Results 11 to 20 of about 8,460 (141)

The γ-secretase complex: from structure to function [PDF]

Frontiers in Cellular Neuroscience, 2014
One of the most critical pathological features of Alzheimer’s disease (AD) is the accumulation of β-amyloid (Aβ) peptides that form extracellular senile plaques in the brain. Aβ is derived from β-amyloid precursor protein through sequential cleavage by β-
Xian eZhang, Yanfang eLi, Huaxi eXu, Huaxi eXu, Yun-Wu eZhang   +4 more
doaj   +3 more sources

Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretase. [PDF]

PLoS ONE, 2011
Regulated intramembrane proteolysis of the amyloid precursor protein (APP) by the protease activities α-, β- and γ-secretase controls the generation of the neurotoxic amyloid β peptide.
Sebastian Hogl, Peer-Hendrik Kuhn, Alessio Colombo, Stefan F Lichtenthaler   +3 more
doaj   +5 more sources

Hair Cell Generation in Cochlear Culture Models Mediated by Novel γ-Secretase Inhibitors [PDF]

Frontiers in Cell and Developmental Biology, 2021
Sensorineural hearing loss is prevalent within society affecting the quality of life of 460 million worldwide. In the majority of cases, this is due to insult or degeneration of mechanosensory hair cells in the cochlea. In adult mammals, hair cell loss is irreversible as sensory cells are not replaced spontaneously.
Silvia T. Erni, Silvia T. Erni, Silvia T. Erni, Silvia T. Erni, John C. Gill, Carlotta Palaferri, Carlotta Palaferri, Carlotta Palaferri, Gabriella Fernandes, Gabriella Fernandes, Gabriella Fernandes, Michelle Buri, Michelle Buri, Michelle Buri, Katherine Lazarides, Denis Grandgirard, Denis Grandgirard, Albert S. B. Edge, Albert S. B. Edge, Albert S. B. Edge, Stephen L. Leib, Stephen L. Leib, Marta Roccio, Marta Roccio, Marta Roccio, Marta Roccio   +25 more
openaire   +5 more sources

Complex regulation of γ-secretase: from obligatory to modulatory subunits [PDF]

Frontiers in Aging Neuroscience, 2015
γ-Secretase is a four subunit, 19-pass transmembrane enzyme that cleaves amyloid precursor protein (APP), catalyzing the formation of amyloid beta (Aβ) peptides that form amyloid plaques, which contribute to Alzheimer's disease (AD) pathogenesis. γ-Secretase also cleaves Notch, among many other type I transmembrane substrates.
Gertsik, Natalya, Chiu, Danica, Li, Yue-Ming   +2 more
openaire   +3 more sources

β-secretase inhibitor; a promising novel therapeutic drug in Alzheimer’s disease [PDF]

Frontiers in Aging Neuroscience, 2014
Alzheimer's disease (AD) and vascular dementia are responsible for up to 90% of dementia cases. According to the World Health Organization (WHO), a staggering number of 35.6 million people are currently diagnosed with dementia. Blocking disease progression or preventing AD altogether is desirable for both social and economic reasons and recently focus ...
Menting, K.W., Claassen, J.A.H.R.
openaire   +3 more sources

APP intracellular domain derived from amyloidogenic β- and γ-secretase cleavage regulates neprilysin expression [PDF]

Frontiers in Aging Neuroscience, 2015
Alzheimer's disease (AD) is characterized by an accumulation of Amyloid-β (Aβ), released by sequential proteolytic processing of the amyloid precursor protein (APP) by β - and γ-secretase. Aβ peptides can aggregate, leading to toxic Aβ oligomers and amyloid plaque formation.
Grimm, Marcus O. W., Mett, Janine, Stahlmann, Christoph P., Grösgen, Sven, Haupenthal, Viola J., Blümel, Tamara, Hundsdörfer, Benjamin, Zimmer, Valerie C., Mylonas, Nadine T., Tanila, Heikki, Müller, Ulrike, Grimm, Heike S., Hartmann, Tobias   +12 more
openaire   +3 more sources

Cholesterol retention in Alzheimer's brain is responsible for high β- and γ-secretase activities and Aβ production

Neurobiology of Disease, 2008
Alzheimer's disease (AD) is characterized by overproduction of Aβ derived from APP cleavage via β- and γ-secretase pathway. Recent evidence has linked altered cholesterol metabolism to AD pathogenesis. In this study, we show that AD brain had significant
Huaqi Xiong, Debbie Callaghan, Aimee Jones, Douglas G. Walker, Lih-Fen Lue, Thomas G. Beach, Lucia I. Sue, John Woulfe, Huaxi Xu, Danica B. Stanimirovic, Wandong Zhang   +10 more
doaj   +1 more source

Axonal amyloid precursor protein and its fragments undergo somatodendritic endocytosis and processing. [PDF]

, 2015
Deposition of potentially neurotoxic Aβ fragments derived from amyloid precursor protein (APP) at synapses may be a key contributor to Alzheimer's disease.
Goldstein, Lawrence SB, Niederst, Emily D, Reyna, Sol M   +2 more
core   +1 more source

Mucin-Type O-Glycosylation Proximal to β-Secretase Cleavage Site Affects APP Processing and Aggregation Fate

Frontiers in Chemistry, 2022
The amyloid-β precursor protein (APP) undergoes proteolysis by β- and γ-secretases to form amyloid-β peptides (Aβ), which is a hallmark of Alzheimer’s disease (AD).
YashoNandini Singh, Deepika Regmi, David Ormaza, Ramya Ayyalasomayajula, Nancy Vela, Gustavo Mundim, Deguo Du, Dmitriy Minond, Maré Cudic   +8 more
doaj   +1 more source

Multi-compartmental modeling of SORLA’s influence on amyloidogenic processing in Alzheimer’s disease [PDF]

, 2012
BACKGROUND: Proteolytic breakdown of the amyloid precursor protein (APP) by secretases is a complex cellular process that results in formation of neurotoxic Aβ peptides, causative of neurodegeneration in Alzheimer’s disease (AD).
Angelyn Lao, Olaf Wolkenhauer, Thomas E Willnow, Vanessa Schmidt, Yvonne Schmitz   +4 more
core   +2 more sources