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GBA2 encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Zusätzlich bieten wir Ihnen GBA2 Proteine (5) und und viele weitere Produktgruppen zu diesem Protein an.
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These results provide a foundation for the use of zebrafish in screening GBA2-targeting molecules, and for wider studies investigating GBA2 biology.
GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.
sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity.
GBA2 is particularly abundant in Purkinje cells (PCs), one of the most affected neuronal populations in NPC (zeige NPC1 Antikörper) disease.
glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane. Similar cytoskeletal defects were observed in male germ and Sertoli cells from GBA2 knockout-mice.
the deletion of Gba2 significantly rescues the type 1 Gaucher disease clinical phenotype.
redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.
GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.
The repression of IL-6 (zeige IL6 Antikörper)/STAT3 (zeige STAT3 Antikörper) signalling pathway seems to be one of the mechanisms for the delay of liver regeneration in GBA2-deficient mice.
GBA1 (zeige GBA Antikörper) and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples.
The coiled-coil structure of LIMP-2 (zeige SCARB2 Antikörper) is required for its interaction with beta-glucocerebrosidase (zeige GBA Antikörper).
L-type calcium channel blockers have the ex vivo effects of increasing GCase (zeige GBA Antikörper) activity and protein in mouse fibroblasts
Our protocol showed high specificity and sensitivity for homozygosity detection and facilitated the identification of novel mutations in GAN (zeige GAN Antikörper), GBA2, and ZFYVE26 (zeige ZFYVE26 Antikörper) in four families affected by hereditary spastic paraplegia or Charcot-Marie-Tooth disease
GBA (zeige GBA Antikörper) mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology.
GBA2 mutations causing a Marinesco-Sjogren-like syndrome in two Norwegian families, are reported.
Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2
Spastic paraplegia/cerebellar ataxia patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount.
The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis
Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia: GBA2, TGM6 (zeige TGM5 Antikörper), ANO10 (zeige ANO10 Antikörper) and SYT14 (zeige SYT14 Antikörper)
We hereby report a novel GBA2 mutation associated with spastic ataxia and suggest that GBA2 mutations may be a relatively frequent cause of autosomal recessive cerebellar ataxias.
observations make GBA2 a likely candidate to be involved in Gaucher disease etiology.
This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.
bile acid beta-glucosidase
, talin 1
, glucosidase, beta (bile acid) 2
, non-lysosomal glucosylceramidase-like
, beta-glucocerebrosidase 2
, beta-glucosidase 2
, bile acid
, glucosylceramidase 2
, non-lysosomal glucosylceramidase