PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33802460-2 2021 Similar to Gaucher disease (GD), patients deficient in glucocerebrosidase (GCase) degrading GlcCer, NPC patients show an elevated glucosylsphingosine and glucosylated cholesterol. Glucosylceramides 92-98 glucosidase, beta, acid Mus musculus 75-80 34509608-2 2021 GCase metabolizes the glycosphingolipids glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph). Glucosylceramides 41-57 glucosidase, beta, acid Mus musculus 0-5 34509608-2 2021 GCase metabolizes the glycosphingolipids glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph). Glucosylceramides 59-65 glucosidase, beta, acid Mus musculus 0-5 32144204-1 2020 beta-Glucocerebrosidase (GBA) hydrolyzes glucosylceramide (GlcCer) to generate ceramide. Glucosylceramides 41-57 glucosidase, beta, acid Mus musculus 25-28 34622801-3 2021 We developed an efficient strategy to screen for modulators of beta-glucocerebrosidase (GCase), a lysosomal enzyme that exhibits decreased activity in patients with PD, leading to accumulation of the substrate glucosylceramide and oxidized dopamine and alpha-synuclein, which contribute to PD pathogenesis. Glucosylceramides 210-226 glucosidase, beta, acid Mus musculus 88-93 34458595-1 2021 The acid beta-glucocerebrosidase (GCase) enzyme cleaves glucosylceramide into glucose and ceramide. Glucosylceramides 56-72 glucosidase, beta, acid Mus musculus 9-32 34458595-1 2021 The acid beta-glucocerebrosidase (GCase) enzyme cleaves glucosylceramide into glucose and ceramide. Glucosylceramides 56-72 glucosidase, beta, acid Mus musculus 34-39 34106956-1 2021 Multiple mutations have been described in the human GBA1 gene, which encodes the lysosomal enzyme beta-glucocerebrosidase (GCase) that degrades glucosylceramide and is pivotal in glycosphingolipid substrate metabolism. Glucosylceramides 144-160 glucosidase, beta, acid Mus musculus 123-128 33152398-4 2021 Gba-/-;Gbatg mice, which contain a Gba transgene regulated by doxycycline, accumulate moderate levels of the offending substrate in GD, glucosylceramide, and live for up to 10 months, i.e. significantly longer than mice which model type 2 GD. Glucosylceramides 136-152 glucosidase, beta, acid Mus musculus 0-3 33152398-4 2021 Gba-/-;Gbatg mice, which contain a Gba transgene regulated by doxycycline, accumulate moderate levels of the offending substrate in GD, glucosylceramide, and live for up to 10 months, i.e. significantly longer than mice which model type 2 GD. Glucosylceramides 136-152 glucosidase, beta, acid Mus musculus 7-10 34686711-4 2021 Here, we aim to alleviate the lipid storage burden by inhibiting the de novo synthesis of the primary glycosphingolipid substrate of GCase, glucosylceramide (GlcCer). Glucosylceramides 140-156 glucosidase, beta, acid Mus musculus 133-138 34686711-4 2021 Here, we aim to alleviate the lipid storage burden by inhibiting the de novo synthesis of the primary glycosphingolipid substrate of GCase, glucosylceramide (GlcCer). Glucosylceramides 158-164 glucosidase, beta, acid Mus musculus 133-138 33189821-8 2020 Also, the levels of acid ceramidase (Asah1) and glucocerebrosidase (Gba)-lysosomal enzymes involved in the hydrolysis of glucosylceramides-were consistently elevated in the lungs after CS exposure. Glucosylceramides 121-138 glucosidase, beta, acid Mus musculus 48-66 33189821-8 2020 Also, the levels of acid ceramidase (Asah1) and glucocerebrosidase (Gba)-lysosomal enzymes involved in the hydrolysis of glucosylceramides-were consistently elevated in the lungs after CS exposure. Glucosylceramides 121-138 glucosidase, beta, acid Mus musculus 68-71 32144204-1 2020 beta-Glucocerebrosidase (GBA) hydrolyzes glucosylceramide (GlcCer) to generate ceramide. Glucosylceramides 41-57 glucosidase, beta, acid Mus musculus 0-23 32144204-1 2020 beta-Glucocerebrosidase (GBA) hydrolyzes glucosylceramide (GlcCer) to generate ceramide. Glucosylceramides 59-65 glucosidase, beta, acid Mus musculus 0-23 32144204-1 2020 beta-Glucocerebrosidase (GBA) hydrolyzes glucosylceramide (GlcCer) to generate