Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.
about
Structural and dynamic study of the transmembrane domain of the amyloid precursor proteinFamilial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage siteNeuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers.Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GxxxG motif.Structural heterogeneity in transmembrane amyloid precursor protein homodimer is a consequence of environmental selection.Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's diseaseLowering of amyloid beta peptide production with a small molecule inhibitor of amyloid-β precursor protein dimerizationEvidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.Molecular determinants and thermodynamics of the amyloid precursor protein transmembrane domain implicated in Alzheimer's disease.A subset of membrane-altering agents and γ-secretase modulators provoke nonsubstrate cleavage by rhomboid proteasesSolution NMR approaches for establishing specificity of weak heterodimerization of membrane proteinsN-cadherin enhances APP dimerization at the extracellular domain and modulates Aβ production.Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing.Homodimerization of amyloid precursor protein at the plasma membrane: a homoFRET study by time-resolved fluorescence anisotropy imagingExtension of a protein docking algorithm to membranes and applications to amyloid precursor protein dimerization.The effects of transmembrane sequence and dimerization on cleavage of the p75 neurotrophin receptor by γ-secretaseStructural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?A helix-to-coil transition at the epsilon-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis.Toward structural elucidation of the gamma-secretase complex.Interaction and conformational dynamics of membrane-spanning protein helices.Direct binding of cholesterol to the amyloid precursor protein: An important interaction in lipid-Alzheimer's disease relationships?Lessons from genome-wide association studies findings in Alzheimer's disease.Latest developments in experimental and computational approaches to characterize protein-lipid interactions.The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.TMP21 transmembrane domain regulates gamma-secretase cleavage.Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites.The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase.Comparable dimerization found in wildtype and familial Alzheimer's disease amyloid precursor protein mutants.APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms.Competition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.Dominant negative effect of the loss-of-function γ-secretase mutants on the wild-type enzyme through heterooligomerization.β-Sheet Structure within the Extracellular Domain of C99 Regulates Amyloidogenic Processing.Coupled Transmembrane Substrate Docking and Helical Unwinding in Intramembrane Proteolysis of Amyloid Precursor Protein
P2860
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P2860
Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@ast
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@en
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@nl
type
label
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@ast
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@en
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@nl
prefLabel
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@ast
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@en
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@nl
P2093
P2860
P356
P1433
P1476
Dimerization of the transmembr ...... l Alzheimer's disease mutants.
@en
P2093
Avijit Chakrabartty
James U Bowie
Joanne McLaurin
Paul E Fraser
Paul M Gorman
Roman A Melnyk
P2860
P2888
P356
10.1186/1471-2202-9-17
P50
P577
2008-01-30T00:00:00Z
P5875
P6179
1031615925