Results 41 to 50 of about 27,905 (224)

Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons [PDF]

, 2016
Background: The protease BACE1 (beta-site APP cleaving enzyme) is a major drug target in Alzheimer’s disease. However, BACE1 therapeutic inhibition may cause unwanted adverse effects due to its additional functions in the nervous system, such as in ...
De Strooper, B, Feederle, R, Gunnersen, JM, Hrupka, BJ, Kuhn, P-H, Levasseur, MD, Lichtenthaler, SF, Mueller, SA, Munro, KM, Pigoni, M, Takeshima, H, Voytyuk, I, Wanngren, J   +12 more
core   +5 more sources

Role of cholesterol in substrate recognition by $$\gamma$$ γ -secretase

Scientific Reports, 2021
$$\gamma$$ γ -Secretase is an enzyme known to cleave multiple substrates within their transmembrane domains, with the amyloid precursor protein of Alzheimer’s Disease among the most prominent examples.
Łukasz Nierzwicki, Michał Olewniczak, Paweł Chodnicki, Jacek Czub   +3 more
doaj   +1 more source

Selective amyloid-β lowering agents [PDF]

, 2012
The amyloid-\(\beta\) peptide (A\(\beta\)), implicated in the pathogenesis of Alzheimer's disease (AD), is produced through sequential proteolysis of the A\(\beta\) precursor protein (APP) by \(\beta\)- and \(\gamma\)-secretases. Thus, blocking either of
Michael S Wolfe, D Beher, DR Howlett, H Cai, Y Luo, M Willem, L Hong, AK Ghosh, MS Wolfe, R Kopan, GH Searfoss, GT Wong, S Weggen, S Weggen, Y Zhou, T Sato, TL Kukar, WJ Netzer, PC Fraering, P Bakshi   +19 more
core   +1 more source

Discovery of biphenylacetamide-derived inhibitors of BACE1 using de novo structure-based molecular design [PDF]

, 2013
β-Secretase (BACE1), the enzyme responsible for the first and rate-limiting step in the production of amyloid-β peptides, is an attractive target for the treatment of Alzheimer’s disease.
A. Peter Johnson, Aoyama T., Baret P., Baxter E. W., Bedford R. B., Besong G. E., Callaway E., Cesar J., Cole D. C., Colin W. G. Fishwick, Coutts R. T., Davies M., Eder J., Eva Casas-Arce, Ghosh A. K., Ghosh A. K., Gillet V. J., Goodyer C. L. M., Guengerich F. P., Hardy J. A., Hong L., Hooper N. M., Huang D. Z., Huang D. Z., Huang W. H., Hussain I., James Chadwick, Ju Y. H., Katherine A. B. Kellett, Law J. M. S., Lin X. L., Mancini F., Mok N. Y., N. Yi Mok, Nigel M. Hooper, Parvathy S., Robichaud J., Selkoe D. J., Serafin B., Sinha S., Sun X. L., Vassar R., Woon E. C. Y., Xu W. J.   +43 more
core   +1 more source

Alzheimer's Beta‐Secretase in Health and Disease

The FASEB Journal, 2008
The neuritic plaques of Alzheimer's Disease (AD) are comprised of extracellular deposits of amyloid‐β (Aβ) peptides surrounded by dystrophic neurites, reactive astrocytes, and microglia. The Aβ peptides are derived from the sequential processing of amyloid‐β precursor protein (APP) by the activities of two enzymes termed, β‐ and γ ...
Mohamed Farah, Philip C Wong
openaire   +1 more source

Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP

Frontiers in Aging Neuroscience, 2019
Processing of amyloid beta precursor protein (APP) into amyloid-beta peptide (Aβ) by β-secretase and γ-secretase complex is at the heart of the pathogenesis of Alzheimer’s disease (AD).
Laura García-González, Dominika Pilat, Kévin Baranger, Santiago Rivera   +3 more
doaj   +1 more source

BACE1 activity regulates cell surface contactin-2 levels [PDF]

, 2014
Background: Although BACE1 is a major therapeutic target for Alzheimer’s disease (AD), potential side effects of BACE1 inhibition are not well characterized. BACE1 cleaves over 60 putative substrates, however the majority of these cleavages have not been
D’Avanzo, Carla, Gautam, Vivek, Hebisch, Matthias, Kim, Doo Yeon, Kovacs, Dora M   +4 more
core   +1 more source

gamma-Secretase dependent production of intracellular domains is reduced in adult compared to embryonic rat brain membranes. [PDF]

PLoS ONE, 2010
BACKGROUND: gamma-Secretase is an intramembrane aspartyl protease whose cleavage of the amyloid precursor protein (APP) generates the amyloid beta-peptide (Abeta) and the APP intracellular domain.
Jenny Frånberg, Helena Karlström, Bengt Winblad, Lars O Tjernberg, Susanne Frykman   +4 more
doaj   +1 more source

Axonal BACE1 dynamics and targeting in hippocampal neurons: a role for Rab11 GTPase [PDF]

, 2014
BACKGROUND: BACE1 is one of the two enzymes that cleave amyloid precursor protein to generate Alzheimer's disease (AD) beta amyloid peptides. It is widely believed that BACE1 initiates APP processing in endosomes, and in the brain this cleavage is known ...
Celia G Fernandez, Gopal Thinakaran, Jack Waters, Jelita Roseman, Kulandaivelu S Vetrivel, Robert Vassar, Sean Riordan, Virginie Buggia-Prévot, Vytautas P Bindokas   +8 more
core   +1 more source

Beta‐secretase regulation in aging and disease

The FASEB Journal, 2007
Background: Beta‐secretase (BACE, types 1 and 2) has been identified as the enzyme that cleaves the β‐amyloid Precursor Protein to form the amyloid‐β peptide (Aβ). As the Aβ peptide is considered a primary causal factor in Alzheimer's disease (AD) pathogenesis, reducing Aβ production is currently a major ...
Rachel R Ahmed, M Paul Murphy, Marjorie J Rochette, Todd E Golde   +3 more
openaire   +1 more source