Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Jaehong Suh"'
Publikováno v:
STAR Protocols, Vol 3, Iss 2, Pp 101349- (2022)
Summary: Utilization of live animals for mechanistic study is challenging yet pivotal to elucidate pathogenesis of neurological diseases. Here, we present a protocol that employs cultured brain slices derived from adult mice to examine mRNA metabolis
Externí odkaz:
https://doaj.org/article/f7718a9ccfe74cd9b395e6317b2bc707
Publikováno v:
Neurobiology of Disease, Vol 30, Iss 2, Pp 174-185 (2008)
Cortical neurons deprived of serum undergo apoptosis that is sensitive to inhibitors of macromolecule synthesis. Proteomic analysis revealed differential expression of 49 proteins in cortical neurons 8 h after serum deprivation. Tissue inhibitor of m
Externí odkaz:
https://doaj.org/article/d7f5dee3a5c14eee9a7bc040a668172b
Autor:
Jaehong Suh, Mary K. Oram, Scott P. Herrick, Wilma Wasco, Kristina Mullin, Donna M. Romano, Jeremy D. Schmahmann, Mark W. Albers, Rudolph E. Tanzi, Basavaraj Hooli
Publikováno v:
SSRN Electronic Journal.
Expansion of CAG trinucleotide repeats in the Ataxin-1 gene (ATXN1) causes spinocerebellar ataxia type 1 (SCA1), a neurodegenerative disease that impairs coordinated movement and cognitive functions. ATXN1 is associated with genetic risk for Alzheime
Autor:
Britt A. DiMarzio, Volodymyr Dzhala, Donna M. Romano, Jun Seok Bae, Scott P. Herrick, Wilma Wasco, Mark W. Albers, Rudolph E. Tanzi, Huda Y. Zoghbi, Kristina Mullin, Mary K. Oram, Jeremy D. Schmahmann, Yuejiao Zheng, Jaehong Suh, Basavaraj Hooli, Larissa Nitschke, Vincenzo A. Gennarino
Publikováno v:
Cell
Summary Expansion of CAG trinucleotide repeats in ATXN1 causes spinocerebellar ataxia type 1 (SCA1), a neurodegenerative disease that impairs coordination and cognition. While ATXN1 is associated with increased Alzheimer’s disease (AD) risk, CAG re
Autor:
Se Hoon Choi, Andrea N. Lesinski, Jaehong Suh, Donna M. Romano, Doo Yeon Kim, Rudolph E. Tanzi, Moira A. Gannon
Publikováno v:
Neuron. 80(2):385-401
SummaryThe generation of Aβ, the main component of senile plaques in Alzheimer’s disease (AD), is precluded by α-secretase cleavage within the Aβ domain of the amyloid precursor protein (APP). We identified two rare mutations (Q170H and R181G) i
Publikováno v:
Human molecular genetics. 25(12)
Extracellular deposition of amyloid-beta (Aβ) peptide, a metabolite of sequential cleavage of amyloid precursor protein (APP), is a critical step in the pathogenesis of Alzheimer's disease (AD). While death-associated protein kinase 1 (DAPK1) is hig
Publikováno v:
Journal of Neurochemistry. 119:377-388
Amyloid precursor protein (APP) family members and their proteolytic products are implicated in normal nervous system function and Alzheimer's disease pathogenesis. APP processing and Aβ secretion are regulated by neuronal activity. Various data sug
Publikováno v:
Neurobiology of Disease, Vol 30, Iss 2, Pp 174-185 (2008)
Cortical neurons deprived of serum undergo apoptosis that is sensitive to inhibitors of macromolecule synthesis. Proteomic analysis revealed differential expression of 49 proteins in cortical neurons 8 h after serum deprivation. Tissue inhibitor of m
Publikováno v:
Journal of Neurochemistry. 95:684-694
Evidence has accumulated showing that pharmacological inhibition of proteasome activity can both induce and prevent neuronal apoptosis. We tested the hypothesis that these paradoxical effects of proteasome inhibitors depend on the degree of reduced p
Publikováno v:
Cancer Letters. 203:91-98
In the present study, we demonstrate the inhibitory effect of 2-acetylaminofluorene (AAF) on interleukin-1beta (IL-1beta) gene expression in lipopolysaccharide (LPS)-stimulated macrophages. Acetylaminofluorene inhibited IL-1 production in LPS-stimula