Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Sadia Paracha"'
Autor:
Christa N. Hestekin, Jamie A. Hestekin, Sadia Paracha, Grace Morrison, Efecan Pakkaner, John Moore, Leticia Santos de Souza, Sam Stephens, Catey Atchley, Ira Kurtz
Publikováno v:
Communications Materials, Vol 1, Iss 1, Pp 1-10 (2020)
The nephrons in the kidney transport ions and organic molecules, but may not work effectively in patients with kidney disease. Here, a synthetic nephron is created, based on activated wafer electrodeionization, and shown to enable the transport of se
Externí odkaz:
https://doaj.org/article/3cac5cb4e31d4aeda415f046332d15cc
Autor:
Christa N. Hestekin, Jamie A. Hestekin, Sadia Paracha, Grace Morrison, Efecan Pakkaner, John Moore, Leticia Santos de Souza, Sam Stephens, Catey Atchley, Ira Kurtz
Publikováno v:
Communications Materials, Vol 1, Iss 1, Pp 1-1 (2020)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Externí odkaz:
https://doaj.org/article/ed8eaa3b686d408eaca76cde98d67389
Autor:
Grace Morrison, Sam Stephens, Ira Kurtz, Jamie A. Hestekin, Sadia Paracha, Catey Atchley, John P. Moore, Christa N. Hestekin, Efecan Pakkaner, Leticia Santos de Souza
Publikováno v:
Communications Materials, Vol 1, Iss 1, Pp 1-10 (2020)
Current approaches for treating patients with end stage renal disease include hemodialysis and peritoneal dialysis, both of which are diffusion-based treatments that require a dialysate solution. The native kidney has separate filtration (glomerulus)
Autor:
Ira Kurtz, Grace Morrison, Sadia Paracha, Efecan Pakkaner, Leticia Santos de Souza, Christa N. Hestekin, John P. Moore, Jamie A. Hestekin, Sam Stephens, Catey Atchley
Publikováno v:
Communications Materials, Vol 1, Iss 1, Pp 1-1 (2020)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Autor:
Sadia Paracha, Christa N. Hestekin
Publikováno v:
Biomicrofluidics. 10(3)
Oligomeric forms of the amyloid beta (Aβ) protein have been indicated to be an important factor in the development of Alzheimer's disease (AD). Since the oligomeric forms of Aβ can vary in size and conformation, it is vital to understand the early