Results 101 to 110 of about 36,206 (272)

Inhibition of amyloid precursor protein secretases reduces recovery after spinal cord injury [PDF]

Brain Research, 2014
Amyloid-β (Aβ) is produced through the enzymatic cleavage of amyloid precursor protein (APP) by β (Bace1) and γ-secretases. The accumulation and aggregation of Aβ as amyloid plaques is the hallmark pathology of Alzheimer׳s disease and has been found in other neurological disorders, such as traumatic brain injury and multiple sclerosis.
Ahdeah, Pajoohesh-Ganji, Mark P, Burns, Sonali, Pal-Ghosh, Gauri, Tadvalkar, Nicole G, Hokenbury, Mary Ann, Stepp, Alan I, Faden   +6 more
openaire   +2 more sources

Role of P2X7 and P2Y2 receptors on α-secretase-dependent APP processing: Control of amyloid plaques formation “in vivo” by P2X7 receptor

Computational and Structural Biotechnology Journal, 2015
Amyloid precursor protein (APP) is expressed in a large variety of neural and non-neural cells. The balance between non-pathogenic and pathologic forms of APP processing, mediated by α-secretase and β-secretase respectively, remains a crucial step to ...
M. Teresa Miras-Portugal, Juan I. Diaz-Hernandez, Rosa Gomez-Villafuertes, Miguel Diaz-Hernandez, Antonio R. Artalejo, Javier Gualix   +5 more
doaj   +1 more source

Astrocytic LRP1 mediates brain Aβ clearance and impacts amyloid deposition [PDF]

, 2017
Accumulation and deposition of amyloid-β (Aβ) in the brain represent an early and perhaps necessary step in the pathogenesis of Alzheimer's disease (AD).
Bu, Guojun, Cirrito, John R, Holtzman, David M, Hu, Jin, Kanekiyo, Takahisa, Liu, Chia-Chen, Na, Wang, Wang, Jian, Zhao, Na   +8 more
core   +2 more sources

ADAM10‐Mediated Proteolytic Remodelling of Signalling and Adhesion Proteins on Brain Cell‐Derived Small Extracellular Vesicles

Journal of Extracellular Biology, Volume 5, Issue 4, April 2026.
ABSTRACT Proteases are common components of extracellular vesicles (EVs), yet the extent and functional relevance of ongoing proteolytic activity on EV surfaces remain largely unexplored. Such activity could significantly influence EV function and identity, with likely implications for EV‐mediated signalling, recipient cell targeting, cargo delivery ...
Christopher C. Reimann, Hermann C. Altmeppen, Tomas Koudelka, Michaela Schweizer, Andreas Tholey, Behnam Mohammadi, Julia Bär, Lesley Cheng, Markus Glatzel, Marina Mikhaylova, Andrew F. Hill   +10 more
wiley   +1 more source

Protein Aggregates and Polyglutamine Tracts In Neurodegenerative Disease [PDF]

, 2018
The incidence of neurodegenerative diseases such as Alzheimer\u27s Disease, Parkinson\u27s Disease, Huntington\u27s Disease and other Polyglutamine Diseases is projected to dramatically increase throughout the developed world, and yet the pathology of ...
Mack, John
core   +1 more source

Different types of γ-secretes complexes and their effect on substrate processing [PDF]

, 2012
The γ-secretase complex is a transmembrane aspartyl protease that generates the Alzheimer disease (AD) related amyloid β-peptide (Aβ) from the amyloid precursor protein (APP). The γ- secretase complex cleaves APP at two different sites (γ- and ε-sites)
Pamrén, Annelie
core   +1 more source

Analyzing Nicotine Action Against Amyloid Toxicity by NMR‐Pharmacometabolomics: An Exploratory Study

NMR in Biomedicine, Volume 39, Issue 4, April 2026.
Combined metabolomic analysis of the intracellular and extracellular portions of SH‐SY5Y cells revealed that, in the presence of Aβ 1–42, nicotine primarily influences pathways related to neurotransmission, energy metabolism, as well as the biosynthesis and degradation of membrane phospholipids.
Enza Napolitano, Carmen Marino, Manuela Grimaldi, Michela Buonocore, Angelo Santoro, Anna Maria D'Ursi   +5 more
wiley   +1 more source

Herpes Simplex Virus type-1 infection induces synaptic dysfunction in cultured cortical neurons via GSK-3 activation and intraneuronal amyloid-β protein accumulation [PDF]

, 2015
Increasing evidence suggests that recurrent Herpes Simplex Virus type 1 (HSV-1) infection spreading to the CNS is a risk factor for Alzheimer's Disease (AD) but the underlying mechanisms have not been fully elucidated yet.
De Chiara, Giovanna, Garaci, Enrico, Grassi, Claudio, Li Puma, Domenica Donatella, Marcocci, Maria Elena, Palamara, ANNA TERESA, Piacentini, Roberto, Ripoli, Cristian   +7 more
core   +2 more sources

Toxic mechanisms of amyloid oligomers and therapeutic strategies

Protein Science, Volume 35, Issue 4, April 2026.
Abstract Amyloid oligomers are increasingly recognized as the major toxic contributors across protein‐misfolding disorders. In this review, we cover mechanistic evidence showing how these transient and structurally heterogeneous oligomers disrupt cellular homeostasis by: (i) permeabilizing lipid membranes and forming ion‐conducting pores; (ii ...
Magdalena I. Ivanova, Carmelo La Rosa, Ayyalusamy Ramamoorthy   +2 more
wiley   +1 more source

Destruxin E Decreases Beta-Amyloid Generation by Reducing Colocalization of Beta-Amyloid-Cleaving Enzyme 1 and Beta-Amyloid Protein Precursor [PDF]

, 2009
Alzheimer-disease-associated beta-amyloid (A beta) is produced by sequential endoproteolysis of beta-amyloid protein precursor (beta APP): the extracellular portion is shed by cleavage in the juxtamembrane region by beta-amyloid-cleaving enzyme (BACE ...
Dohi, Keiji, Fukumori, Akio, Haass, Christian, Hasegawa, Hiroshi, Hosono, Motoko, Itoh, Naohiro, Jiang, Jingwei, Kato, Akira, Katoh, Takaaki, Kikuchi, Jyunko, Kudo, Takashi, Minagawa, Kazuyuki, Mori, Kohji, Morihara, Takashi, Nakano, Yuko, Nakayama, Taisuke, Nishigaki, Atsuko, Nishimura, Masaki, Nishitomi, Kouhei, Okochi, Masayasu, Sakaguchi, Gaku, Tagami, Shinji, Takeda, Masatoshi, Takemoto, Hiroshi, Takinami, Yoshihiko, Tanaka, Toshihisa, Willem, Michael, Yanagida, Kanta   +27 more
core   +1 more source