Zobrazeno 1 - 10
of 10
pro vyhledávání: '"William A. Anong"'
Publikováno v:
American Society for Clinical Laboratory Science.
Background: Fluid intake is critical for metabolic and physiological processes to function properly in a homeostatic environment. When compared to other cells, normal red cells are more resilient to fluctuations in serum osmolality, remaining intact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8e917d74355334effd78d84edf3e3d5
https://doi.org/10.9734/bpi/nfmmr/v15/1902c
https://doi.org/10.9734/bpi/nfmmr/v15/1902c
Background: Blood ionized calcium (iCa) concentration has been shown to be pH dependent. In the clinical laboratory, plasma specimen for iCa measurement is routinely rejected when exposed to air prior to analysis. A preanalytical variable such as spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2e3abb1ab6ca8ecdf95995adce9aa45
Autor:
Jude Nnaemeka Okoyeh, William A. Anong
Publikováno v:
Integrative Journal of Medical Sciences.
Globally, more than two million people, about 53,000 in Africa have died from COVID-19 infection. By any metric, Africa has so far fared better than most parts of the world including, some of the most developed and affluent nations like the United St
Publikováno v:
Journal of Clinical Medical Research.
Autor:
Philip S. Low, Narla Mohandas, David M. Bodine, Xiuli An, Tahlia L. Weis, William A. Anong, Emily E. Devlin, Taina Franco, Haiyan Chu
Publikováno v:
Blood. 114:1904-1912
The erythrocyte membrane skeleton is the best understood cytoskeleton. Because its protein components have homologs in virtually all other cells, the membrane serves as a fundamental model of biologic membranes. Modern textbooks portray the membrane
Publikováno v:
The Journal of biological chemistry. 281(31)
The principal bridge connecting the erythrocyte membrane to the spectrin-based skeleton is established by band 3 and ankyrin; mutations leading to reduced bridge formation or increased bridge rupture result in morphological and mechanical abnormaliti
Autor:
William A. Anong, Francesca Rossi, Lucia De Franceschi, Bruno Nobili, Emanuele Miraglia del Giudice, Andrea Scaloni, Maria Luisa Conte, Fulvio Della Ragione, Arianna Donella-Deana, Adriana Borriello, Francesco Michelangelo Turrini, Silverio Perrotta, Narla Mohandas, Vincenzo Zappia, Vincenzo Poggi, Anna Maria Brunati, Achille Iolascon, Philip S. Low, Vincenzo Nigro
Publikováno v:
Blood 106 (2005): 4359–4366. doi:10.1182/blood-2005-07-2806
info:cnr-pdr/source/autori:Perrotta S, Borriello A, Scaloni A, De Franceschi L, Brunati AM, Turrini F, Nigro V, Miraglia del Giudice E, Nobili B, Conte ML, Rossi F, Iolascon A, Donella-Deana A, Zappia V, Poggi V, Anong W, Low P, Mohandas N, Della Ragione F./titolo:The n-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function/doi:10.1182%2Fblood-2005-07-2806/rivista:Blood/anno:2005/pagina_da:4359/pagina_a:4366/intervallo_pagine:4359–4366/volume:106
info:cnr-pdr/source/autori:Perrotta S, Borriello A, Scaloni A, De Franceschi L, Brunati AM, Turrini F, Nigro V, Miraglia del Giudice E, Nobili B, Conte ML, Rossi F, Iolascon A, Donella-Deana A, Zappia V, Poggi V, Anong W, Low P, Mohandas N, Della Ragione F./titolo:The n-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function/doi:10.1182%2Fblood-2005-07-2806/rivista:Blood/anno:2005/pagina_da:4359/pagina_a:4366/intervallo_pagine:4359–4366/volume:106
The 911 amino acid band 3 (SLC4A1) is the major intrinsic membrane protein of red cells and is the principal Cl-/HCO3- exchanger. The N-terminal cytoplasmic domain of band 3 anchors the spectrin-based membrane skeleton to the lipid bilayer through it
Autor:
Nicholas O. Markham, William A. Anong, Xuli An, Patrick G. Gallagher, David M. Bodine, Philip S. Low, Narla Mohandas
Publikováno v:
Blood. 106:808-808
The classical model of the human erythrocyte membrane (RBCM) shows two bridges connecting the lipid bilayer to the membrane skeleton: 1) a bridge attaching the cytoplasmic domain of band 3 (CDB3) to ankyrin, which in turn binds β-spectrin, and 2) a
Autor:
William A. Anong, Philip S. Low, Athar H. Chishti, Cheryl A. Hillary, Nancy J. Wandersee, Estela Campanella
Publikováno v:
Blood. 104:1571-1571
Glycolytic enzymes have been recently shown to exist as multi-enzyme complexes in association with the cytoplasmic domain of band 3 at the inner surface of the human erythrocyte membrane. Because several of the glycolytic enzyme binding sites have be