排序方式: 共有6条查询结果,搜索用时 15 毫秒
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Antonia Piazzesi Yiru Wang Joshua Jackson Lena Wischhof Viktoria ZeislerDiehl Enzo Scifo Ina Oganezova Thorben Hoffmann Pablo Gmez Martín Fabio Bertan Chester J J Wrobel Frank C Schroeder Dan Ehninger Kristian Hndler Joachim L Schultze Lukas Schreiber Gerhild van EchtenDeckert Pierluigi Nicotera Daniele Bano 《EMBO reports》2022,23(5)
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Hintze Maik Griesing Sebastian Michels Marion Blanck Birgit Wischhof Lena Hartmann Dieter Bano Daniele Franz Thomas 《Mammalian genome》2021,32(1):12-29
Mammalian Genome - We investigated the contribution of apoptosis-inducing factor (AIF), a key regulator of mitochondrial biogenesis, in supporting hair growth. We report that pelage abnormalities... 相似文献
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Lena Wischhof Aasha Adhikari Mrityunjoy Mondal Anaïs Marsal-Cots Jacek Biernat Eva Maria Mandelkow Eckhard Mandelkow Dan Ehninger Pierluigi Nicotera Daniele Bano 《The Journal of biological chemistry》2022,298(4)
Microtubule-associated protein tau is a naturally unfolded protein that can modulate a vast array of physiological processes through direct or indirect binding with molecular partners. Aberrant tau homeostasis has been implicated in the pathogenesis of several neurodegenerative disorders, including Alzheimer’s disease. In this study, we performed an unbiased high-content protein profiling assay by incubating recombinant human tau on microarrays containing thousands of human polypeptides. Among the putative tau-binding partners, we identify SAH hydrolase–like protein 1/inositol 1,4,5-trisphosphate receptor (IP3R)–binding protein (AHCYL1/IRBIT), a member of the SAH hydrolase family and a previously described modulator of IP3R activity. Using coimmunoprecipitation assays, we show that endogenous as well as overexpressed tau can physically interact with AHCYL1/IRBIT in brain tissues and cultured cells. Proximity ligation assay experiments demonstrate that tau overexpression may modify the close localization of AHCYL1/IRBIT to IP3R at the endoplasmic reticulum. Together, our experimental evidence indicates that tau interacts with AHCYL1/IRBIT and potentially modulates AHCYL1/IRBIT function. 相似文献
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Fabio Bertan Lena Wischhof Liudmila Sosulina Manuel Mittag Dennis Dalügge Alessandra Fornarelli Fabrizio Gardoni Elena Marcello Monica Di Luca Martin Fuhrmann Stefan Remy Daniele Bano Pierluigi Nicotera 《Cell death and differentiation》2020,27(12):3354
Dendritic spines are postsynaptic domains that shape structural and functional properties of neurons. Upon neuronal activity, Ca2+ transients trigger signaling cascades that determine the plastic remodeling of dendritic spines, which modulate learning and memory. Here, we study in mice the role of the intracellular Ca2+ channel Ryanodine Receptor 2 (RyR2) in synaptic plasticity and memory formation. We demonstrate that loss of RyR2 in pyramidal neurons of the hippocampus impairs maintenance and activity-evoked structural plasticity of dendritic spines during memory acquisition. Furthermore, post-developmental deletion of RyR2 causes loss of excitatory synapses, dendritic sparsification, overcompensatory excitability, network hyperactivity and disruption of spatially tuned place cells. Altogether, our data underpin RyR2 as a link between spine remodeling, circuitry dysfunction and memory acquisition, which closely resemble pathological mechanisms observed in neurodegenerative disorders.Subject terms: Neuroscience, Neurological disorders 相似文献
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