ceramide. Glucosylceramides 59-65 glucosidase, beta, acid Mus musculus 25-28 32144204-2 2020 Previously, we demonstrated that lysosomal GBA1 and non-lysosomal GBA2 possess not only GlcCer hydrolase activity, but also transglucosylation activity to transfer the glucose residue from GlcCer to cholesterol to form beta-cholesterylglucoside (beta-GlcChol) in vitro beta-GlcChol is a member of sterylglycosides present in diverse species. Glucosylceramides 88-94 glucosidase, beta, acid Mus musculus 43-47 31660434-7 2019 An enhanced Gba1 activity elevates ceramide levels responsible for apoptosis and decreases glucosylceramides to overcome drug resistance. Glucosylceramides 91-108 glucosidase, beta, acid Mus musculus 12-16 28225753-2 2017 GBA1 mutations drive extensive accumulation of glucosylceramide (GC) in multiple innate and adaptive immune cells in the spleen, liver, lung and bone marrow, often leading to chronic inflammation. Glucosylceramides 47-63 glucosidase, beta, acid Mus musculus 0-4 31447678-4 2019 Glucosylceramide is the main precursor of complex glycosphingolipids that is degraded by lysosomal (GBA1) or non-lysosomal (GBA2) glucocerebrosidase. Glucosylceramides 0-16 glucosidase, beta, acid Mus musculus 100-104 31447678-4 2019 Glucosylceramide is the main precursor of complex glycosphingolipids that is degraded by lysosomal (GBA1) or non-lysosomal (GBA2) glucocerebrosidase. Glucosylceramides 0-16 glucosidase, beta, acid Mus musculus 130-148 30578288-1 2019 Gaucher disease (GD) is a rare lysosomal storage disorder caused by mutations in the GBA1 gene, encoding the lysosome-resident glucocerebrosidase enzyme involved in the hydrolysis of glucosylceramide. Glucosylceramides 183-199 glucosidase, beta, acid Mus musculus 127-145 28686011-2 2017 Reduced GCase activity primarily leads to the accumulation of two substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph). Glucosylceramides 78-94 glucosidase, beta, acid Mus musculus 8-13 28686011-2 2017 Reduced GCase activity primarily leads to the accumulation of two substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph). Glucosylceramides 96-102 glucosidase, beta, acid Mus musculus 8-13 28485919-1 2017 Glucocerebrosidase (GBA) is a lysosomal beta-glucosidase that degrades glucosylceramide. Glucosylceramides 71-87 glucosidase, beta, acid Mus musculus 0-18 28485919-1 2017 Glucocerebrosidase (GBA) is a lysosomal beta-glucosidase that degrades glucosylceramide. Glucosylceramides 71-87 glucosidase, beta, acid Mus musculus 20-23 30689867-7 2019 Dm mice showed an increased level of glucosylsphingosine without any noticeable accumulation of glucosylceramide, a direct substrate of GBA. Glucosylceramides 96-112 glucosidase, beta, acid Mus musculus 136-139 29900534-3 2019 Gaucher disease is caused by the loss of activity of glucocerebrosidase, leading to accumulation of glucosylceramide. Glucosylceramides 100-116 glucosidase, beta, acid Mus musculus 53-71 30600575-1 2019 Glucocerebrosidase (GBA) is a lysosomal beta-glucosidase-degrading glucosylceramide. Glucosylceramides 67-83 glucosidase, beta, acid Mus musculus 0-18 30600575-1 2019 Glucocerebrosidase (GBA) is a lysosomal beta-glucosidase-degrading glucosylceramide. Glucosylceramides 67-83 glucosidase, beta, acid Mus musculus 20-23 28225753-2 2017 GBA1 mutations drive extensive accumulation of glucosylceramide (GC) in multiple innate and adaptive immune cells in the spleen, liver, lung and bone marrow, often leading to chronic inflammation. Glucosylceramides 65-67 glucosidase, beta, acid Mus musculus 0-4 27539321-4 2016 In particular, heterozygous mutations in the gene encoding for glucocerebrosidase (GBA1), a lysosomal enzyme converting glucosyl-ceramides (Glc-Cer) into Cer, increase the risk of developing PD. Glucosylceramides 120-138 glucosidase, beta, acid Mus musculus 63-81 28933411-7 2016 Decreased catalytic activity and/or instability of GCase leads to accumulation of glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in the lysosomes of macrophage cells and visceral organs. Glucosylceramides 82-98 glucosidase, beta, acid