Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Elfrida R. Benjamin"'
Autor:
Brandon Durant, Sabrina Forni, Lawrence Sweetman, Nastry Brignol, Xing-Li Meng, Elfrida R. Benjamin, Raphael Schiffmann, Jin-Song Shen
Publikováno v:
Journal of Lipid Research, Vol 52, Iss 9, Pp 1742-1746 (2011)
The aim of our study was to measure globotriaosylceramide (Gb3) and lyso-Gb3 levels by tandem mass spectrometry in the urine and kidney in Fabry (gla knockout) mice and wild-type controls. We found that urine Gb3 of male and female Fabry mice was hig
Externí odkaz:
https://doaj.org/article/79f9c326f6a74fac99491ff63a03c80d
Autor:
Brandy Young-Gqamana, Nastry Brignol, Hui-Hwa Chang, Richie Khanna, Rebecca Soska, Maria Fuller, Sheela A Sitaraman, Dominique P Germain, Roberto Giugliani, Derralynn A Hughes, Atul Mehta, Kathy Nicholls, Pol Boudes, David J Lockhart, Kenneth J Valenzano, Elfrida R Benjamin
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e57631 (2013)
Fabry disease (FD) results from mutations in the gene (GLA) that encodes the lysosomal enzyme α-galactosidase A (α-Gal A), and involves pathological accumulation of globotriaosylceramide (GL-3) and globotriaosylsphingosine (lyso-Gb3). Migalastat hy
Externí odkaz:
https://doaj.org/article/b1ae5dbd0fb74b4bbf482e8731fdda6c
Autor:
Leo B. Dungan, Hui H. Chang, Sean W. Clark, Nastry Brignol, Michelle Frascella, Kenneth J. Valenzano, Richie Khanna, Elfrida R. Benjamin, Robert Boyd, Rick Hamler, Sean Morrison
Publikováno v:
Analytical Chemistry. 89:8288-8295
Gaucher disease (GD) is caused by mutations in the GBA1 gene that encodes the lysosomal enzyme acid β-glucosidase (GCase). Reduced GCase activity primarily leads to the accumulation of two substrates, glucosylceramide (GlcCer) and glucosylsphingosin
Autor:
Elfrida R. Benjamin, Behzad Najafian, Hadis Williams, Jay A. Barth, A.N. Sokolovskiy, Jeffrey P. Castelli, Michael Mauer
Publikováno v:
Journal of Medical Genetics
Objective Deficiency of α-galactosidase A (αGal-A) in Fabry disease leads to the accumulation mainly of globotriaosylceramide (GL3) in multiple renal cell types. Glomerular podocytes are relatively resistant to clearance of GL3 inclusions by enzyme
Autor:
Jay A. Barth, Benjamin Bronfin, David J. Lockhart, William R. Wilcox, Robert J. Desnick, Daniel G. Bichet, Dominique P. Germain, Xiaoyang Wu, John Kirk, Raphael Schiffmann, Hadis Williams, Roberto Giugliani, Julie Yu, Sarah Bond, Elfrida R. Benjamin, Kenneth J. Valenzano, Farhana Pruthi, Carrolee Barlow, Derralynn Hughes, Maria Cecilia Della Valle, Evan Katz, Jeff Castelli
Publikováno v:
Genetics in Medicine
Purpose: Fabry disease is an X-linked lysosomal storage disorder caused by mutations in the α-galactosidase A gene. Migalastat, a pharmacological chaperone, binds to specific mutant forms of α-galactosidase A to restore lysosomal activity. Methods:
Autor:
David J. Lockhart, Ana Jovanovic, Toya Ohashi, Elfrida R. Benjamin, Norio Sakai, Raphael Schiffmann, David M. Koeller, Gere Sunder-Plassmann, Dominique P. Germain, Jeffrey P. Castelli, Elizabeth Ludington, Charles Marques Lourenço, Kathleen Nicholls, Mark Thomas, Ozlem Goker-Alpan, Robin H. Lachmann, David Dimmock, Ulla Feldt-Rasmussen, Jay A. Barth, Carrolee Barlow, François Eyskens, Patrick Deegan, Eric Hachulla, Nina Skuban, William R. Wilcox, Daniel G. Bichet, John Kirk, Iacopo Olivotto, Suma P. Shankar, Gerard Vockley, Takashi Hamazaki, Franklin K. Johnson, Derralynn Hughes, Pol Boudes, Christopher Viereck, Ichiei Narita, Khan Nedd, Julie Yu
Publikováno v:
Journal of medical genetics
Journal of medical genetics, vol 54, iss 4
Hughes, D A, Nicholls, K, Shankar, S P, Sunder-Plassmann, G, Koeller, D, Nedd, K, Vockley, G, Hamazaki, T, Lachmann, R, Ohashi, T, Olivotto, I, Sakai, N, Deegan, P, Dimmock, D, Eyskens, F, Germain, D P, Goker-Alpan, O, Hachulla, E, Jovanovic, A, Lourenco, C M, Narita, I, Thomas, M, Wilcox, W R, Bichet, D G, Schiffmann, R, Ludington, E, Viereck, C, Kirk, J, Yu, J, Johnson, F, Boudes, P, Benjamin, E R, Lockhart, D J, Barlow, C, Skuban, N, Castelli, J P, Barth, J & Feldt-Rasmussen, U 2017, ' Oral pharmacological chaperone migalastat compared with enzyme replacement therapy in Fabry disease : 18-month results from the randomised phase III ATTRACT study ', Journal of Medical Genetics, vol. 54, no. 4, pp. 288-296 . https://doi.org/10.1136/jmedgenet-2016-104178
Journal of medical genetics, vol 54, iss 4
