Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2
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Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteinsPhosphorylation of LRP1 regulates the interaction with Fe65Alzheimer's disease--a panorama glimpsePhox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPasesSolution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding proteinStructural aspects and physiological consequences of APP/APLP trans-dimerization.Capturing cooperative interactions with the PSI-MI formatThe structural biology of the amyloid precursor protein APP - a complex puzzle reveals its multi-domain architecture.Identification and characterization of a neuronal enriched novel transcript encoding the previously described p60Fe65 isoform.Amyloid precursor protein (APP) mediated regulation of ganglioside homeostasis linking Alzheimer's disease pathology with ganglioside metabolism.Turnover of amyloid precursor protein family members determines their nuclear signaling capabilityIntracellular APP Domain Regulates Serine-Palmitoyl-CoA Transferase Expression and Is Affected in Alzheimer's Disease.Analysis of the overall structure of the multi-domain amyloid precursor protein (APP).A persistent stress response to impeded axonal transport leads to accumulation of amyloid-β in the endoplasmic reticulum, and is a probable cause of sporadic Alzheimer's disease.Coexistence of phases in a protein heterodimerAmyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain.Direct binding of cholesterol to the amyloid precursor protein: An important interaction in lipid-Alzheimer's disease relationships?Physiological functions of APP family proteins.Nuclear localization of amyloid-β precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis.Impact of bilayer lipid composition on the structure and topology of the transmembrane amyloid precursor C99 proteinFe65-PTB2 Dimerization Mimics Fe65-APP Interaction.The Role of APP in Structural Spine Plasticity.Conformational landscape of an amyloid intra-cellular domain and Landau-Ginzburg-Wilson paradigm in protein dynamics.APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells.Is abnormal axonal transport a cause, a contributing factor or a consequence of the neuronal pathology in Alzheimer's disease?APP intracellular domain derived from amyloidogenic β- and γ-secretase cleavage regulates neprilysin expression.Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing.Protein interactions among Fe65, the low-density lipoprotein receptor-related protein, and the amyloid precursor protein.The amyloid precursor protein intracellular domain-fe65 multiprotein complexes: a challenge to the amyloid hypothesis for Alzheimer's disease?Phosphorylation of FE65 at threonine 579 by GSK3β stimulates amyloid precursor protein processing.Purification and aggregation of the amyloid precursor protein intracellular domain.¹H, ¹³C, and ¹⁵N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65.Basal condensation of Numb and Pon complex via phase transition during Drosophila neuroblast asymmetric division.
P2860
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P2860
Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@ast
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@en
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@nl
type
label
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@ast
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@en
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@nl
prefLabel
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@ast
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@en
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@nl
P2860
P50
P356
P1433
P1476
Structure of the intracellular ...... tein in complex with Fe65-PTB2
@en
P2860
P304
P356
10.1038/EMBOR.2008.188
P577
2008-11-01T00:00:00Z