نتایج جستجو برای: bace 1

تعداد نتایج: 2752751  

Journal: :Neurobiology of Aging 2016
Nicolau Beckmann Arno Doelemeyer Stefan Zurbruegg Karine Bigot Diethilde Theil Wilfried Frieauff Carine Kolly Pierre Moulin Daniel Neddermann Robert Kreutzer Ludovic Perrot Irena Brzak Laura H. Jacobson Matthias Staufenbiel Ulf Neumann Derya R. Shimshek

Currently, several immunotherapies and BACE (Beta Site APP Cleaving Enzyme) inhibitor approaches are being tested in the clinic for the treatment of Alzheimer's disease. A crucial mechanism-related safety concern is the exacerbation of microhemorrhages, which are already present in the majority of Alzheimer patients. To investigate potential safety liabilities of long-term BACE inhibitor therap...

Journal: :ChemMedChem 2010
Elisabet Viayna Tània Gómez Carles Galdeano Lorena Ramírez Míriam Ratia Albert Badia M Victòria Clos Ester Verdaguer Félix Junyent Antoni Camins Mercè Pallàs Manuela Bartolini Francesca Mancini Vincenza Andrisano Mariana P Arce María Isabel Rodríguez-Franco Axel Bidon-Chanal F Javier Luque Pelayo Camps Diego Muñoz-Torrero

A new family of dual binding site acetylcholinesterase (AChE) inhibitors has been designed, synthesized, and tested for their ability to inhibit AChE, butyrylcholinesterase (BChE), AChE-induced and self-induced β-amyloid (Aβ) aggregation and β-secretase (BACE-1), and to cross the blood-brain barrier. The new heterodimers consist of a unit of racemic or enantiopure huprine Y or X and a donepezil...

2005
Alemayehu A. Gorfe Amedeo Caflisch

The aspartic protease -secretase (BACE) cleaves the amyloid precursor protein into a 42 residue -peptide, which is the principal biochemical marker of Alzheimer’s disease. Multiple explicit-water molecular dynamics simulations of the apo and inhibitor bound structures of BACE indicate that both openand closed-flap conformations are accessible at room temperature and should be taken into account...

Journal: :Biochemistry 2011
Sabyashachi Mishra Amedeo Caflisch

The aspartic protease β-secretase (BACE) catalyzes the hydrolysis of the amyloid precursor protein (APP) which leads to amyloid-β aggregation and, ultimately, the perilous Alzheimer's disease. The conformational dynamics and free energy surfaces of BACE at three steps of the catalytic cycle are studied here by explicit solvent molecular dynamics simulations (multiple runs for a total of 2.2 μs)...

Journal: :Acta biochimica Polonica 2004
Barbara Nawrot

beta-Secretase, a beta-site amyloid precursor protein (APP) cleaving enzyme (BACE), participates in the secretion of beta-amyloid peptides (Abeta), the major components of the toxic amyloid plaques found in the brains of patients with Alzheimer's disease (AD). According to the amyloid hypothesis, accumulation of Abeta is the primary influence driving AD pathogenesis. Lowering of Abeta secretion...

Journal: :Biochemical Society transactions 2005
J A Johnston W W Liu S A Todd D T R Coulson S Murphy G B Irvine A P Passmore

Several lines of evidence indicate that the Abeta peptide is involved at some level in the pathological process that results in the clinical symptoms of AD (Alzheimer's disease). The N-terminus of Abeta is generated by cleavage of the Met-Asp bond at position 671-672 of APP (amyloid precursor protein), catalysed by a proteolytic activity called beta-secretase. Two 'beta-secretase' proteases hav...

Journal: :Science-Business eXchange 2011

2015
Jihad El Andari Florian Altegoer Gert Bange Peter L. Graumann Dirk-Jan Scheffers

Bactofilins are a widely conserved protein family implicated in cell shape maintenance and in bacterial motility. We show that the bactofilins BacE and BacF from Bacillus subtilis are essential for motility. The proteins are required for the establishment of flagellar hook- and filament structures, but apparently not for the formation of basal bodies. Functional YFP fusions to BacE and to BacF ...

Journal: :Biochemical and Biophysical Research Communications 2010

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