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pro vyhledávání: '"Ji-Yeun Hur"'
Autor:
Ji Yeun Hur
Publikováno v:
Experimental & Molecular Medicine. 54:433-446
Alzheimer’s disease (AD) is caused by synaptic and neuronal loss in the brain. One of the characteristic hallmarks of AD is senile plaques containing amyloid β-peptide (Aβ). Aβ is produced from amyloid precursor protein (APP) by sequential prote
Autor:
Ji-Yeun Hur
Publikováno v:
DNA and Cell Biology. 40:1351-1355
Several genes in innate immunity have been implicated in Alzheimer's disease (AD). However, the effect of innate immunity on amyloid β (Aβ) production, which makes amyloid plaques in AD brains, was previously not known. Recently, the antiviral prot
Autor:
Ji-Yeun, Hur
Publikováno v:
Experimentalmolecular medicine. 54(4)
Alzheimer's disease (AD) is caused by synaptic and neuronal loss in the brain. One of the characteristic hallmarks of AD is senile plaques containing amyloid β-peptide (Aβ). Aβ is produced from amyloid precursor protein (APP) by sequential proteol
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e80706 (2013)
Alzheimer's disease (AD), the most common cause of dementia in the elderly, has two pathological hallmarks: Aβ plaques and aggregation of hyperphosphorylated tau (p-tau). Aβ is a cleavage product of Amyloid Precursor Protein (APP). Presenilin 1 (PS
Externí odkaz:
https://doaj.org/article/fd48621a8fb244fe9fa698bc23f943a9
Autor:
Susanne Frykman, Ji-Yeun Hur, Jenny Frånberg, Mikio Aoki, Bengt Winblad, Jarmila Nahalkova, Homira Behbahani, Lars O Tjernberg
Publikováno v:
PLoS ONE, Vol 5, Iss 1, p e8948 (2010)
A key player in the development of Alzheimer's disease (AD) is the gamma-secretase complex consisting of at least four components: presenilin, nicastrin, Aph-1 and Pen-2. gamma-Secretase is crucial for the generation of the neurotoxic amyloid beta-pe
Externí odkaz:
https://doaj.org/article/9e22371927fa4938a8616fb043913923
Autor:
Ji-Yeun Hur1, Welander, Hedvig1, Behbahani, Homira1, Aoki, Mikio1,2, Frånberg, Jenny1, Winblad, Bengt1, Frykman, Susanne1, Tjernberg, Lars O.1 Lars.Tjernberg@ki.se
Publikováno v:
FEBS Journal. Mar2008, Vol. 275 Issue 6, p1174-1187. 14p. 5 Black and White Photographs, 1 Diagram.
Autor:
Pengju Nie, Katherine R. Sadleir, Yujia Zhai, Bianca T. Esposito, Andrew M. McKenzie, Christina J. Crump, Eitan Wong, Douglas S. Johnson, Julia Tcw, Eliezer Masliah, Ji-Yeun Hur, Paul Greengard, Yotam Sagi, Chen Ming, Yong Kim, Jen Chyong Wang, Si Jia Pan, Marília A. S. Barros, Bin Zhang, Xianzhong Wu, Robert A. Rissman, Lei Guo, Thomas Li, Georgia R. Frost, Yue-Ming Li, Alison Goate, Minghui Wang, Robert Vassar, Xianxiao Zhou, Ivy Trinh, Alan E. Renton
Publikováno v:
Molecular Neurodegeneration
Nature
Nature
Innate immunity is associated with Alzheimer’s disease1, but the influence of immune activation on the production of amyloid-β is unknown2,3. Here we identify interferon-induced transmembrane protein 3 (IFITM3) as a γ-secretase modulatory protein
Autor:
Taizo Ishikawa, Sophia Schedin-Weiss, Yasuhiro Teranishi, Birgitta Wiehager, Bengt Winblad, Takahiro Kihara, Ji-Yeun Hur, Mitsuhiro Inoue, Natsuko G. Yamamoto, Lars O. Tjernberg
Publikováno v:
FEBS Journal. 282:2587-2599
The transmembrane protease complex γ-secretase is a key enzyme in Alzheimer disease pathogenesis as it liberates the neurotoxic amyloid β-peptide (Aβ); however, the mechanism of regulation of its activity in various cell types and subcellular comp
Autor:
Frykman, Susanne1 susanne.frykman@ki.se, Ji-Yeun Hur1, Frånberg, Jenny2, Aoki, Mikio3, Winblad, Bengt1, Nahalkova, Jarmila1, Behbahani, Homira1, Tjernberg, Lars O.1
Publikováno v:
PLoS ONE. 2010, Vol. 5 Issue 1, p1-10. 10p. 4 Color Photographs, 2 Black and White Photographs, 2 Graphs.
Autor:
Ji-Yeun Hur, Susanne Frykman, Hedvig Welander, Lars O. Tjernberg, Bengt Winblad, Jenny Frånberg, Mikio Aoki, Yasuhiro Teranishi
Publikováno v:
Journal of Cellular and Molecular Medicine
γ-Secretase is a transmembrane protease complex responsible for the processing of a multitude of type 1 transmembrane proteins, including amyloid precursor protein (APP) and Notch. A functional complex is dependent on the assembly of four proteins: