Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. (Q24801846)

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English	Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5.	scientific article

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scholarly article

1 reference

Europe PubMed Central

5 July 2017

Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. (English)

1 reference

Europe PubMed Central

5 July 2017

object named as

Jim Warwicker

5

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Stephen J. Yarwood

object named as

Stephen J Yarwood

3

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author name string

Graeme B Bolger

1

1 reference

Europe PubMed Central

5 July 2017

Angela McCahill

2

1 reference

Europe PubMed Central

5 July 2017

Michael R Steele

4

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Europe PubMed Central

5 July 2017

Miles D Houslay

6

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Europe PubMed Central

5 July 2017

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publication date

23 August 2002

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Europe PubMed Central

5 July 2017

BMC Biochemistry

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Europe PubMed Central

5 July 2017

3

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Europe PubMed Central

5 July 2017

1

0 references

24

1 reference

Europe PubMed Central

5 July 2017

https://scigraph.springernature.com/pub.10.1186/1471-2091-3-24

0 references

Structure and coding content of CST (BART) family RNAs of Epstein-Barr virus

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RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells

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Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene

1 reference

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A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs

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Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins

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Crystal structure of a G-protein beta gamma dimer at 2.1A resolution

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The 2.0 A crystal structure of a heterotrimeric G protein

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Comparative protein modelling by satisfaction of spatial restraints

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The human cyclic AMP-specific phosphodiesterase PDE-46 (HSPDE4A4B) expressed in transfected COS7 cells occurs as both particulate and cytosolic species that exhibit distinct kinetics of inhibition by the antidepressant rolipram

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Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5

1 reference

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ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions

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The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains

1 reference

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The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform

1 reference

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Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit

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The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon

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The cAMP-specific phosphodiesterase PDE4A5 is cleaved downstream of its SH3 interaction domain by caspase-3. Consequences for altered intracellular distribution

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cAMP-specific phosphodiesterase HSPDE4D3 mutants which mimic activation and changes in rolipram inhibition triggered by protein kinase A phosphorylation of Ser-54: generation of a molecular model.

1 reference

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Intracellular localization of the PDE4A cAMP-specific phosphodiesterase splice variant RD1 (RNPDE4A1A) in stably transfected human thyroid carcinoma FTC cell lines

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https://pubmed.ncbi.nlm.nih.gov/12193273

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10.1186/1471-2091-3-24

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Europe PubMed Central

5 July 2017

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1 reference

Europe PubMed Central

5 July 2017

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Europe PubMed Central

5 July 2017

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