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October 22, 1999FEBS Letters

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

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Authors

MBMatthew BeardIpsen (United Kingdom)JOJonathan C. O’ConnellBristol-Myers Squibb (Germany)GBGraeme B. BolgerMemory Enhancement Center of America

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Implication

No immediate clinical implications for PDE4 targeting; leaves open isoform-specific roles in cAMP signaling.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Beard et al. (1999) studied this question.

synapsesocial.com/papers/6a8939147fec28afabc10d9f https://doi.org/10.1016/s0014-5793(99)01335-6

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Alternative Splicing of cAMP-specific Phosphodiesterase mRNA Transcripts1996 · 81 citations
2SH3 domains and drug design: Ligands, structure, and biological function1997 · 165 citations
3Identification, characterization and regional distribution in brain of RPDE-6 (RNPDE4A5), a novel splice variant of the PDE4A cyclic AMP phosphodiesterase family1995 · 115 citations
4Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene1997 · 185 citations
5Chimeric constructs show that the unique N-terminal domain of the cyclic AMP phosphodiesterase RD1 (RNPDE4A1A; rPDE-IVA1) can confer membrane association upon the normally cytosolic protein chloramphenicol acetyltransferase1995 · 71 citations