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anti-Rat (Rattus) ATP13A2 Antikörper:
anti-Human ATP13A2 Antikörper:
anti-Mouse (Murine) ATP13A2 Antikörper:
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Human Polyclonal ATP13A2 Primary Antibody für IHC, SimWes - ABIN188923
Henry, Aghamohammadzadeh, Samaroo, Chen, Mou, Needle, Hirst: Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression. in Human molecular genetics 2015
Show all 2 Pubmed References
Thsi stduy Our findings bring new insight into the biology of ATP13A2 and open novel opportunities for its study using zebrafish as a model organism.
we describe, for the first time, the deleterious effect arising from the interaction between the ATP13A2 familial mutant Dup22 with a-Syn (zeige FYN Antikörper). We show that this ATP13A2 mutant can enhance a-Syn (zeige FYN Antikörper) oligomerization and aggregation in cell culture
ATP13A2 inhibition by hsa (zeige CD24 Antikörper)-miR (zeige MLXIP Antikörper)-4306 efficiently restored manganese-induced cytotoxicity in cultured neurons.
This study demonstrated that loss of ATP13A2 function causes a combination of lysosomal and mitochondrial dysfunction that affects multiple neuronal populations.
The ATP13A2 A746T variant is rare in Han Chinese patients and controls and is not associated with PD susceptibility in this ethnic group.
This study showed that LRRK2 (zeige LRRK2 Antikörper), PARK2 (zeige PARK2 Antikörper) and ATP13A2 are under copy number variations influence in patient with Parkinson disease.
tre (zeige TREH Antikörper) results of this study suggests that the expression of ATP13A2 regulated by the PHD2 (zeige EGLN1 Antikörper)-HIF1alpha (zeige HIF1A Antikörper) signaling pathway,and this is instrumental in maintaining cellular iron homeostasis and cell viability in mitochondrially compromised DAergic neurons.
that ATP13A2 contains a unique N-terminal hydrophobic extension that lies on the cytosolic membrane surface of the lysosome, where it interacts with the lysosomal signaling lipids phosphatidic acid and phosphatidylinositol(3,5)bisphosphate.
ATP13A2 overexpression improves the lysosome membrane integrity and protects against iron-induced cell damage.
A review of recent advances in the emerging association of ATP13A2 mutations with Parkinsonism and neuronal ceroid lipofuscinoses.
The mutation rates of Thr12Met and Ala1144Thr of ATP13A2 in the Uygur and Han Parkinson's disease patients in the Xinjiang region are low.
the loss of Atp13a2 causes sensorimotor impairments, alpha-synuclein (zeige SNCA Antikörper) accumulation as occurs in PD and related synucleinopathies, and accumulation of lipofuscin deposits characteristic of NCL (zeige NCL Antikörper)
study reveals a number of intriguing neuronal phenotypes due to the loss- or gain-of-function of ATP13A2 that support a role for this protein in regulating intracellular cation homeostasis and neuronal integrity
This study showed that ATP13A2 regulates mitochondrial bioenergetics through macroautophagy.
This gene encodes a member of the P5 subfamily of ATPases which transports inorganic cations as well as other substrates. Mutations in this gene are associated with Kufor-Rakeb syndrome (KRS), also referred to as Parkinson disease 9. Multiple transcript variants encoding different isoforms have been found for this gene.
probable cation-transporting ATPase 13A2
, ATPase type 13A2
, probable cation-transporting ATPase 13A2-like
, putative ATPase