Gleevec inhibits beta-amyloid production but not Notch cleavage
about
Gamma-secretase activating protein is a therapeutic target for Alzheimer's diseasec-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's diseaseWhen loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer diseaseThe Guinea Pig as a Model for Sporadic Alzheimer's Disease (AD): The Impact of Cholesterol Intake on Expression of AD-Related GenesDynamin 1 regulates amyloid generation through modulation of BACE-1Involvement of 5-lipoxygenase in the corticosteroid-dependent amyloid beta formation: in vitro and in vivo evidenceBerberine attenuates axonal transport impairment and axonopathy induced by Calyculin A in N2a cellsRegulation of Alzheimer's disease amyloid-beta formation by casein kinase IMeta-analysis for genome-wide association study identifies multiple variants at the BIN1 locus associated with late-onset Alzheimer's diseaseToward the treatment and prevention of Alzheimer's disease: rational strategies and recent progressSelective amyloid-beta lowering agents.Modulation of gamma-secretase specificity using small molecule allosteric inhibitors.Phenotypic analysis of images of zebrafish treated with Alzheimer's gamma-secretase inhibitors.Targeting Abeta and tau in Alzheimer's disease, an early interim reportSynthesis and positron emission tomography studies of carbon-11-labeled imatinib (Gleevec).The secretases: enzymes with therapeutic potential in Alzheimer disease.Novel CSF biomarkers for Alzheimer's disease and mild cognitive impairmentgamma-secretase activating protein is a therapeutic target for alzheimer 's disease: a path-breaking discovery finally paving way towards therapeutic intervention.Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteasesAssociation of differential gene expression with imatinib mesylate and omacetaxine mepesuccinate toxicity in lymphoblastoid cell lines.Chronic cladribine administration increases amyloid beta peptide generation and plaque burden in mice.The β-secretase-derived C-terminal fragment of βAPP, C99, but not Aβ, is a key contributor to early intraneuronal lesions in triple-transgenic mouse hippocampus.Amyloid precursor protein selective gamma-secretase inhibitors for treatment of Alzheimer's disease.Target deconvolution techniques in modern phenotypic profiling.Comparison of pharmacological modulation of APP metabolism in primary chicken telencephalic neurons and in a human neuroglioma cell line5-lipoxygenase as an endogenous modulator of amyloid β formation in vivo.Striking reduction of amyloid plaque burden in an Alzheimer's mouse model after chronic administration of carmustine.gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site.Role of zinc metallothionein-3 (ZnMt3) in epidermal growth factor (EGF)-induced c-Abl protein activation and actin polymerization in cultured astrocytes.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Regulation of gamma-secretase activating protein by the 5Lipoxygenase: in vitro and in vivo evidenceChemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's DiseaseIdentifying drug-pathway association pairs based on L1L2,1-integrative penalized matrix decomposition.Emerging therapeutics for Alzheimer's disease.The role of γ-secretase activating protein (GSAP) and imatinib in the regulation of γ-secretase activity and amyloid-β generation.Modulators and inhibitors of gamma- and beta-secretases.100 years and counting: prospects for defeating Alzheimer's diseaseNovel therapeutic strategies for the treatment of protein-misfolding diseases.Gamma-secretase inhibition and modulation for Alzheimer's disease.Intramembrane proteolysis
