Development of 19F-NMR chemical shift detection of DNA B–Z equilibrium using 19F-NMR

2017 ◽  
Vol 15 (24) ◽  
pp. 5109-5111 ◽  
Author(s):  
S. Nakamura ◽  
H. Yang ◽  
C. Hirata ◽  
F. Kersaudy ◽  
K. Fujimoto

The DNA conformational changes such as B-formed, Z-formed, and single stranded DNA, were detected in one of 19F-NMR measurements using a fluorine-labeled nucleobase.

2009 ◽  
Vol 78 (4) ◽  
pp. 971-984 ◽  
Author(s):  
Predrag Kukić ◽  
Damien Farrell ◽  
Chresten R. Søndergaard ◽  
Una Bjarnadottir ◽  
John Bradley ◽  
...  

2010 ◽  
Vol 131 (5) ◽  
pp. 570-577 ◽  
Author(s):  
Anna Vulpetti ◽  
Gregory Landrum ◽  
Simon Rüdisser ◽  
Paulus Erbel ◽  
Claudio Dalvit

PPAR Research ◽  
2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Tony Velkov

Fatty acid binding proteins (FABPs) act as intracellular shuttles for fatty acids as well as lipophilic xenobiotics to the nucleus, where these ligands are released to a group of nuclear receptors called the peroxisome proliferator activated receptors (PPARs). PPAR mediated gene activation is ultimately involved in maintenance of cellular homeostasis through the transcriptional regulation of metabolic enzymes and transporters that target the activating ligand. Here we show that liver- (L-) FABP displays a high binding affinity for PPAR subtype selective drugs. NMR chemical shift perturbation mapping and proteolytic protection experiments show that the binding of the PPAR subtype selective drugs produces conformational changes that stabilize the portal region of L-FABP. NMR chemical shift perturbation studies also revealed that L-FABP can form a complex with the PPAR ligand binding domain (LBD) of PPARα. This protein-protein interaction may represent a mechanism for facilitating the activation of PPAR transcriptional activity via the direct channeling of ligands between the binding pocket of L-FABP and the PPARαLBD. The role of L-FABP in the delivery of ligands directly to PPARαvia this channeling mechanism has important implications for regulatory pathways that mediate xenobiotic responses and host protection in tissues such as the small intestine and the liver where L-FABP is highly expressed.


1984 ◽  
Vol 13 (6) ◽  
pp. 871-872 ◽  
Author(s):  
Yoko Kanazawa ◽  
Wakako Higuchi

1988 ◽  
Vol 26 (3) ◽  
pp. 197-203 ◽  
Author(s):  
Mark R. Johnson ◽  
Christopher A. Colburn ◽  
Susan J. Ganion ◽  
Byungki Son ◽  
John A. Mosbo ◽  
...  

2001 ◽  
Vol 338 (2-3) ◽  
pp. 95-100 ◽  
Author(s):  
Mitsuhiro Kanakubo ◽  
Tatsuya Umecky ◽  
Hajime Kawanami ◽  
Takafumi Aizawa ◽  
Yutaka Ikushima ◽  
...  

Carbon ◽  
1982 ◽  
Vol 20 (2) ◽  
pp. 134
Author(s):  
Gerald Ray Miller ◽  
Lewis Banks ◽  
M.J. Moran ◽  
H.A. Resing

2018 ◽  
Vol 16 (6) ◽  
pp. 891-894
Author(s):  
Shigetaka Nakamura ◽  
Yasuharu Takashima ◽  
Kenzo Fujimoto

The 19F NMR identical to trifluorothymidine was large shifted by DNA photo-cross-linking. The shifted signal dispersion was induced by the substituent of 3-vinylcarbazole derivatives.


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