Hughes, D A, Nicholls, K, Shankar, S P, Sunder-Plassmann, G, Koeller, D, Nedd, K, Vockley, G, Hamazaki, T, Lachmann, R, Ohashi, T, Olivotto, I, Sakai, N, Deegan, P, Dimmock, D, Eyskens, F, Germain, D P, Goker-Alpan, O, Hachulla, E, Jovanovic, A, Lourenco, C M, Narita, I, Thomas, M, Wilcox, W R, Bichet, D G, Schiffmann, R, Ludington, E, Viereck, C, Kirk, J, Yu, J, Johnson, F, Boudes, P, Benjamin, E R, Lockhart, D J, Barlow, C, Skuban, N, Castelli, J P, Barth, J & Feldt-Rasmussen, U 2017, ' Oral pharmacological chaperone migalastat compared with enzyme replacement therapy in Fabry disease : 18-month results from the randomised phase III ATTRACT study ', Journal of Medical Genetics, vol. 54, no. 4, pp. 288-296 . https://doi.org/10.1136/jmedgenet-2016-104178
Background Fabry disease is an X-linked lysosomal storage disorder caused by GLA mutations, resulting in α-galactosidase (α-Gal) deficiency and accumulation of lysosomal substrates. Migalastat, an oral pharmacological chaperone being developed as a
Autor:
Daniel G. Bichet, Elfrida R. Benjamin, Roberto Giugliani, Derralynn Hughes, Jay A. Barth, Nina Skuban, Christopher Viereck, Jeffrey P. Castelli, Kathy Nicholls, J. Charles Jennette, Dominique P. Germain, Robert B. Colvin, Laura Barisoni
Publikováno v:
Repositório Institucional da UFRGS
Universidade Federal do Rio Grande do Sul (UFRGS)
instacron:UFRGS
Genetics in Medicine
Universidade Federal do Rio Grande do Sul (UFRGS)
instacron:UFRGS
Genetics in Medicine
PURPOSE: Outcomes in patients with Fabry disease receiving migalastat during the phase 3 FACETS trial (NCT00925301) were evaluated by phenotype. METHODS: Data were evaluated in two subgroups of patients with migalastat-amenable GLA variants: "classic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9884c3d590afb71cac1e4b7fbbba387f
Autor:
Jay A. Barth, Elfrida R. Benjamin, Xuan Wang, Caren Swift, Xiaoyang Wu, Raphael Schiffmann, Lawrence Sweetman, Jeffrey P. Castelli, Nathan McNeill
Publikováno v:
Genet Med
To test the hypothesis that undiagnosed patients with Fabry disease exist among patients affected by common heart disease. Globotriaosylceramide in random whole urine using tandem mass spectroscopy, α-galactosidase A activity in dried blood spots, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::046b16f2353fb2ea13b665bfb9aac8d7
https://europepmc.org/articles/PMC9302444/
https://europepmc.org/articles/PMC9302444/
Autor:
Kate Chang, Amol Ketkar, Nicola Robertson, Masahito Miyamoto, Kenneth J. Valenzano, Yi Lun, Nastry Brignol, Su Xu, Kazutoshi Mihara, Rebecca Soska, Jessie Feng, Hidehito Yasukawa, Robert Boyd, Michelle Frascella, Carole Shardlow, Rick Hamler, Susie Fowles, Alison Churchill, Richie Khanna, David J. Lockhart, Anadina Garcia, Tohru Hirato, Elfrida R. Benjamin, Adriane Schilling, Sean Sullivan
Publikováno v:
Molecular Therapy
Fabry disease is an X-linked lysosomal storage disorder caused by mutations in the gene that encodes α-galactosidase A and is characterized by pathological accumulation of globotriaosylceramide and globotriaosylsphingosine. Earlier, the authors demo
Autor:
Sheela Sitaraman, Todd Levine, Carrolee Barlow, Mark Roberts, Barry J. Byrne, Tahseen Mozaffar, Priya S. Kishnani, Pascal Laforêt, Richie Khanna, Jessie Feng, Mark A. Tarnopolsky, David J. Lockhart, Majed Dasouki, Matthews Adera, Ozlem Goker-Alpan, Franklin K. Johnson, Mazen M. Dimachkie, K. Sivakumar, Pol Boudes, Kenneth J. Valenzano, Erika Finanger, Muhammad Ali Pervaiz, K. Guter, Elfrida R. Benjamin, John J. Flanagan, Richard Lazauskas, Jay A. Barth
Publikováno v:
Molecular Therapy
Kishnani, P; Tarnopolsky, M; Roberts, M; Sivakumar, K; Dasouki, M; Dimachkie, MM; et al.(2017). Duvoglustat HCl Increases Systemic and Tissue Exposure of Active Acid α-Glucosidase in Pompe Patients Co-administered with Alglucosidase α. Molecular Therapy, 25(5), 1199-1208. doi: 10.1016/j.ymthe.2017.02.017. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/7kd7w6h0
Kishnani, P; Tarnopolsky, M; Roberts, M; Sivakumar, K; Dasouki, M; Dimachkie, MM; et al.(2017). Duvoglustat HCl Increases Systemic and Tissue Exposure of Active Acid α-Glucosidase in Pompe Patients Co-administered with Alglucosidase α. Molecular Therapy, 25(5), 1199-1208. doi: 10.1016/j.ymthe.2017.02.017. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/7kd7w6h0
Duvoglustat HCl (AT2220, 1-deoxynojirimycin) is an investigational pharmacological chaperone for the treatment of acid α-glucosidase (GAA) deficiency, which leads to the lysosomal storage disorder Pompe disease, which is characterized by progressive