(Q28140262)

2

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K F Lau

3

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S Ackerley

4

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T P Bartnikas

5

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J D Gitlin

6

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C C Miller

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

23 March 2001

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published in

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volume

276

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issue

12

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page(s)

9303-7

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cites work

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Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid [...]

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

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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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The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of 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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PDZ domains: fundamental building blocks in the organization of protein complexes at the plasma membrane

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

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

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Basolateral localization of the Caenorhabditis elegans epidermal growth factor receptor in epithelial cells by the PDZ protein LIN-10.

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

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Association of neuronal calcium channels with modular adaptor proteins

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

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PDZ domains in synapse assembly and signalling

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The copper chaperone for superoxide dismutase

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Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants

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The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase

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Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase

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Crystal structure of the copper chaperone for superoxide dismutase

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Crystal structure of the second domain of the human copper chaperone for superoxide dismutase

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

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Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity

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Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis

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The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain

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Superoxide radical and superoxide dismutases

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase

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The role of copper in neurodegenerative disease

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Metals and neuroscience.

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The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection

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Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase

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Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells. Monoclonal antibody production, isolation, and localization

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Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide

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