Zobrazeno 1 - 10
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pro vyhledávání: '"Riordan, A"'
Akademický článek
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Autor:
Annie S. Hong, Andrew Schuster, Dickson Luong, John R. McCarrey, Wei Yan, Connor R. Riordan, Seungil Ro, Jianqiang Bao, Nicole Ortogero, Daniel Oliver, Grant W. Hennig, Bhupal P. Bhetwal
Publikováno v:
Journal of Biological Chemistry. 289:32824-32834
PIWI-interacting RNAs (piRNAs) are small noncoding RNAs that bind PIWI family proteins exclusively expressed in the germ cells of mammalian gonads. MIWI2-associated piRNAs are essential for silencing transposons during primordial germ cell developmen
Autor:
Mark F. Rosenberg, John R. Riordan, Liam O'Ryan, Guy Hughes, Luba A. Aleksandrov, Zhefeng Zhao, Robert C. Ford
Publikováno v:
Journal of Biological Chemistry. 286:42647-42654
Cystic fibrosis affects about 1 in 2500 live births and involves loss of transmembrane chloride flux due to a lack of a membrane protein channel termed the cystic fibrosis transmembrane conductance regulator (CFTR). We have studied CFTR structure by
Akademický článek
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Publikováno v:
Journal of Biological Chemistry. 278:6440-6449
ClC chloride channels are widely distributed in organisms across the evolutionary spectrum, and members of the mammalian family play crucial roles in cellular function and are mutated in several human diseases (Jentsch, T. J., Stein, V., Weinreich, F
Autor:
Frédéric Buyse, Jean Marie Ruysschaert, Adelin Gustot, Yue-Xian Hou, Xiu-Bao Chang, Liliana Manciu, John R. Riordan
Publikováno v:
Journal of Biological Chemistry. 278:3347-3356
Human multidrug resistance protein 1 (MRP1) is a member of the ATP-binding cassette transporter family and transports chemotherapeutic drugs as well as diverse organic anions such as leukotriene LTC(4). The transport of chemotherapeutic drugs require
Publikováno v:
Journal of Biological Chemistry. 277:15419-15425
As in other adenine nucleotide binding cassette (ABC) proteins the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR) bind and hydrolyze ATP and in some manner regulate CFTR ion channel gating. Unlike some ot
Autor:
Jin San Yoo, John R. Riordan, Sergei I. Bannykh, Bryan D. Moyer, William E. Balch, Hyeon Mi Yoo
Publikováno v:
Journal of Biological Chemistry. 277:11401-11409
The mechanism(s) of cystic fibrosis transmembrane conductance regulator (CFTR) trafficking from the endoplasmic reticulum (ER) through the Golgi apparatus, the step impaired in individuals afflicted with the prevalent CFTR-ΔF508 mutation leading to
Publikováno v:
Journal of Biological Chemistry. 277:5110-5119
Multidrug resistance protein (MRP1) utilizes two non-equivalent nucleotide-binding domains (NBDs) to bind and hydrolyze ATP. ATP hydrolysis by either one or both NBDs is essential to drive transport of solute. Mutations of either NBD1 or NBD2 reduce
Publikováno v:
Journal of Biological Chemistry. 276:12918-12923
After phosphorylation by protein kinase A, gating of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel is regulated by the interaction of ATP with its nucleotide binding domains (NBDs). Models of this gating regulation h