduction of β-Site APP-Cleaving Enzyme 1 Levels.Alzheimer's secretases regulate voltage-gated sodium channels.Proteolytic degradation of amyloid β-protein.

P2860

Q22242329-3242E343-ABDD-4273-A83F-C2C8F66F1A27 Q24654821-500CBC71-1172-4E2C-9F52-4754C7A47ACD Q26825686-F15561DC-D81C-4142-95CF-5B6F7791E7A2 Q27022080-247B591F-6613-47B1-8285-35614E3826F3 Q28238942-EDB1FBD6-21FE-49F4-AA0C-2B2410D4521F Q28307707-9F7E45C5-72C0-453E-83D0-46EB990F7690 Q28504667-FDC0572B-56E2-45CA-B294-7B5D5ADEB6B8 Q28506045-CAA44D6A-7646-4EB9-A597-5F315A3B5245 Q28594541-06FAF0EF-2AE9-42CD-AD96-A2829CE6F95D Q28661055-E1B7B2DD-A305-4C21-84F7-0315D7122BF4 Q30483997-C0CEF539-3C8C-4215-8C7E-BD660A88EBBE Q30486959-2E65F0D4-DC71-4555-9FFE-EEC67E36ADF3 Q30489361-ED3BBDA8-5919-45D4-BAB8-134DEA2AC7D4 Q30544249-D25D0CB2-85BD-4E68-8562-81EDCD74BF66 Q33299077-D6F2E1BB-84C6-44F9-B391-FBB8181F42F5 Q33926960-5772FA9F-431A-477F-ACE0-3E1FA98BF723 Q34389397-15EEBB2B-BACB-4925-8E49-E3BA11CCB34E Q34718255-93C3B511-67E3-4D4B-94A5-9A4075CAFF32 Q35055486-194D640A-0FA8-4076-BE79-242568C852E3 Q35801936-1F2C120B-F4D7-4586-89A8-95F95AA6F77F Q35824582-1FAF859F-3D32-48D9-8908-B2D02A029E8E Q35845240-83D17FAD-6B6C-4C6B-89B9-1B41F4E2ED48 Q35917682-1B36C690-8E3C-41BE-BB9E-56B0079F7A8F Q36012200-DBD1F4CB-C5D5-473D-AB2D-8C19DF479994 Q36231595-9554FE55-791D-46DD-A69C-9258AF1084BD Q36379542-FDCB2BD8-E601-405C-BC35-AE632BFC78C8 Q36418911-3256B9DA-F3FA-407C-A242-B714D3773D6C Q36448521-5FD13821-4EDA-4272-8ADC-62FFDFD48E46 Q36586319-2A59DFFE-D7BA-4BCD-A71E-534DC980437E Q36610341-FF57AD92-EC49-4586-8E24-12723A5A1F7A Q36626440-2EAC396C-E9BB-48BF-AE17-2159DC5291D0 Q36638747-ADAB6A22-F241-4ACD-823A-5B71F0E7E50B Q37105896-2DCF09AF-9A93-4BB7-9D34-9E053E587E5F Q37155515-C86D00F8-BAA6-4EB4-9593-9E764C179B59 Q37174236-B6A46597-1FE9-4F21-9763-E5D2EA5C6A2A Q37234006-95FC8BE0-F33F-4AAC-B790-E7EAEF970C99 Q37355641-13D0D67E-9448-4B4C-B0DC-3F7CE450DBCF Q37458204-E7555B07-74D2-46E0-9D76-E726CB92F7A8 Q37785311-A400D8CE-380E-4588-95F9-0ED12BBFAA25 Q38016899-966A6E06-34FB-48B1-9060-3A234D74C127

P2860

BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo

http://www.wikidata.org/entity/Q36321125

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@ast

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@en

type

label

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@ast

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@en

prefLabel

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@ast

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@en

P1433

Q36321125-D807C82E-51C9-4A96-8044-A3FA56268D90

P1476

Q36321125-660ABC5B-39EE-4BCC-99F3-CD0DE0054B33

P2093

Q36321125-518CD64A-8B41-442E-B4B7-3397875530DE

Q36321125-5195D7D0-6D92-45DB-8E3C-40B7D6FA7099

Q36321125-995D3742-8627-4C84-9EBD-4317E5FB1916

Q36321125-9A9DA5AC-1111-480F-A8E7-8A1030371FD0

Q36321125-AFB2CEB2-44F1-4957-8368-CAFFE99C4254

Q36321125-B2E24F42-F17D-46C2-A957-2D988BB4BD87

P2860

Q36321125-007E6350-5D3C-4AC4-8792-CAF2D9AE0608

Q36321125-08229A93-3476-4A03-BA6A-ED0795F4681A

Q36321125-0C5422A9-F9B3-4703-8838-32C2289FB4C4

Q36321125-0F473A7D-CD27-47CE-8828-4CDB5723F3D8

Q36321125-126E8AC7-DF4E-47B9-B6B1-08175AAC12E5

Q36321125-13BD99B1-E01A-4882-B2FD-E1C9AD53960B

Q36321125-145857D8-8D56-4405-8D5B-A18DB5FBE980

Q36321125-150DB8D7-C396-4581-8BDC-918437555089

Q36321125-1F229135-6B0F-48C1-A253-1FE6D6CA8BF6

Q36321125-2498AC50-BA6A-4AF9-9210-E2BF165E46ED

P304

Q36321125-CC9BEEB4-D9DF-4DB1-B65A-467187386690

P31

Q36321125-A214F89C-6D16-40DD-A189-20D1AC8E871C

P356

Q36321125-D8C64C55-25F7-45C2-8370-8AB581D075A8

P407

Q36321125-07A99250-1E60-4FD2-A735-AB5CBA113FAA

P433

Q36321125-9AE0D4E3-60EC-445D-A6F2-77E3FFACF346

P478

Q36321125-960B5CE0-106C-4986-80C5-75316AF0F6E5

P50

Q36321125-59D308F5-1062-4017-AD80-8D15DAD12932

P577

Q36321125-E3DF8B96-94C2-4366-8353-CA6D70B2EA27

P5875

Q36321125-8416FDE5-477B-4B49-BAEA-5D36FC0B8095

P698

Q36321125-2B11FFD0-91C1-4E0B-9516-BF67B0A6A610

P921

Q36321125-F1427CCE-7FE6-4093-AD75-FFDE0B702926

P932

Q36321125-B444D446-A560-4997-A4EE-DCD1003A1B0E

P356

P1433

Journal of Cell Biology

P1476

BACE overexpression alters the ...... ibits Abeta deposition in vivo

@en

P2093

Bin Zhang

http://www.w3.org/2001/XMLSchema#string

Edward B Lee

http://www.w3.org/2001/XMLSchema#string

Eric A Greenbaum

http://www.w3.org/2001/XMLSchema#string

Kangning Liu

http://www.w3.org/2001/XMLSchema#string

Robert W Doms

http://www.w3.org/2001/XMLSchema#string

Virginia M-Y Lee

http://www.w3.org/2001/XMLSchema#string

P2860

Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation

Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE

Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity

Purification and cloning of amyloid precursor protein beta-secretase from human brain

Correlative Memory Deficits, Abeta Elevation, and Amyloid Plaques in Transgenic Mice

Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path

Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein

P304

291-302

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.200407070

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

168

http://www.w3.org/2001/XMLSchema#string

P50

John Q. Trojanowski

P577

2005-01-10T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8088165

http://www.w3.org/2001/XMLSchema#string

P698

15642747

http://www.w3.org/2001/XMLSchema#string

P921

P932

2171598

http://www.w3.org/2001/XMLSchema#string