JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65
about
Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor proteinCD74 interacts with APP and suppresses the production of AbetaModulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold proteinBRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2An X11alpha/FSBP complex represses transcription of the GSK3beta gene promoterThe amyloid-beta precursor protein: integrating structure with biological functionAPP 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 functionsDeletion of the γ-secretase subunits Aph1B/C impairs memory and worsens the deficits of knock-in mice modeling the Alzheimer-like familial Danish dementiaTyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo.beta-Secretase cleavage is not required for generation of the intracellular C-terminal domain of the amyloid precursor family of proteins.Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner.PAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.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.Turnover of amyloid precursor protein family members determines their nuclear signaling capabilityThe diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases.Lineage-specific and ubiquitous biological roles of the mammalian transcription factor LSFTyr682 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.APP Receptor? To Be or Not To Be.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.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.The physiology of the β-amyloid precursor protein intracellular domain AICD.Facilitation of stress-induced phosphorylation of beta-amyloid precursor protein family members by X11-like/Mint2 protein.Fe65 is not involved in the platelet-derived growth factor-induced processing of Alzheimer's amyloid precursor protein, which activates its caspase-directed cleavage.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 NeurodegenerationAmyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1.Amyloid beta protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1.Secretion of long Abeta-related peptides processed at epsilon-cleavage site is dependent on the alpha-secretase pre-cutting.Role of 14-3-3gamma in FE65-dependent gene transactivation mediated by the amyloid beta-protein precursor cytoplasmic fragment.APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.APLP1 promotes dFoxO-dependent cell death in Drosophila.
P2860
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P2860
JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին 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
JNK-interacting protein-1 prom ...... nistically different than Fe65
@ast
JNK-interacting protein-1 prom ...... nistically different than Fe65
@en
JNK-interacting protein-1 prom ...... nistically different than Fe65
@nl
type
label
JNK-interacting protein-1 prom ...... nistically different than Fe65
@ast
JNK-interacting protein-1 prom ...... nistically different than Fe65
@en
JNK-interacting protein-1 prom ...... nistically different than Fe65
@nl
prefLabel
JNK-interacting protein-1 prom ...... nistically different than Fe65
@ast
JNK-interacting protein-1 prom ...... nistically different than Fe65
@en
JNK-interacting protein-1 prom ...... nistically different than Fe65
@nl
P2860
P50
P356
P1476
JNK-interacting protein-1 prom ...... nistically different than Fe65
@en
P2093
Shuji Matsuda
P2860
P304
P356
10.1073/PNAS.0437908100
P407
P577
2003-01-31T00:00:00Z