Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Daniel Sevlever"'
Autor:
Steven G. Younkin, Mariet Younkin, Gina Bisceglio, Dennis W. Dickson, Nilufer Ertekin-Taner, Sakae Nobutaka, Li Ma, Daniel Sevlever
Publikováno v:
Alzheimer's & Dementia. 12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90de1812f12ea9fb73299c12fa160351
https://doi.org/10.1016/j.jalz.2016.06.1495
https://doi.org/10.1016/j.jalz.2016.06.1495
Autor:
Neill R. Graff-Radford, Daniel Sevlever, Mariet Allen, Nobutaka Sakae, Li Ma, Steven G. Younkin, Dennis W. Dickson, Nilufer Ertekin-Taner
Publikováno v:
Molecular Neurodegeneration
Background Genetic analyses showed that the triggering receptor expressed in myeloid cells 2 (TREM2) p.R47H variant increases the risk for Alzheimer’s disease (AD). The question of whether the p.R47H mutation affects expression or function of the r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e712b8fe230d1aced5fa567f8dc0ad
https://pubmed.ncbi.nlm.nih.gov/27887626
https://pubmed.ncbi.nlm.nih.gov/27887626
Autor:
Xianlin Han, Masaya Tachibana, Miao Wang, Fanggeng Zou, Yu Yamazaki, Yasumasa Ohyagi, Nobutaka Sakae, Romain Fol, Aishe Kurti, Minerva M. Carrasquillo, Jessica L. Frisch-Daiello, Daniel Sevlever, Linda H. Younkin, Ming Gan, Gina Bisceglio, Steven G. Younkin, Guojun Bu, Chia Chen Liu, John D. Fryer, Li Ma, Takahisa Kanekiyo, Michael L. Fitzgerald, Mitsuru Shinohara, Patrick Knight
In Alzheimer's disease (AD), the accumulation and deposition of amyloid-β (Aβ) peptides in the brain is a central event. Aβ is cleaved from amyloid precursor protein (APP) by β-secretase and γ-secretase mainly in neurons. Although mutations inAP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52dc142d9f1256d2407afd5cc1fab2a1
https://europepmc.org/articles/PMC4812140/
https://europepmc.org/articles/PMC4812140/
Autor:
Michael McKinney, Dennis W. Dickson, Satoshi Yamamoto, Christopher B. Eckman, Daniel Sevlever, Justin H. Nguyen, Wen-Lang Lin, Naoki Shimojima
Publikováno v:
Journal of Investigative Surgery. 21:101-108
Brain edema secondary to increased blood-brain barrier (BBB) permeability is a lethal complication in fulminant hepatic failure (FHF). Intact tight junctions (TJ) between brain capillary endothelial cells are critical for normal BBB function. However
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c9095688e1ad0002e5a38a512098ead
https://doi.org/10.1080/08941930802043565
https://doi.org/10.1080/08941930802043565
Autor:
Makio Takahashi, Shu Hui C. Yen, Jayanarayan Kulathingal, Li Wen Ko, Daniel Sevlever, Peizhou Jiang
Publikováno v:
European Journal of Neuroscience. 26:863-874
Intracellular accumulation of alpha-synuclein (alpha-Syn) as filamentous aggregates is a pathological feature shared by Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, referred to as synucleinopathies. To understand the me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcd6c647ab93f79416078ea97b9ef8d0
https://doi.org/10.1111/j.1460-9568.2007.05736.x
https://doi.org/10.1111/j.1460-9568.2007.05736.x
Autor:
Sigrid Botne Sando, Minerva M. Carrasquillo, Michael Crump, Oliver J. Culley, Li Ma, Talisha A. Hunter, Gina Bisceglio, Fanggeng Zou, Dennis W. Dickson, Linda H. Younkin, Ronald C. Petersen, Jan O. Aasly, Ferenc Deak, Olivia Belbin, Mariet Allen, Neill R. Graff-Radford, Sebastian Carrasquillo, Daniel Sevlever
Publikováno v:
Molecular Neurodegeneration
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Background Alzheimer’s disease is a neurodegenerative disorder in which extracellular deposition of β-amyloid (Aβ) oligomers causes synaptic injury resulting in early memory loss, altered homeostasis, accumulation of hyperphosphorylated tau and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e4145f009a648310b2142bb1acb3a54
http://europepmc.org/articles/PMC4426163
http://europepmc.org/articles/PMC4426163
Publikováno v:
Biochemical and Biophysical Research Communications. 330:163-171
The synthesis of the glycosylphosphatidylinositol (GPI) anchor occurs in different compartments within the ER. We have previously shown that GPI anchor intermediates including GlcNAc-PI and GlcN-(acyl)PI are present in Triton insoluble membranes (TIM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bab0e2053aa45bd8464f1f7891033a69
https://doi.org/10.1016/j.bbrc.2005.02.136
https://doi.org/10.1016/j.bbrc.2005.02.136
Publikováno v:
Biochemical Journal. 378:641-648
GPI-PLD [glycosylphosphatidylinositol (GPI)-specific phospholipase D (PLD)] is a secreted mammalian enzyme that specifically cleaves GPI-anchored proteins. In addition, the enzyme has been shown to cleave GPI anchor intermediates in cell lysates. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2fccc121853fab8e6ddbef5d614b804
https://doi.org/10.1042/bj20031326
https://doi.org/10.1042/bj20031326
Autor:
Karl J. Mann, Daniel Sevlever
Publikováno v:
Biochemistry. 40:1205-1213
The glycosylphosphatidylinositol (GPI) moiety is widely used to anchor a functionally diverse group of proteins to the plasma membrane of eukaryotes. In mammals, the predominant glycan structure of the GPI anchor consists of EthN-P-Man-Man-(EthN-P)Ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::613128a044ddd3abe7d80dfdead42e1a
https://doi.org/10.1021/bi0024512
https://doi.org/10.1021/bi0024512
Publikováno v:
Biochemical Journal. 343:627-635
Glycosylphosphatidylinositol (GPI)-anchored proteins are resistant to solubilization with Triton X-100 at 4 °C, and they can be recovered in Triton-insoluble membranes (TIMs) that float to a characteristic buoyant density. Because the GPI structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2776863be9d6129dafede125cea717e
https://doi.org/10.1042/bj3430627
https://doi.org/10.1042/bj3430627