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Keywords: 14-3-3 protein
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Articles
Mark Linch, Philippe Riou, Jeroen Claus, Angus J. Cameron, Julien de Naurois, Banafshe Larijani, Tony Ng, Neil Q. McDonald, Peter J. Parker
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2014) 42 (1): 35–41.
Published: 23 January 2014
...@cancer.org.uk ). 9 8 2013 © The Authors Journal compilation © 2014 Biochemical Society 2014 AGC kinase family 14-3-3 protein protein kinase RhoE Rnd3 Understanding the physiological and pathological variations in the epiproteome has increasingly been in demand as the era...
Articles
Jing Zhao, Spencer B. Hermanson, Coby B. Carlson, Steven M. Riddle, Kurt W. Vogel, Kun Bi, R. Jeremy Nichols
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (5): 1158–1162.
Published: 19 September 2012
... To whom correspondence should be addressed (email jnichols@parkinsonsinstitute.org ). 24 5 2012 © The Authors Journal compilation © 2012 Biochemical Society 2012 14-3-3 protein high-throughput screening leucine-rich repeat kinase 2 (LRRK2) phosphorylation Parkinson's disease...
Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2012) 40 (2): 451–456.
Published: 21 March 2012
... at two serine residues, Ser 274 and Ser 299 , which form a docking site for 14-3-3 proteins. Binding to 14-3-3 proteins protects RdgBβ from degradation that occurs at the proteasome after ubiquitination. In addition to binding 14-3-3, the PITP domain of RdgBβ interacts with the Ang II (angiotensin II...
Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2007) 35 (2): 250–252.
Published: 20 March 2007
... cytokines and growth factors are able to control these pleiotropic responses. 1 To whom correspondence should be addressed (email mark.guthridge@imvs.sa.gov.au ). 26 10 2006 © 2007 The Biochemical Society 2007 14-3-3 protein cytokine growth factor phosphoinositide 3-kinase...
Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2003) 31 (3): 587–591.
Published: 01 June 2003
.... Phosphorylation-dependent binding between tuberin and members of the 14-3-3 protein family indicates how the tuberin–hamartin complex may interact with upstream and downstream effectors, and suggests how phosphorylation-dependent regulation of the complex may be controlled. 1 To whom correspondence should...