Results 11 to 20 of about 40,397 (225)

Presenilin 1 Modulates Acetylcholinesterase Trafficking and Maturation. [PDF]

Int J Mol Sci, 2023
In Alzheimer’s disease (AD), the reduction in acetylcholinesterase (AChE) enzymatic activity is not paralleled with changes in its protein levels, suggesting the presence of a considerable enzymatically inactive pool in the brain. In the present study, we validated previous findings, and, since inactive forms could result from post-translational ...
Cortés-Gómez MÁ, Barberá VM, Alom J, Sáez-Valero J, García-Ayllón MS.   +4 more
europepmc   +5 more sources

Versatility of presenilin 1 [PDF]

Proceedings of the National Academy of Sciences, 2017
Mutations in PSEN1 and PSEN2 genes, encoding presenilin 1 (PS1) and presenilin 2 (PS2), respectively, cause autosomal-dominant Alzheimer’s disease (ADAD) (1, 2). The precise mechanism by which PS1 mutations lead to AD is under active investigation. Multiple theories have been suggested to explain the role of PS1 and PS2 mutations on AD pathogenesis ...
Georgia R, Frost, Eitan, Wong, Yue-Ming, Li   +2 more
openaire   +2 more sources

Presenilin-1-Dependent Transcriptome Changes [PDF]

The Journal of Neuroscience, 2005
Familial forms of Alzheimer's disease (FADs) are caused by the expression of mutant presenilin 1 (PS1) or presenilin 2. Using DNA microarrays, we explored the brain transcription profiles of mice with conditional knock-out ofPS1(cKOPS1) in the forebrain.
Károly, Mirnics, Zeljka, Korade, Dominique, Arion, Orly, Lazarov, Travis, Unger, Melissa, Macioce, Michael, Sabatini, David, Terrano, Katherine C, Douglass, Nina F, Schor, Sangram S, Sisodia   +10 more
openaire   +2 more sources

Protein Topology of Presenilin 1 [PDF]

Neuron, 1996
Mutations in a gene encoding a multitransmembrane protein, termed presenilin 1 (PS1), are causative in the majority of early-onset cases of AD. To determine the topology of PS1, we utilized two strategies: first, we tested whether putative transmembranes are sufficient to export a protease-sensitive substrate across a lipid bilayer; and second, we ...
Doan, Andrew, Thinakaran, Gopal, Borchelt, David R, Slunt, Hilda H, Ratovitsky, Tamara, Podlisny, Marcia, Selkoe, Dennis J, Seeger, Mary, Gandy, Samuel E, Price, Donald L, Sisodia, Sangram S   +10 more
openaire   +2 more sources

Pen2 and Presenilin-1 Modulate the Dynamic Equilibrium of Presenilin-1 and Presenilin-2 γ-Secretase Complexes [PDF]

Journal of Biological Chemistry, 2009
gamma-Secretase is known to play a pivotal role in the pathogenesis of Alzheimer disease through production of amyloidogenic Abeta42 peptides. Early onset familial Alzheimer disease mutations in presenilin (PS), the catalytic core of gamma-secretase, invariably increase the Abeta42:Abeta40 ratio.
Lisa, Placanica, Leonid, Tarassishin, Guangli, Yang, Erica, Peethumnongsin, Seong-Hun, Kim, Hui, Zheng, Sangram S, Sisodia, Yue-Ming, Li   +7 more
openaire   +2 more sources

Oligomerization of human presenilin‐1 fragments [PDF]

FEBS Letters, 2003
To gain insight into presenilin‐1 (PS1) structural aspects, we explored the structure–function relationship of its N‐ and C‐terminal (NTF and CTF, respectively) complexes. We demonstrated that both NTF and CTF act as independent but inter‐changing binding units capable of binding each other (NTF/CTF) or their homologues (NTF/NTF; CTF/CTF).
Hébert, Sébastien S, Godin, Chantal, Lévesque, Georges   +2 more
openaire   +2 more sources

Presenilin 1 Glu318Gly Polymorphism [PDF]

Archives of Neurology, 2005
The significance of the presenilin 1 (PSEN1) Glu318Gly polymorphism has been described as either a causal mutation with reduced penetrance or a benign polymorphism. When this polymorphism is found in a symptomatic person with a family history of dementia, counseling on recurrence risk becomes very problematic.To demonstrate that the PSEN1 Glu318Gly ...
Jill S, Goldman, Julene K, Johnson, Karen, McElligott, Oksana, Suchowersky, Bruce L, Miller, Vivianna M, Van Deerlin   +5 more
openaire   +2 more sources

Structural biology of presenilin 1 complexes [PDF]

Molecular Neurodegeneration, 2014
The presenilin genes were first identified as the site of missense mutations causing early onset autosomal dominant familial Alzheimer's disease. Subsequent work has shown that the presenilin proteins are the catalytic subunits of a hetero-tetrameric complex containing APH1, nicastrin and PEN-2.
Li, Yi, Bohm, Christopher, Dodd, Roger, Chen, Fusheng, Qamar, Seema, Schmitt-Ulms, Gerold, Fraser, Paul E, St George-Hyslop, Peter H   +7 more
openaire   +3 more sources

Presenilin-1 mutations and Alzheimer’s disease [PDF]

Proceedings of the National Academy of Sciences, 2017
Mutations in the PSEN1 gene, encoding presenilin-1 (PS1), are the most common cause of familial Alzheimer’s disease (FAD). PS1 functions as the catalytic subunit of γ-secretase, an intramembranous protease that cleaves a variety of type 1 transmembrane proteins, notably including the amyloid precursor protein (APP) and Notch.
Raymond J, Kelleher, Jie, Shen
openaire   +2 more sources

A patient with posterior cortical atrophy possesses a novel mutation in the presenilin 1 gene. [PDF]

PLoS ONE, 2013
Posterior cortical atrophy is a dementia syndrome with symptoms of cortical visual dysfunction, associated with amyloid plaques and neurofibrillary tangles predominantly affecting visual association cortex. Most patients diagnosed with posterior cortical
Emilia J Sitek, Ewa Narożańska, Beata Pepłońska, Sławomir Filipek, Anna Barczak, Maria Styczyńska, Krzysztof Mlynarczyk, Bogna Brockhuis, Erik Portelius, Dorota Religa, Maria Barcikowska, Jarosław Sławek, Cezary Żekanowski   +12 more
doaj   +1 more source