P2860
Q24298408-799FDC6F-F58B-49E2-8B8D-22A4117E4A9FQ24318974-6FA75CE2-9391-4DCF-9F45-EFE6F1DE6520Q24676480-2768113B-CEEF-4FAE-8287-74993BD7DD01Q27315066-B9310838-91E7-49EB-8A68-79A2DBEE5274Q27318742-D56FC9B1-8817-4FBC-9808-F134CF687726Q28476697-915BC67D-7356-4056-BD83-B24E18A67A9BQ28537637-08F70576-08CB-4A4D-AD56-31E7B743F00CQ28577875-55DE9E9E-CBC3-483A-A20F-EABAF91FF8DBQ28742427-3CAFEF87-8EF0-45AE-93FB-E8699B64578EQ30419992-BF75E544-22B9-4DBD-AD89-F38D0950B967Q30855103-4A19DABD-8422-4E3E-9D19-0EE062BEC818Q33515793-31AEAD3F-D782-4A85-9C41-7A80C44B584AQ33543978-F1343A4F-9C1C-4E6D-8618-DBB252DEA26AQ33829008-54A95ABD-FDE5-4816-9022-88562911E222Q33836021-AAAA7807-00FB-466E-86DB-406214CCA6F5Q33887222-DFAAEC7F-322F-423F-B557-E23516B3A1CAQ33894316-0758E4D8-6FB8-4B43-924A-5F998BE65613Q33979489-3DFBBEA9-5E35-445D-858E-C446DC1A9925Q34382868-E7813697-DD40-41ED-81F9-387A14204F00Q34392064-824A0DD9-5B4B-4583-829E-AC3FD8C9826BQ34441015-84CDEA2C-F71C-42EC-BF68-2C6D7B6B7E8EQ34477111-2EF2B317-239C-406F-8AD2-8BE23D83249DQ34543713-A9C865AB-1BEB-466F-85AD-22EAE639ACF1Q34556513-D7023E25-7722-44D9-BA56-797FC9D3A830Q34586941-8F488F6F-599D-4E44-B1A6-C681F53735C3Q34636148-4075F285-49E7-49F3-8017-8B8F55B09855Q34636863-28C5E3F4-74EB-4AB0-98CD-AE4BC7DB5F7EQ34872108-14AE9FD0-C361-4802-A7B4-4ABDD9EB87D3Q35562577-302A5139-3955-40AC-9669-EE1102B5854AQ35658184-638FF818-3BD6-4469-AF8B-88ACEAF7639AQ35745694-4DF22C7C-1C68-4058-9D9F-321EE1FC8895Q36081889-60B0BFD0-8A6F-4538-8E6A-9DDFD5AA3C27Q36408203-C19152EB-A2F9-4B47-8911-5A646230671EQ36492347-5D071409-2747-493B-A657-9616FCA115E7Q36562023-1BCF7811-6490-4AC7-8391-EB8ECDD99A35Q36626443-EEFDFDD2-0970-4934-B283-A4D12C06A603Q36643419-DBABC8B5-7873-449D-A848-399619146751Q36863389-7B32CA9B-F735-48BC-BF52-EDC351BD1F28Q37130650-7ED708CA-798D-4D6F-8728-6311494565A1Q37155734-5756BDCC-E501-4589-8AAF-509F22BFE834
P2860
Gleevec inhibits beta-amyloid production but not Notch cleavage
description
2003 nî lūn-bûn
@nan
2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Gleevec inhibits beta-amyloid production but not Notch cleavage
@ast
Gleevec inhibits beta-amyloid production but not Notch cleavage
@en
Gleevec inhibits beta-amyloid production but not Notch cleavage
@nl
type
label
Gleevec inhibits beta-amyloid production but not Notch cleavage
@ast
Gleevec inhibits beta-amyloid production but not Notch cleavage
@en
Gleevec inhibits beta-amyloid production but not Notch cleavage
@nl
prefLabel
Gleevec inhibits beta-amyloid production but not Notch cleavage
@ast
Gleevec inhibits beta-amyloid production but not Notch cleavage
@en
Gleevec inhibits beta-amyloid production but not Notch cleavage
@nl
P2093
P2860
P356
P1476
Gleevec inhibits beta-amyloid production but not Notch cleavage
@en
P2093
Bayard Clarkson
Darren Veach
Dongming Cai
Stephanie Jean
William G Bornmann
William J Netzer
Yueming Li
P2860
P304
P356
10.1073/PNAS.1534745100
P407
P577
2003-10-14T00:00:00Z