about
Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis.Genetic inhibition of phosphorylation of the translation initiation factor eIF2α does not block Aβ-dependent elevation of BACE1 and APP levels or reduce amyloid pathology in a mouse model of Alzheimer's disease.Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer's diseaseAβ reduction in BACE1 heterozygous null 5XFAD mice is associated with transgenic APP levelIntraneuronal Aβ detection in 5xFAD mice by a new Aβ-specific antibody.β-Site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1)-deficient mice exhibit a close homolog of L1 (CHL1) loss-of-function phenotype involving axon guidance defectsAPOE4-specific changes in Aβ accumulation in a new transgenic mouse model of Alzheimer disease.The Alzheimer's β-secretase BACE1 localizes to normal presynaptic terminals and to dystrophic presynaptic terminals surrounding amyloid plaques.Specificity of Toll-Like Receptor 2 and Dectin-1 Signaling in CNS Macrophages.Erratum to: The Alzheimer’s β-secretase BACE1 localizes to normal presynaptic terminals and to dystrophic presynaptic terminals surrounding amyloid plaques
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
William A Eimer
@ast
William A Eimer
@en
William A Eimer
@es
William A Eimer
@nl
William A Eimer
@sl
type
label
William A Eimer
@ast
William A Eimer
@en
William A Eimer
@es
William A Eimer
@nl
William A Eimer
@sl
prefLabel
William A Eimer
@ast
William A Eimer
@en
William A Eimer
@es
William A Eimer
@nl
William A Eimer
@sl
P106
P21
P31
P496
0000-0003-1067-9339