Results 141 to 150 of about 86,542 (275)

Nontranscriptional Role of Hif-1α in Activation of γ-Secretase and Notch Signaling in Breast Cancer

open access: yesCell Reports, 2014
γ-Secretase is composed of four proteins that are obligatory for protease activity: presenilin, nicastrin, Aph1, and Pen-2. Despite the progress toward understanding the function of these individual subunits, there is no information available pertaining ...
Jennifer C. Villa   +11 more
doaj   +1 more source

Sampling the conformational space of the catalytic subunit of human γ-secretase

open access: yesbioRxiv, 2015
Human γ-secretase is an intra-membrane protease that cleaves many different substrates. Aberrant cleavage of Notch is implicated in cancer, while abnormalities in cutting amyloid precursor protein lead to Alzheimer’s disease.
X. Bai   +4 more
semanticscholar   +1 more source

γ-Secretase promotes membrane insertion of the human papillomavirus L2 capsid protein during virus infection

open access: yesJournal of Cell Biology, 2018
Despite their importance as human pathogens, entry of human papillomaviruses (HPVs) into cells is poorly understood. The transmembrane protease &ggr;-secretase executes a crucial function during the early stages of HPV infection, but the role of &ggr ...
Takamasa Inoue   +6 more
semanticscholar   +1 more source

Γ-secretase components as predictors of breast cancer outcome.

open access: yesPLoS ONE, 2013
γ-secretase is a large ubiquitously expressed protease complex composed of four core subunits: presenilin, Aph1, PEN-2, and nicastrin. The function of γ-secretase in the cells is to proteolytically cleave various proteins within their transmembrane ...
Hanna M Peltonen   +5 more
doaj   +1 more source

The trans-Golgi network is a major site for α-secretase processing of amyloid precursor protein in primary neurons

open access: yesJournal of Biological Chemistry, 2018
Amyloid precursor protein (APP) is processed along the amyloidogenic pathway by the β-secretase, BACE1, generating β-amyloid (Aβ), or along the nonamyloidogenic pathway by α-secretase, precluding Aβ production. The plasma membrane is considered the major
J. Z. A. Tan, P. Gleeson
semanticscholar   +1 more source

The γ-secretase complex: from structure to function

open access: yesFrontiers 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   +4 more
doaj   +1 more source

Identification of potent inhibitors for -secretase through structure based virtual screening and molecular dynamics simulations [PDF]

open access: yesJournal of Clinical and Scientific Research, 2013
Background: Alzheimer's disease (AD) is a neurodegenerative disorder in elderly persons aged above 65 years. The cleavage of amyloid precursor protein (APP) by -secretase generates peptide fragment A42, the main cause of memory and cognitive defects ...
A. Mobeen   +5 more
doaj  

Steroids as γ‐secretase modulators

open access: yesThe FASEB Journal, 2013
Aggregation and accumulation of Aβ 42 play an initiating role in Alzheimer's disease (AD); thus, selective lowering of Aβ 42 by γ‐secretase modulators (GSMs) remains a promising approach to AD therapy.
Joo In, Jung   +7 more
openaire   +3 more sources

Plasmalogens Inhibit APP Processing by Directly Affecting γ-Secretase Activity in Alzheimer’s Disease

open access: yesThe Scientific World Journal, 2012
Lipids play an important role as risk or protective factors in Alzheimer’s disease (AD). Previously it has been shown that plasmalogens, the major brain phospholipids, are altered in AD.
Tatjana L. Rothhaar   +9 more
doaj   +1 more source

Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE.

open access: yesScience, 1999
R. Vassar   +23 more
semanticscholar   +1 more source

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