Results 91 to 100 of about 2,570 (187)

Biochemical Characterization of the GBA2 c.1780G>C Missense Mutation in Lymphoblastoid Cells from Patients with Spastic Ataxia [PDF]

, 2018
The GBA2 gene encodes the non-lysosomal glucosylceramidase (NLGase), an enzyme that catalyzes the conversion of glucosylceramide (GlcCer) to ceramide and glucose.
Sandro Sonnino, Malekkou, Anna, Elena Chiricozzi, Pantzaris, Marios, Votsi, Christina, Chiricozzi, Elena, Anthi Drousiotou, Marios Pantzaris, Nicoletta Loberto, Loberto, Nicoletta, Aureli, Massimo, Christina Votsi, Kyproula Christodoulou, Christodoulou, Kyproula, Eleni Zamba-Papanicolaou, Massimo Aureli, Maura Samarani, Drousiotou, Anthi, Anna Malekkou, Sonnino, Sandro, Samarani, Maura, Zamba-Papanicolaou, Eleni   +21 more
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Proposed metabolic pathway of sphingolipids in A. muelleri.

, 2018
Serine palmitoyltransferase (SPT), 3-Dehydrosphinganine reductase (DSR), sphingosine kinase (SPHK), sphinganine C4-monooxygenase (SUR2), sphinganine-1-phosphate aldolase (SPL), acyl-CoA-dependent ceramide synthase (LAG1), neutral ceramidase (ASAH2 ...
Erxi Liu (5029628), Ying Diao (191325), Lin Zhong (157266), Nunung Harijati (5029625), Zhongli Hu (186181), Chaozhu Yang (554675), Jiangdong Liu (450341), Surong Jin (554676)   +7 more
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Glucocerebrosidase deficiency leads to neuropathology via cellular immune activation.

PLoS Genetics
Mutations in GBA (glucosylceramidase beta), which encodes the lysosomal enzyme glucocerebrosidase (GCase), are the strongest genetic risk factor for the neurodegenerative disorders Parkinson's disease (PD) and Lewy body dementia.
Evelyn S Vincow, Ruth E Thomas, Gillian Milstein, Gautam Pareek, Theo K Bammler, James MacDonald, Leo J Pallanck   +6 more
doaj   +1 more source

Visualization of Active Glucocerebrosidase in Rodent Brain with High Spatial Resolution following In Situ Labeling with Fluorescent Activity Based Probes.

PLoS ONE, 2015
Gaucher disease is characterized by lysosomal accumulation of glucosylceramide due to deficient activity of lysosomal glucocerebrosidase (GBA). In cells, glucosylceramide is also degraded outside lysosomes by the enzyme glucosylceramidase 2 (GBA2) of ...
Daniela Herrera Moro Chao, Wouter W Kallemeijn, Andre R A Marques, Marie Orre, Roelof Ottenhoff, Cindy van Roomen, Ewout Foppen, Maria C Renner, Martina Moeton, Marco van Eijk, Rolf G Boot, Willem Kamphuis, Elly M Hol, Jan Aten, Hermen S Overkleeft, Andries Kalsbeek, Johannes M F G Aerts   +16 more
doaj   +1 more source

Synthesis of Cyclophellitol, Cyclophellitol Aziridine, and Their Tagged Derivatives [PDF]

, 2014
Cyclitol epoxides and aziridines are potent and selective irreversible inhibitors of retaining glycosidases. We have previously reported on our studies on the use of activity-based probes derived from cyclophellitol and from its aziridine analogue for ...
Wong, Chung-Sing, Sascha Hoogendoorn, Kallemeijn, Wouter W., Hoogendoorn, Sascha, Jiang, Jianbing, Witte, Martin D., Johannes M. F. G. Aerts, Chander, Sharina D., Kah‐Yee Li, Wouter W. Kallemeijn, Li, Kah-Yee, Jianbing Jiang, van den Elst, Hans, Chung‐Sing Wong, Jeroen D. C. Codée, Hans van den Elst, Gijs A. van der Marel, van der Marel, Gijs A., Martin D. Witte, Aerts, Johannes M. F. G., Witte, Martin D.; id_orcid, Overkleeft, Herman S., Codee, Jeroen D. C., Sharina D. Chander, Herman S. Overkleeft, Thomas J. M. Beenakker, Beenakker, Thomas J. M.   +26 more
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Relative mRNA expression levels of 14 genes in (P) Parental and (R) dox-resistant MCF-7 cells.

, 2021
(A) Transcripts showed a significant increase in the gene expression level in dox-resistant MCF-7. (B) Transcripts showed a significant increase in gene expression level in parental MCF-7.
Sameh S. M. Soliman (9465380), Naglaa S. Ashmawy (10792551), Sarra B. Shakartalla (9465395), Alaa M. Altaie (11553066), Ola D. A. Shammout (11553063), Mohammad H. Semreen (2134234), Hany A. Omar (7592393)   +6 more
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Selective labelling of GBA2 in cells with fluorescent β-d-arabinofuranosyl cyclitol aziridines [PDF]

GBA2, the non-lysosomal β-glucosylceramidase, is an enzyme involved in glucosylceramide metabolism. Pharmacological inhibition of GBA2 by N-alkyl iminosugars is well tolerated and benefits patients suffering from Sandhoff and Niemann-Pick type C diseases,
Lammers, R.F., Su, !., Maurits, E., Artola, M., Su, Qin, Borlandelli, V.B., Aerts, J.M.F.G., Louwerse, Max, Janssen, M., Su, Q., Linzel, D., Davies, Gideon J., Borlandelli, V., Boot, Rolf G., Schröder, Sybrin P., Overkleeft, H.S., Schröder, S.P., Davies, G.J., Borlandelli, Valentina, Louwerse, G.A.M., Boot, R.G., Janssen, Max, Offen, W.A., Lammers, Rob F., Maurits, Elmer, Linzel, Daniël, Overkleeft, Herman S., Artola, Marta, Aerts, Johannes M.F.G., Offen, Wendy A.   +29 more
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Sphingolipids and influenza virus infections.

, 2020
Several studies have demonstrated that inhibition of distinct enzymes in the sphingolipid pathway results in alterations to influenza virus infection levels.
William Casey Harrison (8423064), John D. Han (8423073), Michael P. Calgi (8423061), Pedro Costa-Pinheiro (816456), Mark Kester (499862), Jeremy Joseph Porter Shaw (8423067), Camille M. Drews (4721175), Todd E. Fox (499853), Kelly Drews (8423058), Judith M. White (7164953), Kendra A. Jobe (8423070)   +10 more
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Phospholipid Membrane Interactions of Saposin C: In Situ Atomic Force Microscopic Study

, 2003
Saposin C (Sap C) is a small glycoprotein required for hydrolysis of glucosylceramidase in lysosomes. The full activity of glucosylceramidase requires the presence of both Sap C and acidic phospholipids.
You, Hong Xing, Grabowski, Gregory A., Qi, Xiaoyang, Yu, Lei   +3 more
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Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity. Expression in young flower tissues and in barley seeds

, 2005
The plant- specific insert ( PSI) of cypro11 gene- encoding cyprosin, an aspartic proteinase from Cynara cardunculus, has been cloned by polymerase chain reaction ( PCR) into a bacterial expression vector.
Marttila, S, Al-Karadaghi, Salam, Picaud, S, Hiraiwa, M, Brodelius, M, Brodelius, P E   +5 more
core   +1 more source