Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor? - Wikidata - awgldk - TriplyDB

Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?

Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?

http://www.wikidata.org/entity/Q36948254

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Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment Molecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms Structural and dynamic study of the transmembrane domain of the amyloid precursor protein The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer Implications of Human Transient Receptor Potential Melastatin 8 (TRPM8) Channel Gating from Menthol Binding Studies of the Sensing Domain NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.The quiet renaissance of protein nuclear magnetic resonance.Enrichment of cholesterol in microdissected Alzheimer's disease senile plaques as assessed by mass spectrometry.ACAT1 gene ablation increases 24(S)-hydroxycholesterol content in the brain and ameliorates amyloid pathology in mice with AD.Structural heterogeneity in transmembrane amyloid precursor protein homodimer is a consequence of environmental selection.Structural basis of transmembrane domain interactions in integrin signaling.Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's disease Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases.Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.Exploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micelles Structural basis for the geometry-driven localization of a small protein.Solution NMR approaches for establishing specificity of weak heterodimerization of membrane proteins Notch Transmembrane Domain: Secondary Structure and Topology.Membrane-microdomain localization of amyloid β-precursor protein (APP) C-terminal fragments is regulated by phosphorylation of the cytoplasmic Thr668 residue.ApoE4 upregulates the activity of mitochondria-associated ER membranes.Topologically Diverse Human Membrane Proteins Partition to Liquid-Disordered Domains in Phase-Separated Lipid Vesicles.Biochemical identification of a linear cholesterol-binding domain within Alzheimer's β amyloid peptide Amyloid precursor protein controls cholesterol turnover needed for neuronal activity.Links between copper and cholesterol in Alzheimer's disease.Embedding Aβ42 in heterogeneous membranes depends on cholesterol asymmetries Toward structural elucidation of the gamma-secretase complex.Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretase Transmembrane fragment structures of amyloid precursor protein depend on membrane surface curvature.Perturbations of the straight transmembrane α-helical structure of the amyloid precursor protein affect its processing by γ-secretase.Conformational changes induced by the A21G Flemish mutation in the amyloid precursor protein lead to increased Aβ production.Direct binding of cholesterol to the amyloid precursor protein: An important interaction in lipid-Alzheimer's disease relationships?Structural and functional alterations in amyloid-β precursor protein induced by amyloid-β peptides.Membrane and surface interactions of Alzheimer's Aβ peptide--insights into the mechanism of cytotoxicity.Relationships between the amyloid precursor protein and its various proteolytic fragments and neuronal systems.Cholesterol as a co-solvent and a ligand for membrane proteins.Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.

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Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?

http://www.wikidata.org/entity/Q36948254

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Structural studies of the tran ...... ction as a cholesterol sensor?

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Andrew J Beel

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Arina Hadziselimovic

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Bing Jap

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Charles K Mobley

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Charles R Sanders

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Fang Tian

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Hak Jun Kim

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James H Prestegard

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P2860

The cholesterol transporter ABCG1 modulates the subcellular distribution and proteolytic processing of beta-amyloid precursor protein

Purification and characterization of the human gamma-secretase complex

The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein

The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production

Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein.

Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores.

Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases

Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1

Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts

Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein

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transmembrane protein

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2572687

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