Zobrazeno 1 - 10
of 114
pro vyhledávání: '"Mia, Horowitz"'
Publikováno v:
Cells, Vol 13, Iss 19, p 1619 (2024)
The human GBA1 gene encodes lysosomal acid β-glucocerebrosidase, whose activity is deficient in Gaucher disease (GD). In Drosophila, there are two GBA1 orthologs, Gba1a and Gba1b, and Gba1b is the bona fide GCase encoding gene. Several fly lines wit
Externí odkaz:
https://doaj.org/article/eeb26230631141988833ee22b4a9f518
Autor:
Or Cabasso, Sumit Paul, Gali Maor, Metsada Pasmanik-Chor, Wouter Kallemeijn, Johannes Aerts, Mia Horowitz
Publikováno v:
Cells, Vol 10, Iss 3, p 630 (2021)
Human GBA1 encodes lysosomal acid β-glucocerebrosidase (GCase), which hydrolyzes cleavage of the beta-glucosidic linkage of glucosylceramide (GlcCer). Mutations in this gene lead to reduced GCase activity, accumulation of glucosylceramide and glucos
Externí odkaz:
https://doaj.org/article/1a3b960c9e94479e8bff3c7edfa4213b
Publikováno v:
PLoS ONE, Vol 12, Iss 3, p e0174495 (2017)
[This corrects the article DOI: 10.1371/journal.pone.0169639.].
Externí odkaz:
https://doaj.org/article/0a2b7551b7374f359921087d5439a14a
Publikováno v:
PLoS ONE, Vol 12, Iss 1, p e0169639 (2017)
Endocytosis is a multi-step process involving a large number of proteins, both general factors, such as clathrin and adaptor protein complexes, and unique proteins, which modulate specialized endocytic processes, like the EHD proteins. EHDs are a fam
Externí odkaz:
https://doaj.org/article/c95b1b6480774ffca11b9d751087153f
Publikováno v:
Advanced drug delivery reviews. 187
Lysosomes have a critical role in maintaining normal cellular homeostasis mediated by their involvement in secretion, plasma membrane repair, cell signaling and energy metabolism. Lysosomal storage disorders (LSDs) are a group of approximately 50 rar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86414cf84690dba54a3c8ada4f01549b
https://pubmed.ncbi.nlm.nih.gov/35764179
https://pubmed.ncbi.nlm.nih.gov/35764179
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0134053 (2015)
Endocytosis defines the entry of molecules or macromolecules through the plasma membrane as well as membrane trafficking in the cell. It depends on a large number of proteins that undergo protein-protein and protein-phospholipid interactions. EH Doma
Externí odkaz:
https://doaj.org/article/61abf3fefee84a21927533bc02a2eada
Autor:
Gali Maor, Sumit Paul, Johannes M. F. G. Aerts, Or Cabasso, Mia Horowitz, Wouter W. Kallemeijn, Metsada Pasmanik-Chor
Publikováno v:
Cells, Vol 10, Iss 630, p 630 (2021)
Cells, 10(3). MDPI} {AG
Cells
Volume 10
Issue 3
Cells, 10(3). MDPI} {AG
Cells
Volume 10
Issue 3
Human GBA1 encodes lysosomal acid β-glucocerebrosidase (GCase), which hydrolyzes cleavage of the beta-glucosidic linkage of glucosylceramide (GlcCer). Mutations in this gene lead to reduced GCase activity, accumulation of glucosylceramide and glucos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e65edf09f484327f8f31aa116c442131
https://www.mdpi.com/2073-4409/10/3/630
https://www.mdpi.com/2073-4409/10/3/630
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 19
International Journal of Molecular Sciences, Vol 21, Iss 7397, p 7397 (2020)
Volume 21
Issue 19
International Journal of Molecular Sciences, Vol 21, Iss 7397, p 7397 (2020)
Fabry disease, an X-linked recessive lysosomal disease, results from mutations in the GLA gene encoding lysosomal &alpha
galactosidase A (&alpha
Gal A). Due to these mutations, there is accumulation of globotriaosylceramide (GL-3) in plasma
galactosidase A (&alpha
Gal A). Due to these mutations, there is accumulation of globotriaosylceramide (GL-3) in plasma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89cc5486335a2185a8066231a0006adc
Autor:
Hila Braunstein, Mia Horowitz
Publikováno v:
Molecular Genetics and Metabolism. 135:S25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f2e8200700bc218094aa0e6e8ea584e
https://doi.org/10.1016/j.ymgme.2021.11.047
https://doi.org/10.1016/j.ymgme.2021.11.047