5912-34-5Relevant articles and documents
A new synthesis of 1,7-naphthyridine
Tan, Rosita,Taurins, Alfred
, p. 1233 - 1237 (1966)
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Solubility-driven optimization of phosphodiesterase-4 inhibitors leading to a clinical candidate
Press, Neil J.,Taylor, Roger J.,Fullerton, Joseph D.,Tranter, Pamela,McCarthy, Clive,Keller, Thomas H.,Arnold, Nicola,Beer, David,Brown, Lyndon,Cheung, Robert,Christie, Julie,Denholm, Alastair,Haberthuer, Sandra,Hatto, Julia D. I.,Keenan, Mark,Mercer, Mark K.,Oakman, Helen,Sahri, Helene,Tuffnell, Andrew R.,Tweed, Morris,Tyler, John W.,Wagner, Trixie,Fozard, John R.,Trifilieff, Alexandre
, p. 7472 - 7479 (2012/11/06)
The solubility-driven optimization of a series of 1,7-napthyridine phosphodiesterase-4 inhibitors is described. Directed structural changes resulted in increased aqueous solubility, enabling superior pharmacokinetic properties with retention of PDE4 inhib
Elucidation of a structural basis for the inhibitor-driven, p62 (SQSTM1)-dependent intracellular redistribution of cAMP phosphodiesterase-4A4 (PDE4A4)
Day, Jonathan P.,Lindsay, Barbara,Riddell, Tracy,Jiang, Zhong,Allcock, Robert W.,Abraham, Achamma,Sookup, Sebastian,Christian, Frank,Bogum, Jana,Martin, Elisabeth K.,Rae, Robert L.,Anthony, Diana,Rosair, Georgina M.,Houslay, Daniel M.,Huston, Elaine,Baillie, George S.,Klussmann, Enno,Houslay, Miles D.,Adams, David R.
, p. 3331 - 3347 (2011/07/09)
Figure Presented. A survey of PDE4 inhibitors reveals that some compounds trigger intracellular aggregation of PDE4A4 into accretion foci through association with the ubiquitin-binding scaffold protein p62 (SQSTM1). We show that this effect is driven by i
