Results 11 to 20 of about 3,930 (214)

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, William Casey Harrison, Camille M. Drews, Pedro Costa‐Pinheiro, Jeremy J.P. Shaw, Kendra A. Jobe, Elizabeth A. Nelson, John D. Han, Todd E. Fox, Judith M. White, Mark Kester   +11 more
semanticscholar   +4 more sources

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

Journal of Biological Chemistry, 2006
The primary catabolic pathway for glucosylceramide is catalyzed by the lysosomal enzyme glucocerebrosidase that is defective in Gaucher disease patients.
Rolf G. Boot, Marri Verhoek, Wilma E. Donker‐Koopman, Anneke Strijland, Jan van Marle, Herman S. Overkleeft, Tom Wennekes, Johannes M. F. G. Aerts   +7 more
semanticscholar   +7 more sources

Functional and genetic characterization of the non-lysosomal glucosylceramidase 2 as a modifier for Gaucher disease [PDF]

Orphanet Journal of Rare Diseases, 2013
BackgroundGaucher disease (GD) is the most common inherited lysosomal storage disorder in humans, caused by mutations in the gene encoding the lysosomal enzyme glucocerebrosidase (GBA1).
Yildiz Yildiz, Per Hoffmann, S vom Dahl, Bernadette Breiden, Roger Sandhoff, Claus Niederau, Mia Horwitz, Stefan Karlsson, Mirella Filocamo, Deborah Elstein, Michael Beck, Konrad Sandhoff, Eugen Mengel, Maria Camila González, Markus M. Nöthen, Ellen Sidransky, Ari Zimran, Manuel Mattheisen   +17 more
semanticscholar   +8 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, Marcin Król, Israel Silman, Joel L. Sussman, Anthony H. Futerman   +4 more
semanticscholar   +5 more sources

Glucosylceramidase [PDF]

Definitions, 2020
National Cancer Institute
semanticscholar   +3 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.
D. Lahav, Bing Liu, Richard J. B. H. N. van den Berg, Adrianus M. C. H. van den Nieuwendijk, Tom Wennekes, Amar T. Ghisaidoobe, Imogen Breen, María Pía Ferraz, C.J. Kuo, Liang Wu, Paul P. Geurink, Huib Ovaa, Gijsbert A. van der Marel, Mario van der Stelt, Rolf G. Boot, G.J. Davies, Johannes M. F. G. Aerts, Herman S. Overkleeft   +17 more
semanticscholar   +8 more sources

Non-Lysosomal Glucosylceramidase [PDF]

Definitions, 2020
National Cancer Institute
semanticscholar   +3 more sources

Glucosylceramidase Mass and Subcellular Localization Are Modulated by Cholesterol in Niemann-Pick Disease Type C [PDF]

Journal of Biological Chemistry, 2004
Niemann-Pick disease type C (NPC) is characterized by the accumulation of cholesterol and sphingolipids in the late endosomal/lysosomal compartment. The mechanism by which the concentration of sphingolipids such as glucosylceramide is increased in this ...
Rosa Salvioli, Susanna Scarpa, Fiorella Ciaffoni, Massimo Tatti, Carlo Ramoni, Marie T. Vanier, Anna Maria Vaccaro   +6 more
semanticscholar   +6 more sources

Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes [PDF]

FEBS Letters, 1993
The function of saposin C (Sap C), a glucosylceramidase activator protein, in the enzyme stimulation by phosphatidylserine (PS) liposomes has been investigated. Using gel filtration experiments evidence was obtained for Sap C binding to PS large unilamellar vesicles (LUV) but not to glucosylceramidase.
Anna Maria Vaccaro, Massimo Tatti, Fiorella Ciaffoni, Rosa Salvioli, Bruno Maras, Alessandra Barca   +5 more
semanticscholar   +5 more sources

Erratum to: Current and Novel Aspects on the Non-lysosomal β-Glucosylceramidase GBA2 [PDF]

Neurochemical Research, 2016
Massimo Aureli, Maura Samarani, Nicoletta Loberto, Giulia Mancini, Valentina Murdica, Elena Chiricozzi, Alessandro Prinetti, Rosaria Bassi, Sandro Sonnino   +8 more
semanticscholar   +4 more sources