Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins.
cAMP regulates cellular functions primarily by activating PKA. The involvement of PKAs in various signaling pathways occurring simultaneously in different cellular compartments necessitates stringent spatial and temporal regulation. This specificity is largely achieved by binding of PKA to protein s...
Main Authors: | Aye, T, Mohammed, S, van den Toorn, H, van Veen, T, van der Heyden, MA, Scholten, A, Heck, A |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2009
|
Similar Items
-
Molecular basis of the allosteric mechanism of cAMP in the regulatory PKA subunit.
by: Pantano, S, et al.
Published: (2005) -
A high affinity switch for cAMP in the HCN pacemaker channels
by: Alessandro Porro, et al.
Published: (2024-01-01) -
Impact of cAMP on the T-cell response to type II collagen.
by: Ozegbe, P, et al.
Published: (2004) -
Detecting cAMP-induced Epac activation by fluorescence resonance energy transfer: Epac as a novel cAMP indicator.
by: Ponsioen, B, et al.
Published: (2004) -
Components of the mitochondrial cAMP signalosome
by: Monterisi, S, et al.
Published: (2017)