Results 21 to 30 of about 16,063 (220)

Transcription factor Sp1 induces ADAM17 and contributes to tumor cell invasiveness under hypoxia [PDF]

, 2009
Background Expression of the Sp1 transcription factor is induced by hypoxia, and the ADAM17 promoter contains predicted Sp1 binding sites. ADAM17 contributes to hypoxic-induce invasiveness of glioma.
Alexandra Szalad, Mark Katakowski, Xuguang Zheng, Feng Jiang, Michael Chopp   +4 more
core   +2 more sources

Manipulation of lipid rafts in neuronal cells [PDF]

, 2010
Lipid rafts are specialized plasma membrane micro-domains highly enriched in cholesterol, sphingolipids and glycosylphosphatidylinositol (GPI) anchored proteins.
Eckert, Gunter P.
core   +1 more source

Impact of inhibitors and L2 antibodies upon the infectivity of diverse alpha and beta human papillomavirus types. [PDF]

PLoS ONE, 2014
The licensed human papillomavirus (HPV) vaccines elicit type-restricted immunity but do not target cutaneous HPV types of the beta genus that are associated with non-melanoma skin cancer in immune-compromised patients, and it is unclear if these diverse ...
Kihyuck Kwak, Rosie Jiang, Joshua W Wang, Subhashini Jagu, Reinhard Kirnbauer, Richard B S Roden   +5 more
doaj   +1 more source

HIV-Associated Insults Modulate ADAM10 and Its Regulator Sirtuin1 in an NMDA Receptor-Dependent Manner

Cells, 2022
Neurologic deficits associated with human immunodeficiency virus (HIV) infection impact about 50% of persons with HIV (PWH). These disorders, termed HIV-associated neurocognitive disorders (HAND), possess neuropathologic similarities to Alzheimer’s ...
Claudia Lopez Lloreda, Sarah Chowdhury, Shivesh Ghura, Elena Alvarez-Periel, Kelly Jordan-Sciutto   +4 more
doaj   +1 more source

Bryostatin-1 vs. TPPB: Dose-Dependent APP Processing and PKC-α, -δ, and -ε Isoform Activation in SH-SY5Y Neuronal Cells [PDF]

, 2012
Activation of the α-secretase processing pathway of amyloid precursor protein (APP) is recognized as an important mechanism which diverts APP processing from production of beta-amyloid (Aβ) to non toxic sAPPα, decreasing Alzheimer’s disease (AD) plaque ...
J. S. Alexander, L. Schrott, P. Yi, T. P. Castor   +3 more
core   +1 more source

Developments in the Role of Iron Imbalance in the Pathogenesis of Alzheimer's Disease [PDF]

Zhongguo quanke yixue, 2022
Iron load is closely associated with the initiation and progression of Alzheimer's disease (AD) . Although age-dependent deposition of β-amyloid (A β) in senile plaques (SPs) , and neurofibrillary tangles (NFTs) formed by accumulation ...
GUO Shuang, CHEN Fengyan, YIN Xiang, WANG Lu, GUO Xuefeng, YU Qiming, ZOU Zhenyou, SHU Wei
doaj   +1 more source

Astroglial mGlu3 receptors promote alpha-secretase-mediated amyloid precursor protein cleavage

Neuropharmacology, 2014
Amyloid precursor protein (APP) shedding yields the Alzheimer's disease (AD)-related peptide amyloid β (Aβ) through β- and γ-secretase cleavage. Alternatively, α-secretase cleavage generates a soluble and neuroprotective fragment (sAPPα) while precludes the production of Aβ.
Durand, Daniela Elizabeth, Carniglia, Lila, Beauquis, Juan, Caruso, Carla Mariana, Saravia, Flavia Eugenia, Lasaga, Mercedes Isabel   +5 more
openaire   +3 more sources

Alpha-secretase inhibition impairs Group I metabotropic glutamate receptor-mediated protein synthesis, long-term potentiation and long-term depression. [PDF]

Philos Trans R Soc Lond B Biol Sci
Group I metabotropic glutamate receptors (Gp1-mGluRs) exert a host of effects on cellular functions, including enhancement of protein synthesis and the associated facilitation of long-term potentiation (LTP) and induction of long-term depression (LTD). However, the complete cascades of events mediating these events are not fully understood.
Mockett BG, Davies JWT, Mills ZB, Kweon DY, Abraham WC.   +4 more
europepmc   +3 more sources

ADAM9 inhibition increases membrane activity of ADAM10 and controls α-secretase processing of amyloid precursor protein [PDF]

, 2011
Prodomains of A disintegrin and metalloproteinase (ADAM) metallopeptidases can act as highly specific intra- and intermolecular inhibitors of ADAM catalytic activity. The mouse ADAM9 prodomain (proA9; amino acids 24–204), expressed and characterized from
Amour, Arribas, Bartsch, Black, Cissé, Crawford, De Strooper, Edwards, Fassold, Geretti, Gonzales, Gray, Hass, Hirahashi, Koller, Kuhn, Kveiborg, Lee, Lemieux, Leon, Leonard, Lichtenthaler, Liu, Matei, Miller, Morrison, Moss, Moss, Moss, Moss, Moss, Murphy, Nasarre, Naus, Nocentini, Pan, Postina, Rose, Rose, Saftig, Sahin, Sunnarborg, Tape, Taylor, Tousseyn, Turner, Turtinen, Weskamp, Weskamp, Zhao, Zhou, Zhou   +51 more
core   +1 more source

Constitutive α- and β-secretase cleavages of the amyloid precursor protein are partially coupled in neurons, but not in frequently used cell lines

Neurobiology of Disease, 2013
Proteolytic cleavage of the amyloid precursor protein (APP) by the two proteases α- and β-secretases controls the generation of the amyloid β peptide (Aβ), a key player in Alzheimer's disease pathogenesis. The α-secretase ADAM10 and the β-secretase BACE1
Alessio Colombo, Huanhuan Wang, Peer-Hendrik Kuhn, Richard Page, Elisabeth Kremmer, Peter J. Dempsey, Howard C. Crawford, Stefan F. Lichtenthaler   +7 more
doaj   +1 more source