A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function.
about
Amyloid precursor protein and amyloid precursor-like protein 2 in cancerThe multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foesFE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.Structural aspects and physiological consequences of APP/APLP trans-dimerization.APP 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 functionsAPP Is a Context-Sensitive Regulator of the Hippocampal Presynaptic Active ZoneAmyloid precursor protein (APP) regulates synaptic structure and functionA new molecular explanation for age-related neurodegeneration: the Tyr682 residue of amyloid precursor proteinKnockdown of amyloid precursor protein in zebrafish causes defects in motor axon outgrowth.Deletion of the amyloid precursor-like protein 2 (APLP2) does not affect hippocampal neuron morphology or function.Neddylation dysfunction in Alzheimer's disease.The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function.Turnover of amyloid precursor protein family members determines their nuclear signaling capabilityY682G Mutation of Amyloid Precursor Protein Promotes Endo-Lysosomal Dysfunction by Disrupting APP-SorLA Interaction.APP is phosphorylated by TrkA and regulates NGF/TrkA signaling.APP intracellular domain acts as a transcriptional regulator of miR-663 suppressing neuronal differentiation.Tyr682 in the Aβ-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance.APP and APLP2 interact with the synaptic release machinery and facilitate transmitter release at hippocampal synapses.Neprilysin and Aβ Clearance: Impact of the APP Intracellular Domain in NEP Regulation and Implications in Alzheimer's DiseaseBiology and pathophysiology of the amyloid precursor protein.APP physiological and pathophysiological functions: insights from animal models.Functions of the APP gene family in the nervous system: insights from mouse models.Physiological functions of APP family proteins.Redundancy and divergence in the amyloid precursor protein family.Not just amyloid: physiological functions of the amyloid precursor protein family.APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.Amyloid Precursor Protein (APP) May Act as a Substrate and a Recognition Unit for CRL4CRBN and Stub1 E3 Ligases Facilitating Ubiquitination of Proteins Involved in Presynaptic Functions and Neurodegeneration
P2860
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P2860
A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A single tyrosine residue in t ...... al for developmental function.
@ast
A single tyrosine residue in t ...... al for developmental function.
@en
A single tyrosine residue in t ...... al for developmental function.
@nl
type
label
A single tyrosine residue in t ...... al for developmental function.
@ast
A single tyrosine residue in t ...... al for developmental function.
@en
A single tyrosine residue in t ...... al for developmental function.
@nl
prefLabel
A single tyrosine residue in t ...... al for developmental function.
@ast
A single tyrosine residue in t ...... al for developmental function.
@en
A single tyrosine residue in t ...... al for developmental function.
@nl
P2093
P2860
P356
P1476
A single tyrosine residue in t ...... ial for developmental function
@en
P2093
Alessia P M Barbagallo
Zilai Wang
P2860
P304
P356
10.1074/JBC.C111.219873
P407
P577
2011-01-25T00:00:00Z