Mus musculus 51-56 28933411-7 2016 Decreased catalytic activity and/or instability of GCase leads to accumulation of glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in the lysosomes of macrophage cells and visceral organs. Glucosylceramides 100-106 glucosidase, beta, acid Mus musculus 51-56 27539321-4 2016 In particular, heterozygous mutations in the gene encoding for glucocerebrosidase (GBA1), a lysosomal enzyme converting glucosyl-ceramides (Glc-Cer) into Cer, increase the risk of developing PD. Glucosylceramides 120-138 glucosidase, beta, acid Mus musculus 83-87 24064337-2 2014 Gaucher disease is caused by the defective activity of the lysosomal enzyme, glucocerebrosidase (GCase; GBA1), resulting in intracellular accumulation of the glycosphingolipids, glucosylceramide and psychosine. Glucosylceramides 178-194 glucosidase, beta, acid Mus musculus 77-95 27482815-1 2016 Glucocerebrosidase is a lysosomal hydrolase involved in the breakdown of glucosylceramide. Glucosylceramides 73-89 glucosidase, beta, acid Mus musculus 0-18 26420838-1 2015 Defective lysosomal acid beta-glucosidase (GCase) in Gaucher disease causes accumulation of glucosylceramide (GC) and glucosylsphingosine (GS) that distress cellular functions. Glucosylceramides 92-108 glucosidase, beta, acid Mus musculus 43-48 26312487-2 2015 GBA1 cleaves glucosylceramide to form ceramide, an established bioactive lipid, and defects in GBA1 lead to aberrant accumulation in glucosylceramide and insufficient formation of ceramide. Glucosylceramides 13-29 glucosidase, beta, acid Mus musculus 0-4 26312487-2 2015 GBA1 cleaves glucosylceramide to form ceramide, an established bioactive lipid, and defects in GBA1 lead to aberrant accumulation in glucosylceramide and insufficient formation of ceramide. Glucosylceramides 133-149 glucosidase, beta, acid Mus musculus 0-4 26312487-2 2015 GBA1 cleaves glucosylceramide to form ceramide, an established bioactive lipid, and defects in GBA1 lead to aberrant accumulation in glucosylceramide and insufficient formation of ceramide. Glucosylceramides 133-149 glucosidase, beta, acid Mus musculus 95-99 25996484-3 2015 GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. Glucosylceramides 76-92 glucosidase, beta, acid Mus musculus 0-4 25996484-3 2015 GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. Glucosylceramides 76-92 glucosidase, beta, acid Mus musculus 0-3 25996484-3 2015 GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. Glucosylceramides 94-96 glucosidase, beta, acid Mus musculus 0-4 25996484-3 2015 GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. Glucosylceramides 94-96 glucosidase, beta, acid Mus musculus 0-3 26094487-2 2015 GBA1 encodes for the lysosomal hydrolase glucocerebrosidase and reductions in this enzyme result in the accumulation of the glycolipid substrates glucosylceramide and glucosylsphingosine. Glucosylceramides 146-162 glucosidase, beta, acid Mus musculus 0-4 26094487-2 2015 GBA1 encodes for the lysosomal hydrolase glucocerebrosidase and reductions in this enzyme result in the accumulation of the glycolipid substrates glucosylceramide and glucosylsphingosine. Glucosylceramides 146-162 glucosidase, beta, acid Mus musculus 41-59 26275242-1 2015 The enzyme glucocerebrosidase (GBA) hydrolyses glucosylceramide (GlcCer) in lysosomes. Glucosylceramides 47-63 glucosidase, beta, acid Mus musculus 11-29 26275242-1 2015 The enzyme glucocerebrosidase (GBA) hydrolyses glucosylceramide (GlcCer) in lysosomes. Glucosylceramides 47-63 glucosidase, beta, acid Mus musculus 31-34 26275242-1 2015 The enzyme glucocerebrosidase (GBA) hydrolyses glucosylceramide (GlcCer) in lysosomes. Glucosylceramides 65-71 glucosidase, beta, acid Mus musculus 11-29 26275242-1 2015 The enzyme glucocerebrosidase (GBA) hydrolyses glucosylceramide (GlcCer) in lysosomes. Glucosylceramides 65-71 glucosidase, beta, acid Mus musculus 31-34 25551612-1 2014 Gaucher disease is a lysosomal storage disease caused by defective activity of acid beta-glucosidase (GCase), which leads to the accumulation of its major substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in many cells. Glucosylceramides 167-183 glucosidase, beta, acid Mus musculus 84-100 25551612-1 2014 Gaucher disease is a lysosomal storage disease caused by defective activity of acid beta-glucosidase (GCase), which leads to the accumulation of its major substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in many cells. Glucosylceramides 167-183 glucosidase, beta, acid Mus musculus 102-107 25551612-1 2014 Gaucher disease is a lysosomal storage disease caused by defective activity of acid beta-glucosidase (GCase), which leads to the accumulation of its major substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in many cells. Glucosylceramides 185-191 glucosidase, beta, acid Mus musculus 84-100 25551612-1 2014 Gaucher disease is a lysosomal storage disease caused by defective activity of acid beta-glucosidase (GCase), which leads to the accumulation of its major substrates, glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in many cells. Glucosylceramides 185-191 glucosidase, beta, acid Mus musculus 102-107 25551612-5 2014 GCStg/Gba1 mice showed 2-3 fold increases in tissue GCS activity as well as accelerated GlcCer accumulation and the appearance of lipid-laden CD68 positive macrophages in visceral organs. Glucosylceramides 88-94 glucosidase, beta, acid Mus musculus 6-10 24064337-2 2014 Gaucher disease is caused by the defective activity of the lysosomal enzyme, glucocerebrosidase (GCase; GBA1), resulting in intracellular accumulation of the glycosphingolipids, glucosylceramide and psychosine. Glucosylceramides 178-194 glucosidase, beta, acid Mus musculus 97-102 24064337-2 2014 Gaucher disease is caused by the defective activity of the lysosomal enzyme, glucocerebrosidase (GCase; GBA1), resulting in intracellular accumulation of the glycosphingolipids, glucosylceramide and psychosine. Glucosylceramides 178-194 glucosidase, beta, acid Mus musculus 104-108 24070122-11 2013 GlcCer levels in the spleen from Gba1/Gba2 knockout mice were much higher than the sum of the single knockouts, indicating a cross-talk between the two glucosylceramidases and suggesting a partially compensation of the loss of one enzyme by the other. Glucosylceramides 0-6 glucosidase, beta, acid Mus musculus 33-37 23880767-6 2013 Compared with the well characterized impact of CBE on the lysosomal glucosylceramide-degrading enzyme (glucocerebrosidase, GBA), CBE inactivated GBA2 less efficiently, due to a lower affinity for this enzyme (higher KI) and a lower rate of enzyme inactivation (k(inact)). Glucosylceramides 68-84 glucosidase, beta, acid Mus musculus 103-121 23880767-6 2013 Compared with the well characterized impact of CBE on the lysosomal glucosylceramide-degrading enzyme (glucocerebrosidase, GBA), CBE inactivated GBA2 less efficiently, due to a lower affinity for this enzyme (higher KI) and a lower rate of enzyme inactivation (k(inact)). Glucosylceramides 68-84 glucosidase, beta, acid Mus musculus 123-126 10196186-2 1999 Ceramides, the major components of these multilayered membranes, derive in large part from hydrolysis of glucosylceramides mediated by stratum corneum beta-glucocerebrosidase (beta-GlcCerase). Glucosylceramides 105-122 glucosidase, beta, acid Mus musculus 151-174 22659419-2 2012 Beta-glucosidase 1 (GBA1; lysosomal glucocerebrosidase) and beta-glucosidase 2 (GBA2, non-lysosomal glucocerebrosidase) both have glucosylceramide as a main natural substrate. Glucosylceramides 130-146 glucosidase, beta, acid Mus musculus 20-24 22659419-5 2012 Given that GBA2 hydrolyses both BG and glucosylceramide, it was asked whether vice versa GBA1 hydrolyses both glucosylceramide and BG. Glucosylceramides 110-126 glucosidase, beta, acid Mus musculus 89-93 20015957-2 2010 The few patients with saposin C deficiency develop a Gaucher disease-like central nervous system (CNS) phenotype attributed to diminished glucosylceramide (GC) cleavage activity by acid beta-glucosidase (GCase). Glucosylceramides 138-154 glucosidase, beta, acid Mus musculus 204-209 20015957-2 2010 The few patients with saposin C