γ-Secretase in Alzheimer's disease
JY Hur - Experimental & molecular medicine, 2022 - nature.com
Alzheimer's disease (AD) is caused by synaptic and neuronal loss in the brain. One of the
characteristic hallmarks of AD is senile plaques containing amyloid β-peptide (Aβ). Aβ is …
characteristic hallmarks of AD is senile plaques containing amyloid β-peptide (Aβ). Aβ is …
Update on Alzheimer's disease therapy and prevention strategies
WV Graham, A Bonito-Oliva… - Annual review of …, 2017 - annualreviews.org
Alzheimer's disease (AD) is the primary cause of age-related dementia. Effective strategies
to prevent and treat AD remain elusive despite major efforts to understand its basic biology …
to prevent and treat AD remain elusive despite major efforts to understand its basic biology …
Monoamine oxidase B is elevated in Alzheimer disease neurons, is associated with γ-secretase and regulates neuronal amyloid β-peptide levels
S Schedin-Weiss, M Inoue, L Hromadkova… - Alzheimer's Research & …, 2017 - Springer
Background Increased levels of the pathogenic amyloid β-peptide (Aβ), released from its
precursor by the transmembrane protease γ-secretase, are found in Alzheimer disease (AD) …
precursor by the transmembrane protease γ-secretase, are found in Alzheimer disease (AD) …
Mitofusin‐2 knockdown increases ER–mitochondria contact and decreases amyloid β‐peptide production
NS Leal, B Schreiner, CM Pinho… - Journal of cellular …, 2016 - Wiley Online Library
Mitochondria are physically and biochemically in contact with other organelles including the
endoplasmic reticulum (ER). Such contacts are formed between mitochondria‐associated …
endoplasmic reticulum (ER). Such contacts are formed between mitochondria‐associated …
Development and mechanism of γ-secretase modulators for Alzheimer's disease
CJ Crump, DS Johnson, YM Li - Biochemistry, 2013 - ACS Publications
γ-Secretase is an aspartyl intramembranal protease composed of presenilin, Nicastrin,
Aph1, and Pen2 with 19 transmembrane domains. γ-Secretase cleaves the amyloid …
Aph1, and Pen2 with 19 transmembrane domains. γ-Secretase cleaves the amyloid …
The Golgi outpost protein TPPP nucleates microtubules and is critical for myelination
Oligodendrocytes extend elaborate microtubule arbors that contact up to 50 axon segments
per cell, then spiral around myelin sheaths, penetrating from outer to inner layers. However …
per cell, then spiral around myelin sheaths, penetrating from outer to inner layers. However …
Contribution of the Presenilins in the cell biology, structure and function of γ-secretase
A Escamilla-Ayala, R Wouters, R Sannerud… - Seminars in cell & …, 2020 - Elsevier
Abstract γ-Secretase cleavage is essential for many biological processes and its
dysregulation is linked to disease, including cancer and Alzheimer's disease. Therefore …
dysregulation is linked to disease, including cancer and Alzheimer's disease. Therefore …
Golgi outposts nucleate microtubules in cells with specialized shapes
Classically, animal cells nucleate or form new microtubules off the perinuclear centrosome.
In recent years, the Golgi outpost has emerged as a satellite organelle that can function as …
In recent years, the Golgi outpost has emerged as a satellite organelle that can function as …
Poor transcript‐protein correlation in the brain: negatively correlating gene products reveal neuronal polarity as a potential cause
Transcription, translation, and turnover of transcripts and proteins are essential for cellular
function. The contribution of those factors to protein levels is under debate, as transcript …
function. The contribution of those factors to protein levels is under debate, as transcript …
Complex regulation of γ-secretase: from obligatory to modulatory subunits
N Gertsik, D Chiu, YM Li - Frontiers in aging neuroscience, 2015 - frontiersin.org
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 …
precursor protein (APP), catalyzing the formation of amyloid beta (Aβ) peptides that form …