Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Lindsey T. Lelieveld"'
Autor:
Lindsey T. Lelieveld, Sophie Gerhardt, Saskia Maas, Kimberley C. Zwiers, Claire de Wit, Ernst H. Beijk, Maria J. Ferraz, Marta Artola, Annemarie H. Meijer, Christian Tudorache, Daniela Salvatori, Rolf G. Boot, Johannes M.F.G. Aerts
Publikováno v:
Journal of Lipid Research, Vol 63, Iss 5, Pp 100199- (2022)
Abstract: In Gaucher disease (GD), the deficiency of glucocerebrosidase causes lysosomal accumulation of glucosylceramide (GlcCer), which is partly converted by acid ceramidase to glucosylsphingosine (GlcSph) in the lysosome. Chronically elevated blo
Externí odkaz:
https://doaj.org/article/aa3d445ab3fa4e6ca569b196780b716f
Autor:
Lindsey T. Lelieveld, Mina Mirzaian, Chi-Lin Kuo, Marta Artola, Maria J. Ferraz, Remco E.A. Peter, Hisako Akiyama, Peter Greimel, Richard J.B.H.N. van den Berg, Herman S. Overkleeft, Rolf G. Boot, Annemarie H. Meijer, Johannes M.F.G. Aerts
Publikováno v:
Journal of Lipid Research, Vol 60, Iss 11, Pp 1851-1867 (2019)
μ-glucosidases [GBA1 (glucocerebrosidase) and GBA2] are ubiquitous essential enzymes. Lysosomal GBA1 and cytosol-facing GBA2 degrade glucosylceramide (GlcCer); GBA1 deficiency causes Gaucher disease, a lysosomal storage disorder characterized by lys
Externí odkaz:
https://doaj.org/article/05ce0c35bb594489bd17fa37e18c9942
Autor:
Jingwen Fan, Victoria L. Hale, Lindsey T. Lelieveld, Laura J. Whitworth, Elisabeth M. Busch-Nentwich, Mark Troll, Paul H. Edelstein, Timothy M. Cox, Francisco J. Roca, Johannes M. F. G. Aerts, Lalita Ramakrishnan
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Biallelic mutations in the glucocerebrosidase (GBA1) gene cause Gaucher disease, characterized by lysosomal accumulation of glucosylceramide and glucosylsphingosine in macrophages. This and other lysosomal diseases occur with high frequency in Ashken
Autor:
Chi-Lin Kuo, Rolf G. Boot, Marta Artola, Qin Su, Lindsey T. Lelieveld, Marri Verhoek, Sybrin P. Schröder, Maria J. Ferraz, Herman S. Overkleeft, Johannes M. F. G. Aerts
Publikováno v:
Chembiochem
Chembiochem, 22, 1-10. WILEY-V C H VERLAG GMBH
Chembiochem, 22, 1-10. WILEY-V C H VERLAG GMBH
Glucocerebrosidase (GBA), a lysosomal retaining β‐d‐glucosidase, has recently been shown to hydrolyze β‐d‐xylosides and to transxylosylate cholesterol. Genetic defects in GBA cause the lysosomal storage disorder Gaucher disease (GD), and al
Autor:
Martijn J.C. van der Lienden, Lindsey T. Lelieveld, Chi-Lin Kuo, Johannes M. F. G. Aerts, Marta Artola, Herman S. Overkleeft, Daphne E.C. Boer
Publikováno v:
Current Opinion in Chemical Biology
Current Opinion in Chemical Biology, 53, 204-215
Current Opinion in Chemical Biology, 53, 204-215
Glycosphingolipids are important building blocks of the outer leaflet of the cell membrane. They are continuously recycled, involving fragmentation inside lysosomes by glycosidases. Inherited defects in degradation cause lysosomal glycosphingolipid s
Autor:
Marta Artola, Herman S. Overkleeft, Annemarie H. Meijer, Anthony H. Futerman, Lindsey T. Lelieveld, Ayelet Vardi, Iris Zoutendijk, Mina Mirzaian, Wouter W. Kallemeijn, Chi-Lin Kuo, Johannes M. F. G. Aerts, Herman P. Spaink