deficiency develop a Gaucher disease-like central nervous system (CNS) phenotype attributed to diminished glucosylceramide (GC) cleavage activity by acid beta-glucosidase (GCase). Glucosylceramides 156-158 glucosidase, beta, acid Mus musculus 186-202 12126932-1 2002 Saposin C is a biological activator of acid beta-glucosidase (GCase), the lysosomal hydrolase with activity towards glucosylceramide (GC). Glucosylceramides 116-132 glucosidase, beta, acid Mus musculus 44-60 12126932-1 2002 Saposin C is a biological activator of acid beta-glucosidase (GCase), the lysosomal hydrolase with activity towards glucosylceramide (GC). Glucosylceramides 116-132 glucosidase, beta, acid Mus musculus 62-67 12126932-1 2002 Saposin C is a biological activator of acid beta-glucosidase (GCase), the lysosomal hydrolase with activity towards glucosylceramide (GC). Glucosylceramides 62-64 glucosidase, beta, acid Mus musculus 44-60 11749048-1 2001 The hydrolysis of glucosylceramide (GC) to ceramide and glucose requires the action of the lysosomal enzyme, acid beta-glucosidase (GCase), encoded by gba in the mouse. Glucosylceramides 18-34 glucosidase, beta, acid Mus musculus 132-137 11749048-1 2001 The hydrolysis of glucosylceramide (GC) to ceramide and glucose requires the action of the lysosomal enzyme, acid beta-glucosidase (GCase), encoded by gba in the mouse. Glucosylceramides 18-34 glucosidase, beta, acid Mus musculus 151-154 11749048-1 2001 The hydrolysis of glucosylceramide (GC) to ceramide and glucose requires the action of the lysosomal enzyme, acid beta-glucosidase (GCase), encoded by gba in the mouse. Glucosylceramides 36-38 glucosidase, beta, acid Mus musculus 132-137 11749048-1 2001 The hydrolysis of glucosylceramide (GC) to ceramide and glucose requires the action of the lysosomal enzyme, acid beta-glucosidase (GCase), encoded by gba in the mouse. Glucosylceramides 36-38 glucosidase, beta, acid Mus musculus 151-154 23377801-8 2013 Glucosylceramide (GlcCer), the GCase substrate, influenced formation of purified a-syn by stabilizing soluble oligomeric intermediates. Glucosylceramides 18-24 glucosidase, beta, acid Mus musculus 31-36 23520473-1 2013 Gaucher disease results from GBA1 mutations that lead to defective acid beta-glucosidase (GCase) mediated cleavage of glucosylceramide (GC) and glucosylsphingosine as well as heterogeneous manifestations in the viscera and CNS. Glucosylceramides 118-134 glucosidase, beta, acid Mus musculus 29-33 23520473-1 2013 Gaucher disease results from GBA1 mutations that lead to defective acid beta-glucosidase (GCase) mediated cleavage of glucosylceramide (GC) and glucosylsphingosine as well as heterogeneous manifestations in the viscera and CNS. Glucosylceramides 118-134 glucosidase, beta, acid Mus musculus 72-88 23520473-1 2013 Gaucher disease results from GBA1 mutations that lead to defective acid beta-glucosidase (GCase) mediated cleavage of glucosylceramide (GC) and glucosylsphingosine as well as heterogeneous manifestations in the viscera and CNS. Glucosylceramides 118-134 glucosidase, beta, acid Mus musculus 90-95 23520473-1 2013 Gaucher disease results from GBA1 mutations that lead to defective acid beta-glucosidase (GCase) mediated cleavage of glucosylceramide (GC) and glucosylsphingosine as well as heterogeneous manifestations in the viscera and CNS. Glucosylceramides 90-92 glucosidase, beta, acid Mus musculus 29-33 23520473-1 2013 Gaucher disease results from GBA1 mutations that lead to defective acid beta-glucosidase (GCase) mediated cleavage of glucosylceramide (GC) and glucosylsphingosine as well as heterogeneous manifestations in the viscera and CNS. Glucosylceramides 90-92 glucosidase, beta, acid Mus musculus 72-88 22595426-1 2012 Gaucher disease is a lysosomal storage disease resulting from insufficient acid beta-glucosidase (glucocerebrosidase, GCase, EC 4.2.1.25) activity and the resultant accumulation of glucosylceramide. Glucosylceramides 181-197 glucosidase, beta, acid Mus musculus 118-123 22566609-1 2012 Gaucher"s disease, the most common lysosomal storage disorder, is caused by