Results 11 to 20 of about 3,929 (211)

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).
Glucosylceramidase, H. Overkleeft, G. Renkema, Jolanda M. Neele, Paula Vianello, Irene O. Hung, A. Strijland, Alida M. van der Burg, G. Koomen, U. Pandit, J. Aerts   +10 more
semanticscholar   +11 more sources

Glucosylceramidase Maintains Influenza Virus Infection by Regulating Endocytosis [PDF]

Journal of Virology, 2019
Influenza virus is the pathogen responsible for the second largest pandemic in human history. A better understanding of how influenza virus enters host cells may lead to the development of more-efficacious therapies against emerging strains of the virus.
Kelly Drews, Michael P Calgi, W. Harrison, Camille M Drews, Pedro Costa-Pinheiro, Jeremy J P Shaw, Kendra A Jobe, Elizabeth A. Nelson, John D Han, T. Fox, J. White, M. Kester   +11 more
semanticscholar   +3 more sources

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

International Journal of Molecular Sciences, 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
Julia Aguilera-Herce, Concepción Panadero-Medianero, M. Sánchez-Romero, Roberto Balbontín, Joaquín Bernal-Bayard, F. Ramos-Morales   +5 more
semanticscholar   +5 more sources

Preclinical investigation of artesunate as a therapeutic agent for hepatocellular carcinoma via impairment of glucosylceramidase-mediated autophagic degradation

Experimental & Molecular Medicine, 2022
Artesunate (ART) has been indicated as a candidate drug for hepatocellular carcinoma (HCC). Glucosylceramidase (GBA) is required for autophagic degradation. Whether ART regulates autophagic flux by targeting GBA in HCC remains to be defined.
Wenjia Chen, Zhaochen Ma, Lingxiang Yu, Xia Mao, Nan Ma, Xiaodong Guo, Xiaoli Yin, Funeng Jiang, Qian Wang, Jigang Wang, M. Fang, Na Lin, Yanqiong Zhang   +12 more
semanticscholar   +3 more sources

Identification of the Non-lysosomal Glucosylceramidase as β-Glucosidase 2* [PDF]

Journal of Biological Chemistry, 2007
The primary catabolic pathway for glucosylceramide is catalyzed by the lysosomal enzyme glucocerebrosidase that is defective in Gaucher disease patients.
R. Boot, M. Verhoek, W. Donker‐Koopman, A. Strijland, J. van Marle, H. Overkleeft, T. Wennekes, J. Aerts   +7 more
semanticscholar   +5 more sources

Interaction of saposins, acidic lipids, and glucosylceramidase.

Journal of Biological Chemistry, 1990
Activity of lysosomal glucosylceramidase is stimulated by two small glycoproteins, saposin A and C, which are, together with two other similar glycoproteins, derived from a single precursor protein.
S. Morimoto, Y. Kishimoto, J. Tomich, S. Weiler, T. Ohashi, J. Barranger, K. Kretz, J. O'brien   +7 more
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 ...
M. Woeste, Sina Stern, Diana N Raju, E. Grahn, Dominik Dittmann, K. Gutbrod, P. Dörmann, J. N. Hansen, Sophie Schonauer, Carina E. Marx, Hussein Hamzeh, H. Körschen, J. Aerts, W. Bönigk, H. Endepols, R. Sandhoff, M. Geyer, Thomas K Berger, F. Bradke, D. Wachten   +19 more
semanticscholar   +6 more sources

Molecular Basis of Reduced Glucosylceramidase Activity in the Most Common Gaucher Disease Mutant, N370S [PDF]

Journal of Biological Chemistry, 2010
Gaucher disease is caused by the defective activity of the lysosomal hydrolase, glucosylceramidase. Although the x-ray structure of wild type glucosylceramidase has been resolved, little is known about the structural features of any of the >200 mutations.
Marc N. Offman, M. Król, I. Silman, J. Sussman, A. Futerman   +4 more
semanticscholar   +3 more sources

Biodistribution of AAV1, AAV5, AAV9, and AAVDJ serotypes after intra-cisterna magna delivery in non-human primates [PDF]

Molecular Therapy: Methods & Clinical Development
Delivering drugs effectively to the central nervous system (CNS) is a major challenge in drug development, including adeno-associated virus (AAV) gene therapy.
Takuro Okai, Sho Sato, Hironobu Yasuno, Miyu Nakayama, Syunsuke Yamamoto, Sebastian Sjöqvist, Kentaro Otake, Masato Nakashima, Mugdha Deshpande, Elizabeth Galbreath, Jeong-Ho Oak, Saku Miyamoto, Gabriele Proetzel   +12 more
doaj   +2 more sources

A Fluorescence Polarization Activity-Based Protein Profiling Assay in the Discovery of Potent, Selective Inhibitors for Human Nonlysosomal Glucosylceramidase [PDF]

Journal of the American Chemical Society, 2017
Human nonlysosomal glucosylceramidase (GBA2) is one of several enzymes that controls levels of glycolipids and whose activity is linked to several human disease states.
Daniel Lahav, Bing Liu, R. J. van den Berg, A. M. V. D. van den Nieuwendijk, T. Wennekes, Amar B. T. Ghisaidoobe, I. Breen, M. Ferraz, C. Kuo, Liang Wu, P. Geurink, H. Ovaa, G. A. van der Marel, Mario van der Stelt, R. Boot, G. Davies, J. Aerts, H. Overkleeft   +17 more
semanticscholar   +7 more sources