Publikováno v:
The Febs Journal
FEBS Journal
FEBS Journal, 286(3), 584-600
FEBS Journal
FEBS Journal, 286(3), 584-600
Glucocerebrosidase (GBA) is a lysosomal β‐glucosidase‐degrading glucosylceramide. Its deficiency causes Gaucher disease (GD), a common lysosomal storage disorder. Carrying a genetic abnormality in GBA constitutes at present the largest genetic r
Autor:
Rolf G. Boot, Lindsey T. Lelieveld, Johannes M. F. G. Aerts, Marta Artola, Herman S. Overkleeft, Jeroen D. C. Codée, Rhianna J. Rowland, Gideon J. Davies, Gijsbert A. van der Marel, Chi-Lin Kuo
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 141(10), 4214-4218
Journal of the American Chemical Society, 141(10), 4214-4218
Gaucher disease is caused by inherited deficiency in glucocerebrosidase (GBA, a retaining β-glucosidase), and deficiency in GBA constitutes the largest known genetic risk factor for Parkinson's disease. In the past, animal models of Gaucher disease
Autor:
Annemarie H. Meijer, Johannes M. F. G. Aerts, Mina Mirzaian, Maria J. Ferraz, Richard J. B. H. N. van den Berg, Peter Greimel, Rolf G. Boot, Remco E.A. Peter, Hisako Akiyama, Marta Artola, Lindsey T. Lelieveld, Herman S. Overkleeft, Chi-Lin Kuo
Publikováno v:
Journal of Lipid Research, Vol 60, Iss 11, Pp 1851-1867 (2019)
Journal of Lipid Research, 60, 1851-1867
J Lipid Res
Journal of Lipid Research, 60, 1851-1867
J Lipid Res
β-glucosidases (GBA1 [glucocerebrosidase], GBA2, and GBA3) are ubiquitous, essential enzymes. Lysosomal GBA1 and cytosol-facing GBA2 degrade glucosylceramide (GlcCer); GBA1 deficiency causes Gaucher disease (GD), a lysosomal storage disorder charact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::993aa217a67938ff6fbcec9ed1bc273b
https://hdl.handle.net/1887/80090
https://hdl.handle.net/1887/80090
Autor:
Jan Aten, Maria J. Ferraz, Lindsey T. Lelieveld, Rianne Meijer, Saskia V. Oussoren, Johannes M. F. G. Aerts, Rolf G. Boot, André R. A. Marques, Daphne E.C. Boer, Mina Mirzaian, Chi-Lin Kuo, Daniela H.M. Chao, Kassiani Kytidou, Marc D. Hazeu, Marco van Eijk, Herman S. Overkleeft, Paulo Gaspar, Tanit L. Gabriel, Patrick Wisse, Martijn J.C. van der Lienden
Publikováno v:
eLS
The cellular recycling of glycosphingolipids (GSLs) is mediated by specific lysosomal glycosidases. Inherited deficiencies in these enzymes cause lysosomal storage disorders. Some of the common disorders are Gaucher disease (GD) and Fabry disease (FD
Autor:
Frauke Liebelt, Dris El Atmioui, Ilana Berlin, Huib Ovaa, Remco Merkx, Katharina F. Witting, Dharjath S. Hameed, Monique P. C. Mulder, Alfred C.O. Vertegaal, Lindsey T. Lelieveld, Jacques Neefjes
Publikováno v:
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition
Angewandte Chemie International Edition, 57(29), 8958-8962
Angewandte Chemie International Edition
Angewandte Chemie International Edition, 57(29), 8958-8962
SUMO is a post‐translational modifier critical for cell cycle progression and genome stability that plays a role in tumorigenesis, thus rendering SUMO‐specific enzymes potential pharmacological targets. However, the systematic generation of tools