the defective activity of glucocerebrosidase, the lysosomal hydrolase that degrades glucosylceramide. Glucosylceramides 160-176 glucosidase, beta, acid Mus musculus 102-120 21257328-8 2011 In a chemically induced GCase deficiency, alpha-synuclein aggregates and glucosylceramide accumulation also occurred. Glucosylceramides 73-89 glucosidase, beta, acid Mus musculus 24-29 20962279-1 2010 In nonneuronopathic type 1 Gaucher disease (GD1), mutations in the glucocerebrosidase gene (GBA1) gene result in glucocerebrosidase deficiency and the accumulation of its substrate, glucocerebroside (GL-1), in the lysosomes of mononuclear phagocytes. Glucosylceramides 182-198 glucosidase, beta, acid Mus musculus 67-85 20962279-1 2010 In nonneuronopathic type 1 Gaucher disease (GD1), mutations in the glucocerebrosidase gene (GBA1) gene result in glucocerebrosidase deficiency and the accumulation of its substrate, glucocerebroside (GL-1), in the lysosomes of mononuclear phagocytes. Glucosylceramides 182-198 glucosidase, beta, acid Mus musculus 92-96 20148966-6 2010 IFG incubation also increased the lysosomal trafficking and in situ activity of L444P GCase in intact cells, as measured by reduction in endogenous glucosylceramide levels. Glucosylceramides 148-164 glucosidase, beta, acid Mus musculus 86-91 17080196-6 2006 Recombinant GBA2 hydrolyzed glucosylceramide to glucose and ceramide; the same reaction catalyzed by the beta-glucosidase acid 1 (GBA1) defective in subjects with the Gaucher"s form of lysosomal storage disease. Glucosylceramides 28-44 glucosidase, beta, acid Mus musculus 130-134 16528760-2 2006 The primary manifestation is the accumulation of glucosylceramide (GL-1) in the macrophages of liver and spleen (Gaucher cells), due to a deficiency in the lysosomal hydrolase glucocerebrosidase (GC). Glucosylceramides 49-65 glucosidase, beta, acid Mus musculus 196-198 15912415-0 2005 An accumulation of glucosylceramide in the stratum corneum due to attenuated activity of beta-glucocerebrosidase is associated with the early phase of UVB-induced alteration in cutaneous barrier function. Glucosylceramides 19-35 glucosidase, beta, acid Mus musculus 89-112 12813057-2 2003 In the lysosomal sphingolipid degradation pathway, acid beta-glucosidase (GCase) requires saposin C for optimal in vitro and in vivo hydrolysis of glucocerebroside. Glucosylceramides 147-163 glucosidase, beta, acid Mus musculus 74-79 10037475-2 1999 Incubation of NG108-15 cells with conduritol-B-epoxide, a covalent inhibitor of glucosylceramidase, raised the intracellular concentration of glucosylceramide (GC) by more than fourfold, indicating a glycolipid composition equivalent to that of Gaucher"s cells. Glucosylceramides 142-158 glucosidase, beta, acid Mus musculus 80-98 10214939-2 1999 Ceramides, the main components of these membranes, derive in large part from hydrolysis of glucosylceramides mediated by the lysosomal enzyme beta-glucocerebrosidase. Glucosylceramides 91-108 glucosidase, beta, acid Mus musculus 142-165 10037475-2 1999 Incubation of NG108-15 cells with conduritol-B-epoxide, a covalent inhibitor of glucosylceramidase, raised the intracellular concentration of glucosylceramide (GC) by more than fourfold, indicating a glycolipid composition equivalent to that of Gaucher"s cells. Glucosylceramides 160-162 glucosidase, beta, acid Mus musculus 80-98 7769132-1 1995 Hydrolysis of glucosylceramides (GlcCer) by beta-glucocerebrosidase generates ceramides, critical components of the epidermal permeability barrier. Glucosylceramides 14-31 glucosidase, beta, acid Mus musculus 44-67 7769132-1 1995 Hydrolysis of glucosylceramides (GlcCer) by beta-glucocerebrosidase generates ceramides, critical components of the epidermal permeability barrier. Glucosylceramides 33-39 glucosidase, beta, acid Mus musculus 44-67 8163674-2 1994 Hydrolysis of glucosylceramide by beta-glucocerebrosidase results in ceramide, a critical component of the intercellular lamellae that mediate the epidermal permeability barrier. Glucosylceramides 14-30 glucosidase, beta, acid Mus musculus 34-57