Cyclic nucleotide phosphodiesterases (PDE) and peptide motifs

Current Pharmaceutical Design

Volumn 16, Issue 9, 2010, Pages 1114-1125

  Keravis, Thérèse ^a   Lugnier, Claire ^a  

^a UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

cAMP cGMP signaling; PDEs; Peptide motif; Protein protein interaction; Regulatory domain

Indexed keywords

BETA ARRESTIN; CYCLIC AMP; CYCLIC GMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; DISRUPTED IN SCHIZOPHRENIA 1 PROTEIN; GENE PRODUCT; IMMUNOPHILIN; ISOENZYME; MESSENGER RNA; PHOSPHODIESTERASE 10; PHOSPHODIESTERASE 11; PHOSPHODIESTERASE 2; PHOSPHODIESTERASE 8; PHOSPHODIESTERASE 9; PHOSPHODIESTERASE I; PHOSPHODIESTERASE III; PHOSPHODIESTERASE IV; PHOSPHODIESTERASE V; PHOSPHODIESTERASE VI; PHOSPHODIESTERASE VII; PROTEIN 14 3 3; PROTEIN SH3; PROTEIN XAP2; RECEPTOR FOR ACTIVATED C KINASE 1; SILDENAFIL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; BINDING SITE; CRYSTALLOGRAPHY; DIMERIZATION; DRUG POTENCY; DRUG SELECTIVITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MACROMOLECULE; MAMMAL; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RECEPTOR UPREGULATION; REVIEW; RNA SPLICING; SIGNAL TRANSDUCTION;

3',5'-CYCLIC-AMP PHOSPHODIESTERASES; AMINO ACID MOTIFS; ANIMALS; CONSERVED SEQUENCE; DRUG DELIVERY SYSTEMS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; ISOENZYMES; MODELS, STRUCTURAL; PEPTIDES; PROTEIN INTERACTION DOMAINS AND MOTIFS;

EID: 77950287263     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161210790963760     Document Type: Review

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