Results 1 to 10 of about 3,930 (214)

Enzyme kinetics and inhibition parameters of human leukocyte glucosylceramidase [PDF]

Heliyon, 2020
Glucosylceramidase (GCase) is a lysosomal enzyme that catalyzes the cleavage of β-glucosidic linkage of glucocerebroside (GC) into glucose and ceramide; thereby, plays an essential function in the degradation of complex lipids and the turnover of ...
Mesut Karatas, Senol Dogan, Emrulla Spahiu, Adna Ašić, Larisa Bešić, Yusuf Turan   +5 more
doaj   +7 more sources

Effect of Expression of Human Glucosylceramidase 2 Isoforms on Lipid Profiles in COS-7 Cells [PDF]

Metabolites, 2020
Glucosylceramide (GlcCer) is a major membrane lipid and the precursor of gangliosides. GlcCer is mainly degraded by two enzymes, lysosomal acid β-glucosidase (GBA) and nonlysosomal β-glucosidase (GBA2), which may have different isoforms because of ...
Peeranat Jatooratthawichot, Chutima Talabnin, Lukana Ngiwsara, Yepy Hardi Rustam, Jisnuson Svasti, Gavin E. Reid, James R. Ketudat Cairns   +6 more
doaj   +9 more sources

Salmonella Type III Secretion Effector SrfJ: A Glucosylceramidase Affecting the Lipidome and the Transcriptome of Mammalian Host Cells. [PDF]

Int J Mol Sci, 2023
Type III secretion systems are found in many Gram-negative pathogens and symbionts of animals and plants. Salmonella enterica has two type III secretion systems associated with virulence, one involved in the invasion of host cells and another involved in
Aguilera-Herce J, Panadero-Medianero C, Sánchez-Romero MA, Balbontín R, Bernal-Bayard J, Ramos-Morales F.   +5 more
europepmc   +8 more sources

A novel class of allosteric glucosylceramidase beta 1 correctors that reduce cellular stress and enhance lysosomal function [PDF]

bioRxiv
Mutations in glucosylceramidase beta 1 (GCase) disrupt the protein’s conformational maturation in the endoplasmic reticulum (ER) and hinder its transport to the lysosome.
Fregno I, Pérez-Carmona N, Rudinskiy M, Soldà T, Bergmann TJ, Ruano A, Delgado A, Cubero E, Bellotto M, García-Collazo AM, Molinari M.   +10 more
europepmc   +4 more sources

Generation of Specific Deoxynojirimycin-type Inhibitors of the Non-lysosomal Glucosylceramidase [PDF]

Journal of Biological Chemistry, 1998
The existence of a non-lysosomal glucosylceramidase in human cells has been documented (van Weely, S., Brandsma, M., Strijland, A., Tager, J. M., and Aerts, J. M. F. G. (1993) Biochim. Biophys. Acta 1181, 55–62).
Herman S. Overkleeft, G. Herma Renkema, Jolanda M. Neele, Paula Vianello, Irene O. Hung, Anneke Strijland, Alida M. van der Burg, Gerrit‐Jan Koomen, Upendra K. Pandit, Johannes M. F. G. Aerts   +9 more
semanticscholar   +13 more sources

Glucosylceramidase Beta (GBA) Genotyping v1

, 2021
This protocol details the steps for GBA genotyping. This protocol has been adapted from the PRoBaND Clinical Consortium (incorporating methods described by Neuman et al., 2009 and Stone et al., 2000) and has been used for all publications for PRoBaND ...
Huw R. Morris, Nigel Williams
semanticscholar   +3 more sources

Species-specific differences in nonlysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations [PDF]

Journal of Biological Chemistry, 2019
The nonlysosomal glucosylceramidase β2 (GBA2) catalyzes the hydrolysis of glucosylceramide to glucose and ceramide. Mutations in the human GBA2 gene have been associated with hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia ...
Marina A. Woeste, Sina Stern, Diana N. Raju, Elena Grahn, Dominik Dittmann, Katharina Gutbrod, Peter Dörmann, Jan N. Hansen, Sophie Schonauer, Carina E. Marx, Hussein Hamzeh, Heinz G. Körschen, Johannes M. F. G. Aerts, Wolfgang Bönigk, Heike Endepols, Roger Sandhoff, Matthias Geyer, Thomas K. Berger, Frank Bradke, Dagmar Wachten   +19 more
semanticscholar   +8 more sources

Reducing GBA2 Activity Ameliorates Neuropathology in Niemann-Pick Type C Mice. [PDF]

PLoS ONE, 2015
The enzyme glucocerebrosidase (GBA) hydrolyses glucosylceramide (GlcCer) in lysosomes. Markedly reduced GBA activity is associated with severe manifestations of Gaucher disease including neurological involvement.
André R A Marques, Jan Aten, Roelof Ottenhoff, Cindy P A A van Roomen, Daniela Herrera Moro, Nike Claessen, María Fernanda Vinueza Veloz, Kuikui Zhou, Zhanmin Lin, Mina Mirzaian, Rolf G Boot, Chris I De Zeeuw, Herman S Overkleeft, Yildiz Yildiz, Johannes M F G Aerts   +14 more
doaj   +23 more sources

Mitochondrial dysfunction in NPC1 ‐deficiency is not rescued by drugs targeting the glucosylceramidase GBA2 and the cholesterol‐binding proteins TSPO and StARD1 [PDF]

FEBS Letters
Niemann–Pick type C disease (NPCD) is a rare neurodegenerative disorder most commonly caused by mutations in the lysosomal protein Niemann–Pick C1 (NPC1), which is implicated in cholesterol export.
Simon Wheeler, Meenakshi Bhardwaj, Victor Kenyon, María Pía Ferraz, Johannes M. F. G. Aerts, Daniel J. Sillence   +5 more
openalex   +2 more sources

Clinical and Dopamine Transporter Imaging Characteristics of Leucine Rich Repeat Kinase 2 (LRRK2) and Glucosylceramidase Beta (GBA) Parkinson's Disease Participants in the Parkinson's Progression Markers Initiative: A Cross‐Sectional Study [PDF]

Movement Disorders, 2020
There are limited data on the phenotypic and dopamine transporter (DAT) imaging characterization of the Parkinson's disease (PD) patients with leucine rich kinase 2 (LRRK2) and glucosylceramidase beta (GBA) mutations.
Tanya Simuni, Michael C. Brumm, Liz Uribe, Chelsea Caspell‐Garcia, Christopher S. Coffey, Andrew Siderowf, Roy N. Alcalay, John Q. Trojanowski, Leslie M. Shaw, John Seibyl, Andrew Singleton, Arthur W. Toga, Doug Galasko, Tatiana Foroud, Kelly Nudelman, Duygu Tosun, Kathleen L. Poston, Daniel Weintraub, Brit Mollenhauer, Caroline M. Tanner, Karl Kieburtz, Lana M. Chahine, Alyssa Reimer, Samantha J. Hutten, Susan Bressman, Kenneth Marek, Parkinson's Progression Markers Initiative Investigators   +26 more
openalex   +2 more sources