MR/J007412/1/Medical Research Council/United Kingdom[Grants and Funding] - Search Results

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2014	1
2015	2
2016	1
2017	1
2024	0

Page 1

Identification of a multifunctional docking site on the catalytic unit of phosphodiesterase-4 (PDE4) that is utilised by multiple interaction partners.

Houslay KF, Christian F, MacLeod R, Adams DR, Houslay MD, Baillie GS. Houslay KF, et al. Biochem J. 2017 Feb 15;474(4):597-609. doi: 10.1042/BCJ20160849. Epub 2016 Dec 19. Biochem J. 2017. PMID: 27993970 Free PMC article.

Dimerization of cAMP phosphodiesterase-4 (PDE4) in living cells requires interfaces located in both the UCR1 and catalytic unit domains.

Bolger GB, Dunlop AJ, Meng D, Day JP, Klussmann E, Baillie GS, Adams DR, Houslay MD. Bolger GB, et al. Cell Signal. 2015 Apr;27(4):756-69. doi: 10.1016/j.cellsig.2014.12.009. Epub 2014 Dec 27. Cell Signal. 2015. PMID: 25546709 Free PMC article.

UCR1C is a novel activator of phosphodiesterase 4 (PDE4) long isoforms and attenuates cardiomyocyte hypertrophy.

Wang L, Burmeister BT, Johnson KR, Baillie GS, Karginov AV, Skidgel RA, O'Bryan JP, Carnegie GK. Wang L, et al. Cell Signal. 2015 May;27(5):908-22. doi: 10.1016/j.cellsig.2015.02.003. Epub 2015 Feb 12. Cell Signal. 2015. PMID: 25683917 Free PMC article.

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