Occupancy of the catalytic site of the PDE4A4 cyclic AMP phosphodiesterase by rolipram triggers the dynamic redistribution of this specific isoform in living cells through a cyclic AMP independent process (Q44520775)

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scientific article published in October 2003

Language	Label	Description	Also known as
English	Occupancy of the catalytic site of the PDE4A4 cyclic AMP phosphodiesterase by rolipram triggers the dynamic redistribution of this specific isoform in living cells through a cyclic AMP independent process	scientific article published in October 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

Occupancy of the catalytic site of the PDE4A4 cyclic AMP phosphodiesterase by rolipram triggers the dynamic redistribution of this specific isoform in living cells through a cyclic AMP independent process (English)

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

Miles D. Houslay

8

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Europe PubMed Central

PubMed publication ID

3 December 2017

Robert D. Terry

1

object named as

Robert Terry

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Europe PubMed Central

PubMed publication ID

3 December 2017

author name string

York-Fong Cheung

2

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Europe PubMed Central

PubMed publication ID

3 December 2017

Morten Praestegaard

3

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Europe PubMed Central

PubMed publication ID

3 December 2017

George S Baillie

4

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Europe PubMed Central

PubMed publication ID

3 December 2017

Elaine Huston

5

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Europe PubMed Central

PubMed publication ID

3 December 2017

Irene Gall

6

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Europe PubMed Central

PubMed publication ID

3 December 2017

David R Adams

7

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Europe PubMed Central

PubMed publication ID

3 December 2017

publication date

1 October 2003

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Europe PubMed Central

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3 December 2017

number of pages

17

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Cellular Signalling

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3 December 2017

15

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3 December 2017

10

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3 December 2017

955-971

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PubMed publication ID

3 December 2017

Cyclic nucleotide research -- still expanding after half a century

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PDE4 cAMP-specific phosphodiesterases

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Cyclic nucleotide phosphodiesterases: relating structure and function

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AKAPs: from structure to function

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Tailoring cAMP-signalling responses through isoform multiplicity

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The next generation of PDE4 inhibitors

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Recent advances in PDE4 inhibitors as immunoregulators and anti-inflammatory drugs

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PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization

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Engineered deletion of the unique N-terminal domain of the cyclic AMP-specific phosphodiesterase RD1 prevents plasma membrane association and the attainment of enhanced thermostability without altering its sensitivity to inhibition by rolipram

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

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mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module

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TAPAS-1, a novel microdomain within the unique N-terminal region of the PDE4A1 cAMP-specific phosphodiesterase that allows rapid, Ca2+-triggered membrane association with selectivity for interaction with phosphatidic acid

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The green fluorescent protein

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Long PDE4 cAMP specific phosphodiesterases are activated by protein kinase A-mediated phosphorylation of a single serine residue in Upstream Conserved Region 1 (UCR1)

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Association with the SRC family tyrosyl kinase LYN triggers a conformational change in the catalytic region of human cAMP-specific phosphodiesterase HSPDE4A4B. Consequences for rolipram inhibition

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Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase

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Identifiers

10.1016/S0898-6568(03)00092-5

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

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