Zobrazeno 1 - 10
of 204
pro vyhledávání: '"John R. Riordan"'
Autor:
Maud Sigoillot, Marie Overtus, Magdalena Grodecka, Daniel Scholl, Abel Garcia-Pino, Toon Laeremans, Lihua He, Els Pardon, Ellen Hildebrandt, Ina Urbatsch, Jan Steyaert, John R. Riordan, Cedric Govaerts
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of
Externí odkaz:
https://doaj.org/article/2a36a5cc137946bdbc014d5d58e302cb
Autor:
Ateeq Al-Zahrani, Natasha Cant, Vassilis Kargas, Tracy Rimington, Luba Aleksandrov, John R. Riordan, Robert C. Ford
Publikováno v:
AIMS Biophysics, Vol 2, Iss 2, Pp 131-152 (2015)
The most common inherited disease in European populations is cystic fibrosis. Mutations in the gene lead to loss of function of the cystic fibrosis transmembrane conductance regulator protein (CFTR). CFTR is a member of the ATP-binding cassette famil
Externí odkaz:
https://doaj.org/article/c886b28e1d6045d89ffa15fe9a7ab2b5
Autor:
Jianli An, Netaly Khazanov, Andrei A. Aleksandrov, Christie G. Brouillette, John R. Riordan, Ellen Hildebrandt, John C. Kappes, Hanoch Senderowitz, Haitao Ding, Andrew T. Mezzell, Zhengrong Yang, Ina L. Urbatsch, Bala M. Xavier, Qingxian Zhou, Fan Jiang
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:1193-1204
The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) is an ABC transporter containing two transmembrane domains forming a chloride ion channel, and two nucleotide binding domains (NBD1 and NBD2). CFTR has presented a formidable challenge to
Autor:
C. Brouillette, O. Clarke, S. Vorobiev, F. Jiang, I. Urbatsch, K. Wong, J. Wehby, J. Kappes, A. Aleksandrov, R. Grassucci, C. Wang, Z. Yang, J. Frank, John F. Hunt, John R. Riordan
Publikováno v:
Journal of Cystic Fibrosis. 20:S297
Autor:
Martin Caffrey, Timothy J. Jensen, Brian K. Kobilka, John R. Riordan, Pikyee Ma, Xiangyu Liu, Dietmar Weichert, Luba A. Aleksandrov
Publikováno v:
Nature Protocols. 12:1745-1762
The lipid cubic phase (in meso) method is an important approach for generating crystals and high-resolution X-ray structures of integral membrane proteins. However, as a consequence of instability, it can be impossible-using traditional methods-to co
Publikováno v:
Biochemistry. 57:5073-5075
The cystic fibrosis transmembrane conductance regulator (CFTR) is an asymmetric ATP-binding cassette transporter in which ATP hydrolysis occurs only at the second of the two composite nucleotide-binding sites whereas there are noncanonical substituti
Autor:
Yue Xian Hou, Yanlin Jia, Xiu Bao Chang, John W. Hanrahan, Arnaud Billet, Timothy J. Jensen, John R. Riordan
Publikováno v:
Channels
Channels, Taylor & Francis, 2016, 10 (3), pp.247-251. ⟨10.1080/19336950.2015.1126010⟩
Channels, Taylor & Francis, 2016, 10 (3), pp.247-251. ⟨10.1080/19336950.2015.1126010⟩
The CFTR chloride channel is tightly regulated by phosphorylation at multiple serine residues. Recently it has been proposed that its activity is also regulated by tyrosine kinases, however the tyrosine phosphorylation sites remain to be identified.
Autor:
Drew S. Gingerich, Lihua He, Joseph N. Kousouros, Jonathan F. Fay, James Z. Chen, Timothy J. Jensen, Luba A. Aleksandrov, Liying L. Cui, John R. Riordan, Andrei A. Aleksandrov
Publikováno v:
Biochemistry. 57(43)
The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, crucial to epithelial salt and water homeostasis, and defective due to mutations in its gene in patients with cystic fibrosis, is a unique member of the large family of ATP
Autor:
Farhad Forouhar, Nikolay V. Dokholyan, Anna Kaplan, Jianli An, Elizabeth A. Proctor, Andrei A. Aleksandrov, Christie G. Brouillette, Brent R. Stockwell, John R. Riordan, Hanoch Senderowitz, Grégory Boël, Netaly Khazanov, Pradeep Kota, Jack F.V. Hunt, Zhengrong Yang, Chi Wang
Many disease-causing mutations impair protein stability. Here, we explore a thermodynamic strategy to correct the disease-causing F508del mutation in the human cystic fibrosis transmembrane conductance regulator (hCFTR). F508del destabilizes nucleoti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cac9835ac46fa0d6f531e44f80b53a75
https://europepmc.org/articles/PMC6240863/
https://europepmc.org/articles/PMC6240863/
Autor:
Joseph N. Kousouros, Jonathan F. Fay, Drew S. Gingerich, James Z. Chen, Lihua He, Liying L. Cui, Luba A. Aleksandrov, Andrei A. Aleksandrov, John R. Riordan, Timothy J. Jensen
The Cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, crucial to epithelial salt and water homeostasis, and defective due to mutations in its gene in patients with cystic fibrosis is a unique member of the large family of ATP-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::279c04504f1c9608eb1e603a53db948d