Results 11 to 20 of about 337,024 (290)
Amyloid precursor protein and amyloid precursor-like protein 2 in cancer
Oncotarget, 2016 Amyloid precursor protein (APP) and its family members amyloid precursor-like protein 1 (APLP1) and amyloid precursor-like protein 2 (APLP2) are type 1 transmembrane glycoproteins that are highly conserved across species.
P. Pandey +11 more
semanticscholar +4 more sources
Biology and pathophysiology of the amyloid precursor protein [PDF]
Molecular Neurodegeneration, 2011 The amyloid precursor protein (APP) plays a central role in the pathophysiology of Alzheimer's disease in large part due to the sequential proteolytic cleavages that result in the generation of β-amyloid peptides (Aβ).
Koo Edward H, Zheng Hui
doaj +6 more sources
Amyloid Precursor Protein (APP) and GABAergic Neurotransmission [PDF]
Cells, 2019 The amyloid precursor protein (APP) is the parent polypeptide from which amyloid-beta (Aβ) peptides, key etiological agents of Alzheimer’s disease (AD), are generated by sequential proteolytic processing involving β- and γ-secretases.
Bor Luen Tang
doaj +3 more sources
Amyloid precursor protein and neural development [PDF]
Development, 2014 Interest in the amyloid precursor protein (APP) has increased in recent years due to its involvement in Alzheimer's disease. Since its molecular cloning, significant genetic and biochemical work has focused on the role of APP in the pathogenesis of this ...
Maya Nicolas, Bassem A. Hassan
semanticscholar +4 more sources
Amyloid Precursor Protein and Alzheimer's Disease. [PDF]
Int J Mol Sci, 2023 Alzheimer’s disease (AD) is one of the most common neurodegenerative disorders associated with age or inherited mutations. It is characterized by severe dementia in the late stages that affect memory, cognitive functions, and daily life overall. AD progression is linked to the accumulation of cytotoxic amyloid beta (Aβ) and hyperphosphorylated tau ...
Orobets KS, Karamyshev AL.
europepmc +3 more sources
Amyloid precursor protein processing and bioenergetics [PDF]
Brain Research Bulletin, 2017 The processing of amyloid precursor protein (APP) to amyloid beta (Aβ) is of great interest to the Alzheimer's disease (AD) field. Decades of research define how APP is altered to form Aβ, and how Aβ generates oligomers, protofibrils, and fibrils. Numerous signaling pathways and changes in cell physiology are known to influence APP processing. Existing
Heather M. Wilkins, R. Swerdlow
semanticscholar +4 more sources
Neuroprotective Secreted Amyloid Precursor Protein Acts by Disrupting Amyloid Precursor Protein Dimers [PDF]
Journal of Biological Chemistry, 2009 The amyloid precursor protein (APP) is implied both in cell growth and differentiation and in neurodegenerative processes in Alzheimer disease. Regulated proteolysis of APP generates biologically active fragments such as the neuroprotective secreted ectodomain sAPPalpha and the neurotoxic beta-amyloid peptide.
Gralle, M. +2 more
openaire +5 more sources
Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage [PDF]
Proceedings of the National Academy of Sciences, 2004 Amyloid-β precursor protein (APP), a type I membrane protein, is physiologically processed by α- or β-secretases that cleave APP N-terminal to the transmembrane region. Extracellular α-/β-cleavage of APP generates a large secreted N-terminal fragment, and a smaller cellular C-terminal fragment.
Thomas C. Südhof, Angela Ho
openaire +3 more sources
Heteromers of amyloid precursor protein in cerebrospinal fluid [PDF]
Molecular Neurodegeneration, 2015 Soluble fragments of the amyloid precursor protein (APP) generated by α- and β-secretases, sAPPα and sAPPβ, have been postulated as promising new cerebrospinal fluid (CSF) biomarkers for the clinical diagnosis of Alzheimer's disease (AD). However, the capacity of these soluble proteins to assemble has not been explored and could be relevant. Our aim is
Cuchillo-Ibáñez, Inmaculada +6 more
openaire +7 more sources
AMYPdb: A database dedicated to amyloid precursor proteins [PDF]
BMC Bioinformatics, 2008 Abstract Background Misfolding and aggregation of proteins into ordered fibrillar structures is associated with a number of severe pathologies, including Alzheimer's disease, prion diseases, and type II diabetes. The rapid accumulation of knowledge about the sequences and structures of these proteins allows using of ...
Le Béchec, Antony +2 more
openaire +5 more sources