Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
about
Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor proteinBinding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavageThe amyloid-beta precursor protein: integrating structure with biological functionStructure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expressionProteolytic processing of Alzheimer's β-amyloid precursor proteinAPP is cleaved by Bace1 in pre-synaptic vesicles and establishes a pre-synaptic interactome, via its intracellular domain, with molecular complexes that regulate pre-synaptic vesicles functionsInteraction of Mint2 with TrkA is involved in regulation of nerve growth factor-induced neurite outgrowthFast anterograde transport of herpes simplex virus: role for the amyloid precursor protein of alzheimer's disease.Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays.A new molecular explanation for age-related neurodegeneration: the Tyr682 residue of amyloid precursor proteinTyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo.Dynamic changes of the phosphoproteome in postmortem mouse brains.EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APPAmyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner.Novel adaptors of amyloid precursor protein intracellular domain and their functional implications.Rapamycin promotes beta-amyloid production via ADAM-10 inhibition.An intracellular threonine of amyloid-β precursor protein mediates synaptic plasticity deficits and memory loss.A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function.The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function.JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease.Y682G Mutation of Amyloid Precursor Protein Promotes Endo-Lysosomal Dysfunction by Disrupting APP-SorLA Interaction.APP is phosphorylated by TrkA and regulates NGF/TrkA signaling.All in the Family: How the APPs Regulate NeurogenesisAdaptor protein 2-mediated endocytosis of the β-secretase BACE1 is dispensable for amyloid precursor protein processing.Tyr682 in the Aβ-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance.Nerve growth factor, neural stem cells and Alzheimer's disease.Cathepsin Inhibition Prevents Autophagic Protein Turnover and Downregulates Insulin Growth Factor-1 Receptor-Mediated Signaling in NeuroblastomaAPP Receptor? To Be or Not To Be.Amyloid precursor protein and presenilin involvement in cell signaling.Substrate specificity of gamma-secretase and other intramembrane proteases.The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains.Amyloid precursor family proteins are expressed by thymic and lymph node stromal cells but are not required for lymphocyte development.Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents.APP physiological and pathophysiological functions: insights from animal models.Neurodegeneration in Alzheimer disease: role of amyloid precursor protein and presenilin 1 intracellular signaling.Protein Phosphorylation is a Key Mechanism in Alzheimer's Disease.Activation of amyloid precursor protein processing by growth factors is dependent on Ras GTPase activity.Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1.
P2860
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P248
Q24305128-438339A4-6392-4E5C-B918-22C622A94F70Q24312009-E44C93C8-CC9D-48B5-88D1-7C445B9C9BFBQ24540102-039320C6-2072-4B14-BE9D-55F96B042FEBQ27652388-F47E8593-30C4-4D8F-8631-EBFE46C5105DQ28207751-DD0BEB37-1382-4EAF-8310-3892E6E96BBAQ28254104-A5547C63-BA4D-4BA7-A195-B4DECD1EA0C6Q28543167-1686E732-ED24-461A-BA40-CEADC0EEC367Q28580671-8A20A57C-02C1-434C-B6E9-438FE58C21EDQ30538684-25FD5488-D92A-4407-B8E7-91C5F2DB550FQ33257954-D970837A-4A68-4130-8AB0-ECF770E6E974Q33661653-16BFEB60-1387-4670-A139-420AFF81C4D6Q33754509-094C639B-EFCB-4F0C-B302-E2D1FE0E75E9Q33952409-8EB4C580-BB1A-4134-87E9-C2AF63923BF2Q34311248-D1BB117F-EB57-471A-8D53-1F6AB3C0597EQ34345797-D7DB63D7-EA81-47DD-8BFB-78108DD7FBF3Q34453199-39BC2A91-C546-40A4-83DE-2705417FB508Q34576437-0859E7E8-E0DD-47A1-A320-4466D3D13447Q34603033-6BDAFD3F-BD2F-4ED3-BBE4-31D31DECE3CAQ34685168-10E9FEC8-29C6-4A23-A33F-3A0B73CD8177Q34708261-DA2788B7-043E-4317-A7E4-C719B49FB253Q34761715-02840475-1C64-4C5E-9523-D77F37ECFEF6Q34988301-AD9ABD95-FEF2-49E5-83FC-0F22101D2CB1Q35297339-992C1A30-A2AF-489A-9AA5-97790D0C0910Q35870089-7BDC3D71-1570-49D1-956B-9C1732F74BF7Q36005686-2D750659-1CF7-4D06-BC56-55ACFA3DDE10Q36030499-038020A8-F5FA-44EE-8038-746F3539C7FFQ36405899-FF318E8E-D415-46D1-9F34-3AEB953E0524Q36529555-FE5ACB61-1174-4AEA-8AEE-035EE4E62931Q36559668-C09825AE-25D1-4C8F-9F4C-723A05396852Q36840033-E11D2748-78F6-4801-8697-DBE583E740E7Q36863026-9F6E4403-DF9A-4903-BB74-EA3C90248020Q37073568-B2428FFA-177D-4596-BB26-EF190FA3C9FCQ37295364-D0180FF6-6B07-4490-8FEF-11CB0CC103F8Q37360497-352FC799-8049-4823-96F1-F7608F3F1120Q37614648-AE69D21F-7629-4766-80E5-DA7A0F22C9D4Q37902514-81852B72-98AA-447D-8611-15D5F6A2F32BQ38002023-A4A7E975-7773-462F-A57F-68178FA0CC52Q39319453-F1DE2592-8A49-4466-A2DC-984CED66C630Q39619549-DACD66E8-0D77-4DCE-BDE3-1CC52CEC9080Q39796602-A6166E04-5E30-4C0B-8A79-516C949FD7E6
P2860
Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@ast
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en-gb
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@nl
type
label
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@ast
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en-gb
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@nl
prefLabel
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@ast
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en-gb
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@nl
P2093
P921
P356
P1476
Tyrosine phosphorylation of th ...... promotes interaction with Shc
@en
P2093
Giuliana Pelicci
Philip E Tarr
Pier Giuseppe Pelicci
Roberta Roncarati
P304
16798-16804
P356
10.1074/JBC.M110286200
P407
P577
2002-03-04T00:00:00Z