338 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

    Andisheh Abedini et al.
    Toxic IAPP intermediates have some molecular features that are similar to, and others that are distinct from, toxic species reported for other amyloidogenic polypeptides.
    1. Neuroscience

    APP modulates KCC2 expression and function in hippocampal GABAergic inhibition

    Ming Chen et al.
    APP interacts with KCC2 to limit the latter from tyrosine-phosphorylation and ubiquitination and thus subsequent degradation, revealing a novel molecular pathway in which APP regulates GABAergic signaling and thus inhibition in the hippocampus.
    1. Neuroscience

    Loss of presenilin function is associated with a selective gain of APP function

    Carole Deyts et al.
    Amyloid precursor protein expression and accumulation of its intracellular fragment are required for exuberant neurite outgrowth associated with pathological presenilin 1 loss-of-function mutations before the emergence of amyloid burden in mice.
    1. Neuroscience

    LTP and memory impairment caused by extracellular Aβ and Tau oligomers is APP-dependent

    Daniela Puzzo et al.
    Oligomeric Amyloid-β and Tau, two proteins involved in Alzheimer's disease pathogenesis, require Amyloid Precursor Protein to enter neurons and exert their detrimental effect on synaptic plasticity and memory.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate

    Diana C Rodriguez Camargo et al.
    The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.
    1. Neuroscience

    APP and APLP2 interact with the synaptic release machinery and facilitate transmitter release at hippocampal synapses

    Tomas Fanutza et al.
    A naturally occurring intracellular peptide, derived by processing the Alzheimer's protein APP, reduces synaptic transmission by acting as a dominant negative of APP.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity

    Pascal Krotee et al.
    Atomic structures of hIAPP fibrillar segments, determined using the cryo electron microscopy method MicroED, reveal that strong, stable intermolecular interactions are important features of cytotoxic amyloid proteins.
    1. Neuroscience

    Genomic mosaicism with increased amyloid precursor protein (APP) gene copy number in single neurons from sporadic Alzheimer's disease brains

    Diane M Bushman et al.
    Somatically derived genomic mosaicism in the form of increased DNA content and APP copy number in single neurons plausibly has a function in sporadic Alzheimer’s disease and points to functions for single-neuron gene copy number changes.
    1. Neuroscience

    Physiological and pathophysiological control of synaptic GluN2B-NMDA receptors by the C-terminal domain of amyloid precursor protein

    Paula A Pousinha et al.
    The APP intracellular domain (AICD) physiologically regulates synaptic GluN2B-containing NMDA receptor current, a process that could contribute to pathological Alzheimer's disease-related synaptic failure upon increase of AICD levels in adult neurons.
    1. Developmental Biology
    2. Neuroscience

    APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice

    Hong Y Choi et al.
    Proteins implicated in Alzheimer’s disease, including amyloid precursor protein and ApoE receptors, interact with each other and with a signalling molecule called agrin to influence the development of the neuromuscular junction.

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