Results 181 to 190 of about 16,063 (220)
Some of the next articles are maybe not open access.
SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10.
Cell, 2010A hallmark of Alzheimer's disease (AD) is the accumulation of plaques of Abeta 1-40 and 1-42 peptides, which result from the sequential cleavage of APP by the beta and gamma-secretases. The production of Abeta peptides is avoided by alternate cleavage of APP by the alpha and gamma-secretases.
Gizem, Donmez +3 more
openaire +1 more source
Regulation of alpha-secretase ADAM10 expression and activity
Experimental Brain Research, 2011The amyloid precursor protein (APP) has a pivotal role in pathogenesis of Alzheimer's disease (AD) via its beta- and gamma-secretase-derived cleavage products--the A-beta peptides. An alternative processing pathway provided by the alpha-secretase prevents formation of those toxic peptides and gives rise to the neurotrophic and neuroprotective cleavage ...
Kristina, Endres, Falk, Fahrenholz
openaire +2 more sources
Protein kinase C epsilon suppresses Abeta production and promotes activation of alpha-secretase.
Biochemical and biophysical research communications, 2001Deposition of plaques containing Abeta is considered important in the pathogenesis of Alzheimer's disease. Phorbol esters that activate protein kinase C (PKC) promote alpha-secretase-mediated processing of the beta amyloid precursor protein (APP), which generally reduces formation of Abeta.
G, Zhu +5 more
openaire +1 more source
Current Alzheimer Research, 2012
α-secretase is the name for a metalloprotease activity, which is assumed to play a key role in the prevention of the molecular mechanisms underlying Alzheimer's disease (AD). Proteases similar to α-secretase are essential for a wide range of biological processes, such as cell adhesion and embryonic development.
openaire +3 more sources
α-secretase is the name for a metalloprotease activity, which is assumed to play a key role in the prevention of the molecular mechanisms underlying Alzheimer's disease (AD). Proteases similar to α-secretase are essential for a wide range of biological processes, such as cell adhesion and embryonic development.
openaire +3 more sources
Neurodegenerative Diseases, 2012
<i>Background:</i> ADAM10 (a disintegrin and metalloproteinase 10) has been demonstrated to act as the main physiological α-secretase. Enzymatic activity of the α-secretase on the one hand prevents the formation of toxic Aβ peptides and on the other hand promotes the secretion of a neurotrophic and neuroprotective amyloid precursor protein ...
David, Holthoewer +5 more
openaire +2 more sources
<i>Background:</i> ADAM10 (a disintegrin and metalloproteinase 10) has been demonstrated to act as the main physiological α-secretase. Enzymatic activity of the α-secretase on the one hand prevents the formation of toxic Aβ peptides and on the other hand promotes the secretion of a neurotrophic and neuroprotective amyloid precursor protein ...
David, Holthoewer +5 more
openaire +2 more sources
Levels of beta-secretase BACE and alpha-secretase ADAM10 mRNAs in Alzheimer hippocampus.
Neuroreport, 2002The amyloid cascade hypothesis suggests that amyloid precursor protein (APP) proteolytic processing is a key event in the pathogenesis of Alzheimer's disease (AD). The enzymes beta-site APP cleaving enzyme (BACE) and A disintegrin and metalloproteinase 10 (ADAM10) play an important role in APP proteolysis.
GATTA LB +3 more
openaire +2 more sources
Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17.
Current Alzheimer research, 2008Disintegrin metalloproteases of the ADAM family form a large (at present > 40 members in mammals) family of multidomain membrane proteins that in their ectodomain combine a cystein-rich, disintegrin and a zinc metalloprotease domain. Via their metalloprotease domain, ADAMs are often implicated in ectodomain shedding, either to release e.g.
Miriam, Deuss +2 more
openaire +1 more source
Zhurnal vysshei nervnoi deiatelnosti imeni I P Pavlova, 2006
Intracortical administration of 10(-4) M batimastat, a specific inhibitor of one of metalloproteinases metabolizing amyloid precursor protein, namely alpha-secretase, to adult rats resulted in a decrease in the number of correct runs in a one-level 8-arm maze down to 92.78 +/- 1.03% of the control values (p < 0.01) already 60 min after an injection ...
N M, Dubrovskaia +3 more
openaire +1 more source
Intracortical administration of 10(-4) M batimastat, a specific inhibitor of one of metalloproteinases metabolizing amyloid precursor protein, namely alpha-secretase, to adult rats resulted in a decrease in the number of correct runs in a one-level 8-arm maze down to 92.78 +/- 1.03% of the control values (p < 0.01) already 60 min after an injection ...
N M, Dubrovskaia +3 more
openaire +1 more source
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2006
The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) has neurotrophic as well as anti-apoptotic properties and is involved in learning and memory processes. Its specific G protein-coupled receptor PAC1 is expressed in several central nervous system (CNS) regions, including the hippocampal formation. Here we examined the effect of
Elzbieta, Kojro +5 more
openaire +1 more source
The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) has neurotrophic as well as anti-apoptotic properties and is involved in learning and memory processes. Its specific G protein-coupled receptor PAC1 is expressed in several central nervous system (CNS) regions, including the hippocampal formation. Here we examined the effect of
Elzbieta, Kojro +5 more
openaire +1 more source
[S2‐01‐01]: Alpha‐secretase as a therapeutic target
Alzheimer's & Dementia, 2005Falk Fahrenholz +4 more
openaire +1 more source

