Amyloid β alters vascular CaV1.2 channel spatiotemporal properties
Abstract figure legend Amyloid‐β1‐42 (Aβ1‐42) triggers a male‐specific signalling cascade influencing CaV1.2 spatiotemporal properties in cerebral vascular smooth muscle. The signalling pathway involves NADPH oxidase (NOX)‐derived reactive oxygen species (ROS) activation of protein kinase C (PKC). Aβ1‐42 can also activate protein kinase A (PKA).
Jade L. Taylor +5 more
wiley +1 more source
Expression and function of β-site amyloid precursor protein-cleaving enzyme 2 in vascular endothelium. [PDF]
d'Uscio LV +5 more
europepmc +1 more source
P4‐016: Neuroimaging analysis of human apolipoprotein E targeted replacement mice that overexpress amyloid precursor protein [PDF]
Tammy Dellovade +5 more
openalex +1 more source
Amyloid precursor protein (APP); β-amyloid (Aβ) [PDF]
openaire +1 more source
ABSTRACT Background Proteolytic processing is a fundamental post‐translational modification. Liquid chromatography–tandem mass spectrometry (LC–MS/MS) workflows are powerful for degradomic analyses but inherently sacrifice spatial information, a critical aspect for investigating biological systems such as aberrant extracellular matrix remodeling and ...
Mujia Jenny Li +8 more
wiley +1 more source
Iron-Mediated Overexpression of Amyloid Precursor Protein via Iron Responsive mRNA in Alzheimer's Disease. [PDF]
Khan MA.
europepmc +1 more source
Amyloid precursor protein (APP); β-amyloid (Aβ) [PDF]
openaire +1 more source
MFGM modulated gut microbiota accompanied by the increased serum RVD1 and AEA levels, which subsequently regulated the miRNA profile. This modulation alleviated neuroinflammation via suppressing the NLRP3 inflammasome signaling and microglial activation, thereby attenuating AD‐related cognitive impairment both in vivo and in vitro.
Han Gong +4 more
wiley +1 more source
Evaluation of the Alterations in Central Cholinergic Neurotransmission in Aging and Amyloid Precursor Protein Knock-In Mice. [PDF]
Nagai-Arakawa I +14 more
europepmc +1 more source
CDC42‐Effector Proteins Regulate Higher Order Structure of Septins Required for CNS Myelin Integrity
CDC42‐effector proteins 1/2 are present in CNS myelin. They facilitate the higher order structure of myelin septin filaments. Their loss impairs septin‐dependent scaffolding of myelin. Myelin outfoldings do not cause secondary neuropathology per se. ABSTRACT The regular structure of CNS myelin requires specialized structural proteins, including septin ...
Sophie Hümmert +14 more
wiley +1 more source

