(Q28218036)

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Vlad Marinescu

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Michelle L Steinhilb

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James R Gaut

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Edward L Stuenkel

Journal of Biological Chemistry

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language of work or name

English

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publication date

26 July 2002

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published in

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volume

277

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issue

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page(s)

27021-8

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cites work

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides.

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The discrepancy between presenilin subcellular localization and gamma-secretase processing of amyloid precursor protein

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The role of APP processing and trafficking pathways in the formation of amyloid beta-protein

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The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

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The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein

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The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system

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Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein

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Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain

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The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion

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Regulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding protein

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X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion

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Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein

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LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia

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The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells

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Mints as adaptors. Direct binding to neurexins and recruitment of munc18

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Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport

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Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting

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A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain

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Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease

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Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein

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Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein

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PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein

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Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains.

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X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains

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Mints, Munc18-interacting Proteins in Synaptic Vesicle Exocytosis

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Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2

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Neuronal expression of mint1 and mint2, novel multimodular proteins, in adult murine brain

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The protease inhibitor, MG132, blocks maturation of the amyloid precursor protein Swedish mutant preventing cleavage by beta-Secretase

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X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein

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Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane

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Protease inhibitors divert amyloid precursor protein to the secretory pathway

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Sec1p binds to SNARE complexes and concentrates at sites of secretion

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42

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