The regulation of amyloid precursor protein metabolism by cholinergic mechanisms and neurotrophin receptor signaling
S Roßner, U Ueberham, R Schliebs… - Progress in …, 1998 - Elsevier
The increased expression and/or abnormal processing of the amyloid precursor protein
(APP) is associated with the formation of amyloid plaques and cerebrovascular amyloid …
(APP) is associated with the formation of amyloid plaques and cerebrovascular amyloid …
Proteolytic processing of Alzheimer's βamyloid precursor protein
H Zhang, Q Ma, Y Zhang, H Xu - Journal of Neurochemistry …, 2012 - Wiley Online Library
J. Neurochem.(2012) 120 (Suppl. 1), 9–21. Abstract βAmyloid precursor protein (APP) is a
critical factor in the pathogenesis of Alzheimer's disease (AD). APP undergoes post …
critical factor in the pathogenesis of Alzheimer's disease (AD). APP undergoes post …
Physiology and pharmacology of amyloid precursor protein
Y Cho, HG Bae, E Okun, TV Arumugam… - Pharmacology & …, 2022 - Elsevier
Amyloid precursor protein (APP) is an evolutionarily conserved transmembrane protein and
a well-characterized precursor protein of amyloid-beta (Aβ) peptides, which accumulate in …
a well-characterized precursor protein of amyloid-beta (Aβ) peptides, which accumulate in …
Amyloid precursor protein processing and Alzheimer's disease
RJ O'brien, PC Wong - Annual review of neuroscience, 2011 - annualreviews.org
Alzheimer's disease (AD), the leading cause of dementia worldwide, is characterized by the
accumulation of the β-amyloid peptide (Aβ) within the brain along with hyperphosphorylated …
accumulation of the β-amyloid peptide (Aβ) within the brain along with hyperphosphorylated …
β-Amyloid precursor protein metabolism: focus on the functions and degradation of its intracellular domain
Alzheimer's disease (AD) is a neurodegenerative disorder that represents the most common
type of dementia in the elderly. One of the hallmarks of this disease is a progressive …
type of dementia in the elderly. One of the hallmarks of this disease is a progressive …
[HTML][HTML] APP processing in Alzheimer's disease
Y Zhang, R Thompson, H Zhang, H Xu - Molecular brain, 2011 - Springer
An important pathological feature of Alzheimer's disease (AD) is the presence of
extracellular senile plaques in the brain. Senile plaques are composed of aggregations of …
extracellular senile plaques in the brain. Senile plaques are composed of aggregations of …
Role of neurotransmission in the regulation of amyloid β-protein precursor processing
RM Nitsch, JH Growdon - Biochemical pharmacology, 1994 - Elsevier
Because of the central place of amyloid in the histopathology of Alzheimer's disease (AD*),
current research seeks to determine the proteolytic mechanisms involved in the processing …
current research seeks to determine the proteolytic mechanisms involved in the processing …
Amyloidogenic processing of β-amyloid precursor protein in intracellular compartments
KS Vetrivel, G Thinakaran - Neurology, 2006 - AAN Enterprises
Trafficking and proteolytic processing of amyloid precursor protein (APP) have been the
focus of numerous investigations in the past two decades, since the identification of Aβ as …
focus of numerous investigations in the past two decades, since the identification of Aβ as …
In Vivo Regulation of Amyloid Precursor Protein Secretion in Rat Neocortex by Cholinergic Activity
S Rossner, U Ueberham, J Yu, L Kirazov… - European Journal of …, 1997 - Wiley Online Library
The proteolytic cleavage of the amyloid precursor protein (APP) has been shown to be
modulated through specific muscarinic receptor activation in vitro in both transfected cell …
modulated through specific muscarinic receptor activation in vitro in both transfected cell …
Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
PR Turner, K O'Connor, WP Tate, WC Abraham - Progress in neurobiology, 2003 - Elsevier
Amyloid-β precursor protein (APP) is a membrane-spanning protein with a large
extracellular domain and a much smaller intracellular domain. It is the source of the amyloid …
extracellular domain and a much smaller intracellular domain. It is the source of the amyloid …