Browsing by Author "Timur, Zehra Kevser"
Now showing items 1-4 of 4
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GM2 ganglioside accumulation causes neuroinflammation and behavioral alterations in a mouse model of early onset Tay-Sachs disease
Demir, Secil Akyildiz; Timur, Zehra Kevser; Ates, Nurselin; Martinez, Luis Alarcon; Seyrantepe, Volkan (BMC, 2020)Background Tay-Sachs disease (TSD), a type of GM2-gangliosidosis, is a progressive neurodegenerative lysosomal storage disorder caused by mutations in the alpha subunit of the lysosomal beta-hexosaminidase enzyme. This ... -
Lysosomal Cathepsin A plays a significant role in the processing of endogenous bioactive peptides
Timur, Zehra Kevser; Akyıldız Demir, Seçil; Seyrantepe, Volkan (Frontiers Media, 2016)Lysosomal serine carboxypeptidase Cathepsin A (CTSA) is a multifunctional enzyme with distinct protective and catalytic function. CTSA present in the lysosomal multienzyme complex to facilitate the correct lysosomal routing, ... -
Murine Sialidase Neu3 facilitates GM2 degradation and bypass in mouse model of Tay-Sachs disease
Seyrantepe, Volkan; Akyıldız Demir, Seçil; Timur, Zehra Kevser; Von Gerichten, Johanna; Marsching, Christian; Erdemli, Esra; Öztaş, Emin; Takahashi, Kohta; Yamaguchi, Kazunori; Ateş, Nurselin; Dönmez Demir, Buket; Dalkara, Turgay; Erich, Katrin; Hopf, Carsten; Sandhoff, Roger; Miyagi, Taeko (Elsevier, 2018-01)Tay-Sachs disease is a severe lysosomal storage disorder caused by mutations in Hexa, the gene that encodes for the α subunit of lysosomal β-hexosaminidase A (HEXA), which converts GM2 to GM3 ganglioside. Unexpectedly, ... -
Neuraminidase-1 contributes significantly to the degradation of neuronal B-series gangliosides but not to the bypass of the catabolic block in Tay-Sachs mouse models
Timur, Zehra Kevser; Akyıldız Demir, Seçil; Marsching, C.; Sandhoff, R.; Seyrantepe, Volkan (Elsevier, 2015-08)TaySachs disease is a severe lysosomal storage disorder caused bymutations in the HEXA gene coding for? subunit of lysosomal β-Hexosaminidase A enzyme, which converts GM2 to GM3 ganglioside. HexA mice, depleted of the ...
